|
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 ... |
431-1185 |
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: 1162.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAG-SVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDE 670
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 671 QKACWFILAAIYHLGAAGATKEAaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRQGPEESGl 750
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAA-SAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARS- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 751 gDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELCHNYTQDR 830
Cdd:cd01386 318 -SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQER 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 831 LQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPGASEDTLL 910
Cdd:cd01386 397 LQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 911 ERLFSYYGPQEGDkKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQKKiisnlflgra 990
Cdd:cd01386 477 ERLFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE---------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 991 gsatvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGEp 1070
Cdd:cd01386 546 ----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1071 rsassrrvsssseldlPSGDHCEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGR 1150
Cdd:cd01386 591 ----------------RSTSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGL 654
|
730 740 750
....*....|....*....|....*....|....*
gi 1093953565 1151 NYIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd01386 655 NSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
432-1185 |
1.85e-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: 1.85e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVFS-----VEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 585
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 586 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAEN---NVFGIVPLAKPEEKQKAAQQFSKLQAAMK 662
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSF 741
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSaEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 742 RqgPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSS--QHSLCSMMIVDTPGFQNPEQggsargASF 819
Cdd:cd00124 322 T--VEQ------------AEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV------NSF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 820 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLePPTDDSVAAVDQaSHQSLVRSLarTDEARgllwlleeea 899
Cdd:cd00124 382 EQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEG-KPLGILSLL--DEECL---------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 900 lVPGASEDTLLERLFSYYGPQEGDKKGQspllhSSKPHHFllGHSHGTNWVEYNVTGWLNYTKQNpatqnaprllqdsqk 979
Cdd:cd00124 448 -FPKGTDATFLEKLYSAHGSHPRFFSKK-----RKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 980 kiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqmklQVDALIDTIKKSKLHFVHCF 1059
Cdd:cd00124 505 ----------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLNSTQPHFVRCI 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1060 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1139
Cdd:cd00124 542 KPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1140 LAPHLTKKHGRNYIVVDERRAveellECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALL-----LLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
412-1197 |
1.57e-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: 1.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 412 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 491
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 492 TAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFS 569
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 570 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVFgivpLAKPEEKQK 649
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 650 A----AQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 725
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 726 fkhqhkggtLQRSTSFRQGPEESGLGdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 805
Cdd:smart00242 314 ---------TKRKIKTGGEVITKPLN-----VEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 806 QNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEpptdDSVAAVD--QASHQSLVRSLa 883
Cdd:smart00242 380 EIFEVN------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF----DNQDCIDliEKKPPGILSLL- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 884 rTDEARgllwlleeealVPGASEDTLLERLFSYYGPQEgdkkgqspllHSSKPH-----HFLLGHSHGTnwVEYNVTGWL 958
Cdd:smart00242 449 -DEECR-----------FPKGTDQTFLEKLNQHHKKHP----------HFSKPKkkgrtEFIIKHYAGD--VTYDVTGFL 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 959 nytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGMaavkkkslciQ 1036
Cdd:smart00242 505 ---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS----------Q 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1037 MKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRTQLRGSRLLDA 1116
Cdd:smart00242 551 FKEQLNELMDTLNSTNPHFIRCIKP--------------------NEEKKP---------GDFDSSLVLHQLRYLGVLEN 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1117 MRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDERRAVEELLECLDLEKSSCCMGLSRVFFRAGTLARLEEQR 1196
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 1093953565 1197 D 1197
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
393-1917 |
9.14e-110 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 385.97 E-value: 9.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 393 KLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMH 472
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 473 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKwQALYT--L 550
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 551 LEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL--- 627
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 628 ---NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQAAMKVLGISPDEQKACWFILAAIYHLG--AAGATKEaaeaGRKQFA 702
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGniEFKEDRN----GAAIFS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 703 RHEWAQKAAYLLGCSLEELSSAIFKHQHKGG--TLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLV 780
Cdd:COG5022 350 DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ----------------ALAIRDSLAKALYSNLFDWIV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 781 SLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFD 857
Cdd:COG5022 414 DRINKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfIDYF 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 858 DLEPPTDdsvaavdqashqsLVRSLART-------DEARgllwlleeealVPGASEDTLLERLFSYYgPQEGDKKGQSPL 930
Cdd:COG5022 488 DNQPCID-------------LIEKKNPLgilslldEECV-----------MPHATDESFTSKLAQRL-NKNSNPKFKKSR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 931 LHSSKphhFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLA 1010
Cdd:COG5022 543 FRDNK---FVVKHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGR 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1011 LRRATSMRKTfttgmaavkkkslciqmklQVDALIDTIKKSKLHFVHCFLP--VAEGWageprsassrrvsssseldlps 1088
Cdd:COG5022 604 FPTLGSRFKE-------------------SLNSLMSTLNSTQPHYIRCIKPneEKSPW---------------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1089 gdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDERRAVEELLECL 1168
Cdd:COG5022 643 ---------TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEEL 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1169 DLEKSSCCMGLSRVFFRAGTLARLEEQRDEQTSRNLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWP 1247
Cdd:COG5022 713 VIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYEL 791
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1248 WWKLFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEK----AEKERNELRLNSDRLESRISEltSELTDERNTGESASQL 1323
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETI 869
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1324 LDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKK 1399
Cdd:COG5022 870 YLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIE 949
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1400 RLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsEL 1479
Cdd:COG5022 950 YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EV 1025
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1480 SQAHEEAQREKLQREKLQREKDMLLAEAFSLK--QQLEEKDmdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLR 1557
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLKGLLLLenNQLQARY--------KALKLRRENSLL---DDKQLYQLESTENLLK 1094
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1558 DLEAK---VKDQEEELDEQAGTIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1632
Cdd:COG5022 1095 TINVKdleVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPF 1174
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1633 D--KQKVLREKRELEGKLATLSDQVN--RRDFESEKRLRKDL----KRTKALLADAQLML-----------DHLKNSAPS 1693
Cdd:COG5022 1175 AalSEKRLYQSALYDEKSKLSSSEVNdlKNELIALFSKIFSGwprgDKLKKLISEGWVPTeystslkgfnnLNKKFDTPA 1254
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIakAKTALEEQLSRLQREKNEiqnRLEEDQEDMNELMKK 1773
Cdd:COG5022 1255 SMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVG--LFNALRTKASSLRWKSAT---EVNYNSEELDDWCRE 1329
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 HKAAVAQASRdlaqINDLQAQ--LEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRElETRLEFERTQVK 1851
Cdd:COG5022 1330 FEISDVDEEL----EELIQAVkvLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPK-EILKKIEALLIK 1404
|
1530 1540 1550 1560 1570 1580
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1852 RLESLASRLKENMEKLTEErdqriaaENREKEQNKRLQRQLRDTKEEMGELarkEAEASRKKHELE 1917
Cdd:COG5022 1405 QELQLSLEGKDETEVHLSE-------IFSEEKSLISLDRNSIYKEEVLSSL---SALLTKEKIALL 1460
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
420-1185 |
1.34e-109 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 365.83 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 420 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 500 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGI-SGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDF 576
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 577 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL---------NHLAENNVFGIvplakpeek 647
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 648 qKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKqFARHEWAQKAAYLLGCSLEELSSAIFK 727
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV-PDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 728 HQHKGGTLQRSTSfrQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQ 806
Cdd:pfam00063 310 RRIKTGRETVSKP--QNVEQ------------ANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLDIYGFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 807 NPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptDDSVAAVDQASHQSL-VRSLarT 885
Cdd:pfam00063 376 IFEKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDF----GDNQPCIDLIEKKPLgILSL--L 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 DEArgllwlleeeALVPGASEDTLLERLFSYYgpqegdkkGQSPLLHSSKPH---HFLLGHSHGTnwVEYNVTGWLNYTK 962
Cdd:pfam00063 444 DEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEYNVEGFLEKNK 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 963 qNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkkslciQMKLQVD 1042
Cdd:pfam00063 504 -DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS----------QFKESLG 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1043 ALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQ 1122
Cdd:pfam00063 566 ELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNGVLEGIRIRRA 616
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1123 GYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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, ... |
432-1185 |
1.71e-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: 1.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKW-----QALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 583
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFgIVPLAKPEEKQKAAQQFSKLQAAMKV 663
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 664 LGISPDEQKACWFILAAIYHLGAAGATKEaaeaGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRS 738
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR----RREEQAEldgTEEADKAAHLLGVNSSDLLKALLKPRIKVGRewVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 739 TSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQ----Npeqggsa 814
Cdd:cd01377 316 QNKEQ----------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 815 rgaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAF----DDLEPPTDdsvaavdqashqsLVRS-----LART 885
Cdd:cd01377 373 ---SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-------------LIEKpnmgiLSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 DEargllwlleeEALVPGASEDTLLERLFSyygpQEGDKKGQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLnyTK-Q 963
Cdd:cd01377 437 DE----------ECVFPKATDKTFVEKLYS----NHLGKSKNFKKPKPKKSEaHFILKHYAGD--VEYNIDGWL--EKnK 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 964 NPATQNAPRLLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDA 1043
Cdd:cd01377 499 DPLNENVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NK 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1044 LIDTIKKSKLHFVHCFLPVAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQG 1123
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKG 605
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1124 YPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
8.63e-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: 8.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGI-SGNKVFSVE---KWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 584
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPgelERQLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF--GIVPLAkpeeKQKAAQQFSKLQAAMK 662
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRSts 740
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKE-RNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRdyVQKA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 741 frQGPEESGLGdgtgpklsalecLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSF 819
Cdd:cd14920 314 --QTKEQADFA------------VEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN------SF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 820 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlleeEA 899
Cdd:cd14920 374 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGV--LALLDE----------EC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 900 LVPGASEDTLLERLFSYYGPQEGDKKGQSPllhsSKPHHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPRLLQDSQK 979
Cdd:cd14920 442 WFPKATDKTFVEKLVQEQGSHSKFQKPRQL----KDKADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLHQSSD 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 980 KIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqmklqvDALIDTIKKSKLHFVHCF 1059
Cdd:cd14920 515 RFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATLRNTNPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1060 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1139
Cdd:cd14920 582 IPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1140 LAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
7.46e-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: 7.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAG-----------ISGNKVFSV-EKWQALYT---LLEAFGNSPTIINGNATRFSQILSLD 575
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAskpkgsgavphPAVNPAVLIgELEQQLLQanpILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 576 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVF---GIVPLAKPEEkqkaAQ 652
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 653 QFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKG 732
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSM-KFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 733 GtlQRSTSFRQGPEESGLGdgtgpklsalecLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQG 811
Cdd:cd14911 315 G--RDFVTKAQTKEQVEFA------------VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFEIFELN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 812 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFD----DLEPPTDdsvaavdqashqslvrslaRTDE 887
Cdd:cd14911 381 ------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-------------------LIDK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 888 ARGLLWLLEEEALVPGASEDTLLERLFSYYG--PQ--EGDKKGQSpllhsskphHFLLGHSHGTnwVEYNVTGWLnYTKQ 963
Cdd:cd14911 436 PGGIMALLDEECWFPKATDKTFVDKLVSAHSmhPKfmKTDFRGVA---------DFAIVHYAGR--VDYSAAKWL-MKNM 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 964 NPATQNAPRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQMKLQVDA 1043
Cdd:cd14911 504 DPLNENIVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQLAK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1044 LIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQG 1123
Cdd:cd14911 567 LMDTLRNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICRQG 617
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1124 YPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14911 618 FPNRIPFQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
431-1185 |
2.92e-84 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 292.31 E-value: 2.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIA----GISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 584
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNV--FGIVPLAkpeeKQKAAQQFSKLQAAMK 662
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGG--TLQRSTS 740
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGrdVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 741 FRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSF 819
Cdd:cd14921 316 KEQ----------------ADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN------SF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 820 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQashQSLVRSLARTDEARGLLWLLEEEA 899
Cdd:cd14921 374 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDF---------GLDL---QPCIELIERPNNPPGVLALLDEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 900 LVPGASEDTLLERLFSyygPQEGDKKGQSPLLHSSKPHHFLLghsHGTNWVEYNVTGWLNyTKQNPATQNAPRLLQDSQK 979
Cdd:cd14921 442 WFPKATDKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASSD 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 980 KIISNLFLGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQMKLQVDALIDTIKKSKLHFVHCF 1059
Cdd:cd14921 515 KFVADLWKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1060 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1139
Cdd:cd14921 582 IPNHEKRSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1140 LAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
3.98e-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: 3.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGIS------GNKVFS---VEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQA 579
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqSSIALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 580 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQA 659
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 737
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE-RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRdyVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 STSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsarg 816
Cdd:cd14932 317 AQTQEQ----------------AEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlle 896
Cdd:cd14932 376 -SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGI--LALLDE--------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 897 eEALVPGASEDTLLERLfsyygpqeGDKKGQSPLLHSSKP----HHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPR 972
Cdd:cd14932 444 -ECWFPKATDKSFVEKV--------VQEQGNNPKFQKPKKlkddADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVAT 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 973 LLQDSQKKIISNLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQMKLQVDALIDTIKKSK 1052
Cdd:cd14932 512 LLNQSTDKFVSELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTN 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1053 LHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSE 1132
Cdd:cd14932 578 PNFVRCIIPNHEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1133 FRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
9.93e-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: 9.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKvfsvEKWQALY-------TLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 583
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALEdqimqanPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDGTLRTELHLN------HLAENNVFGIvplakpeEKQKAAQQFSKL 657
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 658 QAAMKVLGISPDEQKACWFILAAIYHLG----AAGATKEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKHQHKGG 733
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGnmkfKQKPREEQLEADGT-----ENADKAAFLMGINSSELVKGLIHPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 734 T--LQRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 811
Cdd:cd14929 304 NeyVTRSQNIEQVTYAVG----------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 812 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE-LAFD---DLEpptddsvAAVDqashqsLVrslartDE 887
Cdd:cd14929 368 ------SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDwVSIDfglDLQ-------ACID------LI------EK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 888 ARGLLWLLEEEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKPH------HFLLGHSHGTnwVEYNVTGWLNYT 961
Cdd:cd14929 423 PMGIFSILEEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKN 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 962 KqNPATQNAPRLLQDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqmklqv 1041
Cdd:cd14929 494 K-DLLNETVVAVFQKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL-------- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1042 DALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYR 1121
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICR 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1122 QGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
1.96e-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: 1.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASI 587
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 588 QTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQAAMKVLGIS 667
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 668 PDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRSTSFRQgp 745
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRdyVQKAQTKEQ-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 746 eesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSFEELCH 824
Cdd:cd14919 316 --------------ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQLCI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 825 NYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlleeEALVPGA 904
Cdd:cd14919 376 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGI--LALLDE----------ECWFPKA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 905 SEDTLLERLFSYYGPQegdKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPRLLQDSQKKIISN 984
Cdd:cd14919 444 TDKSFVEKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 985 LFlgRAGSATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqmklQVDALIDTIKKSKLHFVHCFLPVAE 1064
Cdd:cd14919 517 LW--KDVDRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1065 GWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHL 1144
Cdd:cd14919 584 KKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1093953565 1145 TKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14919 635 IPKG-----FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
431-1185 |
1.28e-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: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYT------------LLEAFGNSPTIINGNATRFSQILSLDFDQ 578
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVA--SSHKTKKDQNSLALSHgelekqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 579 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQ 658
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 659 AAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQ 736
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKE-RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRdyVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 737 RSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsar 815
Cdd:cd15896 316 KAQTQEQ----------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwll 895
Cdd:cd15896 376 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGI--LALLDE-------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 896 eeEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKP----HHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAP 971
Cdd:cd15896 444 --ECWFPKATDKSFVEKVLQ--------EQGTHPKFFKPKKlkdeADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 972 RLLQDSQKKIISNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqmklQVDALIDTIKK 1050
Cdd:cd15896 511 TLLNQSTDKFVSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRN 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1051 SKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1130
Cdd:cd15896 575 TNPNFVRCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1131 SEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd15896 626 QEFRQRYEILTPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
431-1185 |
3.20e-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: 3.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNkvfSVEKWQALYTL---------------LEAFGNSPTIINGNATRFSQILSLD 575
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDG---PGKKAQFLATKtggtledqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 576 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLN------HLAENNVFGIVPLAKPEEkqk 649
Cdd:cd14927 158 FGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 650 aaqqFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATK----EAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAI 725
Cdd:cd14927 235 ----LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQkqreEQAEADGT-----ESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 726 FKHQHKGGtlQRSTSFRQGPEESGLGDGtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 805
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVYAVG------------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 806 QNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRT 885
Cdd:cd14927 372 EIFEFN------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGL---DLQACID------------LI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 DEARGLLWLLEEEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKPH-------HFLLGHSHGTnwVEYNVTGWL 958
Cdd:cd14927 431 EKPLGILSILEEECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPDkkrkyeaHFEVVHYAGV--VPYNIVGWL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 959 NYTKqNPATQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqmk 1038
Cdd:cd14927 502 DKNK-DPLNETVVAIFQKSQNKLLATLYENYVGSD-----STEDPKSGVKEKRKKAAS----FQT-VSQLHKENL----- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1039 lqvDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMR 1118
Cdd:cd14927 566 ---NKLMTNLRATQPHFVRCIIP--------------------NETKTPG---------VMDPFLVLHQLRCNGVLEGIR 613
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1119 MYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
2.59e-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: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIaGISGNKVFSVEKW-----QALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 583
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV-GASKKTDEAAKSKgsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNhlaeNNVFGIVPLAKPE---EKQKAAQQFSKLQAA 660
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 661 MKVLGISPDEQKACWFILAAIYHLGaagaTKEAAEAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQHKGGTlqr 737
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMG----GMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGN--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 sTSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGsarga 817
Cdd:cd14909 309 -EFVTQGRNVQQVTNSIG----------ALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 818 sFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 897
Cdd:cd14909 373 -FEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGM---DLLACID------------LIEKPMGILSILEE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 898 EALVPGASEDTLLERLFSyygpqegDKKGQSPLLHSSKP-------HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNA 970
Cdd:cd14909 437 ESMFPKATDQTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTV 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 971 PRLLQDSQKKIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQMKLQVDALIDTIKK 1050
Cdd:cd14909 507 VDQFKKSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRS 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1051 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1130
Cdd:cd14909 567 TQPHFVRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMY 617
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1131 SEFRRRFDVLAPHLTKKHgrnyivVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
431-1185 |
1.80e-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: 1.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIA---------GISGNkvFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 581
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVAsspkgrkepGVPGE--LERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQkaaQQFSKLQAAM 661
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 662 KVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRST 739
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRE-RNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRdyVQKAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 SFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaS 818
Cdd:cd14930 314 TKEQ----------------ADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 819 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQashQSLVRSLARTDEARGLLWLLEEE 898
Cdd:cd14930 372 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDF---------GLDL---QPCIDLIERPANPPGLLALLDEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 899 ALVPGASEDTLLERLFSYYGPQegdKKGQSPLLHSSKPHHFLLghsHGTNWVEYNVTGWLnYTKQNPATQNAPRLLQDSQ 978
Cdd:cd14930 440 CWFPKATDKSFVEKVAQEQGGH---PKFQRPRHLRDQADFSVL---HYAGKVDYKANEWL-MKNMDPLNDNVAALLHQST 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 979 KKIISNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1056
Cdd:cd14930 513 DRLTAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTNPSFV 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1057 HCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1136
Cdd:cd14930 576 RCIVPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1137 FDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14930 627 YEILTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
432-1185 |
1.53e-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: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 583
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA---A 660
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 661 MKVLGISPDEQKACWFILAAIYHLGaagaTKEAAEAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--L 735
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYG----NMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGNeyV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 736 QRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsar 815
Cdd:cd14913 314 TKGQTVDQ----------------VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLL 895
Cdd:cd14913 374 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGIFSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 896 EEEALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLL 974
Cdd:cd14913 437 EEECMFPKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLY 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 975 QDSQKKIISNLFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqmklqvDALIDTIKKSKL 1053
Cdd:cd14913 512 QKSSNRLLAHLYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1054 HFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEF 1133
Cdd:cd14913 570 HFVRCIIP--------------------NETKTPGA---------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1134 RRRFDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14913 621 KQRYRVLNASAIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
432-1142 |
3.16e-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: 3.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGISGnkvfSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 590 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGIVPLakpeekqKAAQQFSKLQAAMKV 663
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGV-------DDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 664 LGISPDEQKACWFILAAIYHLG---------AAGATKEAAEAgrkqfarhewAQKAAYLLGCSLEELSSAIFKHQHK--G 732
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGnisfqvidnENHVEVVADEA----------VSTAASLLGCNANDLMLALSTRKIQagG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 733 GTLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQH-SLCSMMIVDTPGFQnpeqg 811
Cdd:cd01383 298 DKIVKKLTLQQ----------------AIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 812 gSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEpptdDSVAAVDQASHQSL-VRSLarTDEarg 890
Cdd:cd01383 357 -SFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLDLIEKKPLgLISL--LDE--- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 891 llwlleeEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGWLNytkqnpatQNA 970
Cdd:cd01383 427 -------ESNFPKATDLTFANKLKQHLKSNSCFKGERGGA--------FTIRHYAGE--VTYDTSGFLE--------KNR 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 971 PRLLQDsqkkiISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQMKLQVDALIDTIKK 1050
Cdd:cd01383 482 DLLHSD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLEN 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1051 SKLHFVHCFLPVAEGWAGEprsassrrvsssSELDLpsgdhceagLLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVF 1130
Cdd:cd01383 548 TTPHFIRCIKPNNKQLPGV------------FDQDL---------VLQ--------QLRCCGVLEVVRISRSGYPTRMTH 598
|
730
....*....|..
gi 1093953565 1131 SEFRRRFDVLAP 1142
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 ... |
432-1185 |
1.75e-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: 1.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGIS---------GNKVFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 582
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGdrskkdqtpGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 583 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA--- 659
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEwAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 737
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEE-ADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 STSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 817
Cdd:cd14917 316 GQNVQQVIYATG----------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 818 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 897
Cdd:cd14917 374 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGM---DLQACID------------LIEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 898 EALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 976
Cdd:cd14917 439 ECMFPKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGLYQK 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 977 SQKKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1056
Cdd:cd14917 514 SSLKLLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHPHFV 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1057 HCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1136
Cdd:cd14917 573 RCIIP--------------------NETKSPG---------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 623
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1137 FDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14917 624 YRILNPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
431-1143 |
5.41e-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: 5.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIagisGNKVFSVEKwQAL--YTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAV----TNNHSWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGT--LRTELHL---NHLAENNVFGIVPLAKPEEKQKaaqqFSKLQAAMKV 663
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHSkeLKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FDHLRLAMNV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 664 LGISPDEQKACWFILAAIYHLGaaGATKEAAEAGRKQFAR--HEWAQKAAYLLGCSLEELSSA-IFKHQHKGGTLqrsTS 740
Cdd:cd14883 232 LGIPEEMQEGIFSVLSAILHLG--NLTFEDIDGETGALTVedKEILKIVAKLLGVDPDKLKKAlTIRQINVRGNV---TE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 741 FRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFE 820
Cdd:cd14883 307 IPLKVQE------------ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN------SFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 821 ELCHNYTQDRLQRLFHERTFVQELERYKEENIELA---FDD-------LEPPTDDSVAAVDQASHqslvrslartdearg 890
Cdd:cd14883 369 QLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDnqecldlIEKPPLGILKLLDEECR--------------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 891 llwlleeealVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSkphhFLLGHSHGTnwVEYNVTGWLNytkQNPATQ-- 968
Cdd:cd14883 434 ----------FPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTE----FGVKHYAGE--VTYTVQGFLD---KNKDTQqd 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 969 NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQMKLQVDALIDT 1047
Cdd:cd14883 495 DLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDV 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1048 IKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDH 1127
Cdd:cd14883 558 LSATQPWYVRCIKP--------------------NSLKEPN---------VFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
730
....*....|....*.
gi 1093953565 1128 MVFSEFRRRFDVLAPH 1143
Cdd:cd14883 609 LTFKEFVDRYLCLDPR 624
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
431-1185 |
1.12e-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: 239.93 E-value: 1.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGIS-----GNKVFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 585
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 586 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaennvfgiVPlaKPEEKQKAAQQFSKLQ------- 658
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL-----------VP--NPKEYHWVSQGVTVVDnmddgee 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 659 -----AAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGG 733
Cdd:cd14934 227 lqitdVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREE-QAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 734 T--LQRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 811
Cdd:cd14934 306 NefVQKGQNMEQCNNSIG----------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 812 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDQashqslvrslarTDEARGL 891
Cdd:cd14934 370 ------SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGL---DLQACIDL------------LEKPMGI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 892 LWLLEEEALVPGASEDTLLERLF--------SYYGPQEGDKKGQSPllhsskphHFLLGHSHGTnwVEYNVTGWLNYTKq 963
Cdd:cd14934 429 FSILEEQCVFPKATDATFKAALYdnhlgkssNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 964 NPATQNAPRLLQDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQMKLQVDA 1043
Cdd:cd14934 498 DPLNETVVGLFQKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNK 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1044 LIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQG 1123
Cdd:cd14934 552 LMTTLHSTAPHFVRCIVP---------------------------NEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKG 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1124 YPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14934 603 FPNRLQYPEFKQRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
433-1147 |
1.39e-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: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 433 VLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 590 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQAAMKV 663
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 664 LGISPDEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKhqhkggtlqRSTSF 741
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCK---------RVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 742 RQGPEESGLGdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQnpeqggSARGASFEE 821
Cdd:cd01384 306 PDGIITKPLD-----PDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SFKTNSFEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 822 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddlepptddsVAAVDQASHQSLVRS-----LARTDEArgllwlle 896
Cdd:cd01384 375 FCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSY----------IEFVDNQDVLDLIEKkpggiIALLDEA-------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 897 eeALVPGASEDTLLERLFSYYgpqEGDKKGQSPLLhssKPHHFLLGHSHGTnwVEYNVTGWLNYTKQN--PATQNaprLL 974
Cdd:cd01384 437 --CMFPRSTHETFAQKLYQTL---KDHKRFSKPKL---SRTDFTIDHYAGD--VTYQTDLFLDKNKDYvvAEHQA---LL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 975 QDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQMKLQVDALIDTIKKSKLH 1054
Cdd:cd01384 504 NASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQLQELMETLNTTEPH 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1055 FVHCFLPVAEgwageprsassrrvsssseldLPSGDHCEAGLLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1134
Cdd:cd01384 554 YIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
730
....*....|...
gi 1093953565 1135 RRFDVLAPHLTKK 1147
Cdd:cd01384 605 DRFGLLAPEVLKG 617
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
432-1185 |
6.79e-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: 6.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGI---------SGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 582
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIgdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 583 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA--- 659
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 737
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 STSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 817
Cdd:cd14916 317 GQSVQQ----------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 818 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 897
Cdd:cd14916 375 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGM---DLQACID------------LIEKPMGIMSILEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 898 EALVPGASEDTLLERLF-SYYGPQEGDKKGQSplLHSSKPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 976
Cdd:cd14916 440 ECMFPKASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQK 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 977 SQKKIISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1056
Cdd:cd14916 515 SSLKLMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHPHFV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1057 HCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1136
Cdd:cd14916 575 RCIIP---------------------------NERKAPGV--MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 625
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1137 FDVLAPhLTKKHGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
432-1140 |
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: 231.50 E-value: 1.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAgISGNKVFSVEKWQALYT----------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 581
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTledqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA-- 659
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 -AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrS 738
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG----N 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 739 TSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaS 818
Cdd:cd14923 312 EYVTKGQNVQQVTNSVG----------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 819 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEEE 898
Cdd:cd14923 376 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSILEEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 899 ALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQ 978
Cdd:cd14923 441 CMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEA-HFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 979 KKIISNLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFVHC 1058
Cdd:cd14923 517 LKLLSFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1059 FLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1138
Cdd:cd14923 578 LIP--------------------NETKTPG---------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 628
|
..
gi 1093953565 1139 VL 1140
Cdd:cd14923 629 IL 630
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
432-1140 |
3.19e-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: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAgISGNKV---FSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAG 580
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIA-VTGEKKkeeAASGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA- 659
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 --AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--L 735
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNeyV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 736 QRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsar 815
Cdd:cd14915 316 TKGQTVQQVYNSVG----------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLL 895
Cdd:cd14915 376 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSIL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 896 EEEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQ 975
Cdd:cd14915 439 EEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA-HFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 976 DSQKKIISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHF 1055
Cdd:cd14915 515 KSGMKTLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1056 VHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1135
Cdd:cd14915 575 VRCLIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
....*
gi 1093953565 1136 RFDVL 1140
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 ... |
432-1185 |
8.09e-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: 8.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT----------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 581
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTledqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELhlnhLAENNVFGIVPLAKPEEKQKAAQQFSKLQA-- 659
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 -AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQ 736
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 737 RSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 816
Cdd:cd14910 317 KGQTVQQ----------------VYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLE 896
Cdd:cd14910 376 -SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSILE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 897 EEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKP------HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNA 970
Cdd:cd14910 440 EECMFPKATDTSFKNKLYEQH-------LGKSNNFQKPKPakgkveAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 971 PRLLQDSQKKIISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKK 1050
Cdd:cd14910 510 VGLYQKSSMKTLALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1051 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1130
Cdd:cd14910 570 THPHFVRCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILY 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1131 SEFRRRFDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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, ... |
431-1061 |
1.53e-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: 227.43 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYlatIAGISGNKVFSVE--KWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASAS 586
Cdd:cd01378 81 ESGAGKTEASKRIMQY---IAAVSGGSESEVErvKDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 587 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVF---GIvplakpeekqKAAQQFSKL 657
Cdd:cd01378 158 ITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFdvdGI----------DDAADFKEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 658 QAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQR 737
Cdd:cd01378 228 LNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAED--EEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 ST-SFRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsar 815
Cdd:cd01378 306 SVyEVPLNVEQ------------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKN---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELA----FD-----DL-EPPTDDSVAAVDQAShqslvrslart 885
Cdd:cd01378 370 --SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNnkiicDLiEEKPPGIFAILDDAC----------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 deargllwlleeeALVPGASEDTLLERLfsyygpqegdkkgqspLLHSSKPHHFLLGHSHGTNW------------VEYN 953
Cdd:cd01378 437 -------------LTAGDATDQTFLQKL----------------NQLFSNHPHFECPSGHFELRrgefrikhyagdVTYN 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 954 VTGwlnYTKQNPAT--QNAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkk 1031
Cdd:cd01378 488 VEG---FLDKNKDLlfKDLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT------ 536
|
650 660 670
....*....|....*....|....*....|
gi 1093953565 1032 slciQMKLQVDALIDTIKKSKLHFVHCFLP 1061
Cdd:cd01378 537 ----KFKNSANALVETLMKKQPSYIRCIKP 562
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
433-1185 |
3.90e-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: 226.54 E-value: 3.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 433 VLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSS 512
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 513 GSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 584
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELhlnhLAENNVFGIVPLAKPEEKQKAAQQFSKLQA---AM 661
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 662 KVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrSTSF 741
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVG----NEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 742 RQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEE 821
Cdd:cd14918 314 TKGQTVQQVYNAVG----------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 822 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEEEALV 901
Cdd:cd14918 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPLGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 902 PGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKK 980
Cdd:cd14918 443 PKATDTSFKNKLYDQHLGKSANF--QKPKVVKGKAEaHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSAMK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 981 IISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqmklQVDALIDTIKKSKLHFVHCFL 1060
Cdd:cd14918 518 TLASLFSTYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1061 PvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1140
Cdd:cd14918 577 P--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 627
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1093953565 1141 APHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
432-1185 |
7.62e-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: 7.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 581
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAvtgekkkeEITSGKMQGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGiVPLAKPEEKQKAA----QQFSKL 657
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYD-YPFVSQGEISVASiddqEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 658 QAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqr 737
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVG---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 738 STSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 817
Cdd:cd14912 312 NEYVTKGQTVEQVTNAVG----------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 818 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEE 897
Cdd:cd14912 376 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGIFSILEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 898 EALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 976
Cdd:cd14912 441 ECMFPKATDTSFKNKLYEQHLGKSANF--QKPKVVKGKAEaHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGLYQK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 977 SQKKIISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1056
Cdd:cd14912 516 SAMKTLAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHPHFV 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1057 HCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1136
Cdd:cd14912 578 RCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1137 FDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14912 629 YKVLNASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
431-858 |
8.97e-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: 8.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 505
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 506 IILLGSSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYT------------------LLEAFGNSPTIINGNATR 567
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARIT--SGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 568 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaENNVFGIVPLAK--PE 645
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 646 EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 725
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKLAAELLGVNEDALEKAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 726 FKHQH--KGGTLQRstsfrqgPEESGLgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTP 803
Cdd:cd14890 315 LTRQLfvGGKTIVQ-------PQNVEQ---------ARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIY 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 804 GFQNPEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDD 858
Cdd:cd14890 379 GFEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFND 430
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
431-1185 |
7.84e-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: 7.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGisgnKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNH------LAENNVFGIvplakpeEKQKAAQQFSKLQAAMK 662
Cdd:cd01381 156 QYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEqkaCWFI---LAAIYHLGAAG------ATKEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQ--HK 731
Cdd:cd01381 229 VLMFTDEE---IWDIfklLAAILHLGNIKfeatvvDNLDASE-----VRDPPNLERAAKLLEVPKQDLVDALTTRTifTR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 732 GGTLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAL---KSSQHSLCSMMIVDTPGFQNP 808
Cdd:cd01381 301 GETVVSPLSAEQ----------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 809 EQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsVAAVDQASHQSLVrslart 885
Cdd:cd01381 365 EVN------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMNIMSLI------ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 DEargllwlleeEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHHFLlghshGTnwVEYNVTGWLNytKQNP 965
Cdd:cd01381 431 DE----------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KNRD 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 966 A-TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQMKLQVDAL 1044
Cdd:cd01381 492 TfSADLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1045 IDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRTQLRGSRLLDAMRMYRQGY 1124
Cdd:cd01381 542 MKTLSACQPFFVRCIKP--------------------NEYKKP---------MLFDRELCVRQLRYSGMMETIRIRKAGY 592
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1125 PDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
432-864 |
1.90e-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: 1.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLaTIAGISGNKVFSvEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTML 591
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 592 LEKLRVARRPASEATFNVFYYLLA-------CGDGTLRTELHLNHLAENNvfgiVPLAKPEEKQKAAQQFSKLQAAMKVL 664
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQNDG----LTVQDIVNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 665 GISPDEQKACWFILAAIYHLGA---AGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ--HKGGTLQRST 739
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDiefTEVESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSvvTRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 SFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNPEQGgsarg 816
Cdd:cd01379 316 TVEE----------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFENFQKN----- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIEL---AFDDLEPPTD 864
Cdd:cd01379 375 -SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
431-1185 |
8.80e-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: 8.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILL 509
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 510 GSSGSGKTTSCQHLVQYLATIAGisGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 590 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAennVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPD 669
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 670 EQKACWFILAAIYHLGAAGATKEAAEAGRKQFAR-HEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRqgpees 748
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPgDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 749 glgdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQ 828
Cdd:cd14903 310 --------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCINYAN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 829 DRLQRLFHERTFVQELERYKEENIELAFddlepptddsvaaVDQASHQSLvrsLARTDEARGLLWLLEEEALVPGASEDT 908
Cdd:cd14903 376 EKLQQKFTQDVFKTVQIEYEEEGIRWAH-------------IDFADNQDV---LAVIEDRLGIISLLNDEVMRPKGNEES 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 909 LLERLFSYYgpqeGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKQNpatqnaprLLQD-------SQKKI 981
Cdd:cd14903 440 FVSKLSSIH----KDEQDVIEFPRTSRT-QFTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSSKPF 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 982 ISNLFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQMKLQVDALIDTIKKSKLHFVHCFLP 1061
Cdd:cd14903 505 LRMLFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRCIKP 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1062 VAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1141
Cdd:cd14903 569 NSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1093953565 1142 PhltkKHGRNYIVVDER-RAVEELLECLDLEKSSccMGLSRVFFR 1185
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 ... |
432-858 |
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 1093953565 432 SVLHTLRQRYG-ASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVfSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISP 668
Cdd:cd01380 160 TYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 669 DEQKACWFILAAIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHK--GGTLQRSTSFRQgpe 746
Cdd:cd01380 239 EEQMEIFRILAAILHLGNV-EIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVtrSEVIVKPLTLQQ--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 747 esglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEQGgsargaSFEELCH 824
Cdd:cd01380 315 -------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN------SFEQFCI 375
|
410 420 430
....*....|....*....|....*....|....
gi 1093953565 825 NYTQDRLQRLFHERTFVQELERYKEENIELAFDD 858
Cdd:cd01380 376 NYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
432-1183 |
7.70e-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: 213.50 E-value: 7.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 501
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 502 QDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKW----QALYT--LLEAFGNSPTIINGNATRFSQILSLD 575
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 576 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFS 655
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 656 KLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTL 735
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 736 QRSTSFrqgpeesglgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRALK--SSQHSLCSMMIVDTPGFQNPEQGgs 813
Cdd:cd14901 322 YITMPL--------------SVEQALLTRDVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFEIFATN-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 814 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddLEPPTDDSVAAVDQASHQSLVRSLartDEargllw 893
Cdd:cd14901 386 ----SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF--VEYPNNDACVAMFEARPTGLFSLL---DE------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 894 lleeEALVPGASEDTLLErlfSYYgpqegDKKGQSPLLHSSKPHH----FLLGHSHGTnwVEYNVTGWLNYTKQNPATqN 969
Cdd:cd14901 451 ----QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKLQQgkrqFVIHHYAGA--VCYATDGFCDKNKDHVHS-E 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 970 APRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQMKLQVDALIDTIK 1049
Cdd:cd14901 516 ALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLSSLLEVLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1050 KSKLHFVHCFLPVaegwageprsassrrvsssselDLPSGDhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMV 1129
Cdd:cd14901 549 ATEPHFIRCIKPN----------------------DVLSPS-------EFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1130 FSEFRRRFDVLAPHLTKKHGRNYIVVDERRAVEELLECLDLEKSSCCMGLSRVF 1183
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
432-987 |
3.33e-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: 3.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLS--PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLAcgdGTLRTELHLNHLAENNVFGIVPLA--------KPEEKQKAAQQFSKLQAAMK 662
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFA---GMSRDRLLYYFLEDPDCHRILRDDnrnrpvfnDSEELEYYRQMFHDLTNIMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEQKACWFILAAIYHLgAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIF--KHQHKGGTLQRSTS 740
Cdd:cd14897 237 LIGFSEEDISVIFTILAAILHL-TNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALIsnVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 741 FRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQ-----HSLCSMMIVDTPGFQNPEQGGsar 815
Cdd:cd14897 316 LRQ----------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFENFKINS--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAfdDLEPPTDDSVAAVDQASHQSLvrsLARTDEargllwll 895
Cdd:cd14897 377 ---FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVLELFFKKPLGI---LPLLDE-------- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 896 eeEALVPGASEDTLLERLFSYYGPqegdkkgqSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNpATQNAPRLLQ 975
Cdd:cd14897 441 --ESTFPQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDN-LSSDIVGCLL 509
|
570
....*....|..
gi 1093953565 976 DSQKKIISNLFL 987
Cdd:cd14897 510 NSNNEFISDLFT 521
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
431-1141 |
9.24e-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: 210.02 E-value: 9.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGIS-GNKVFSVEKwqaLYTLLEAFGNSPTIINGNATRFSQILSLDFdQAGQVASASIQT 589
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQtEDRLRQPED---VLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 590 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAEN----NVFGIVPLAKPEEkqkaAQQFSKLQAAMKVLG 665
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 666 ISPDEQKACWFILAAIYHLGA---AGATKEAAEAGrkqfARHEWA--QKAAYLLGCSLEELSSAIFKhqhkggtlqRSTS 740
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNicfSSSERESQEVA----AVSSWAeiHTAARLLQVPPERLEGAVTH---------RVTE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 741 FRQGPEESGLgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRAL--KSSQHSLCSMMIVDTPGFQnpeqggSARGAS 818
Cdd:cd14896 299 TPYGRVSRPL-----PVEGAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALRVNG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 819 FEELCHNYTQDRLQRLFHERTFVQELERYKEEniELAFDDLEPPTDDSVAAVDQASHQSLVRSLartdeargllwllEEE 898
Cdd:cd14896 368 LEQLCINLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLDLLVDQPHSLLSIL-------------DDQ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 899 ALVPGASEDTLLERLFSYYGPQEGDKKGQSPLlhsskPhHFLLGHSHGTnwVEYNVTGWLNYTKQ--NPATQNaprLLQD 976
Cdd:cd14896 433 TWLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----P-VFTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---MLAQ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 977 SQKKIISNLFlGRAGSAtvlsgsiAGLE-GGSQLALRratsmrktfttgmaavkkkslcIQMKLQvdALIDTIKKSKLHF 1055
Cdd:cd14896 502 SQLQLVGSLF-QEAEPQ-------YGLGqGKPTLASR----------------------FQQSLG--DLTARLGRSHVYF 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1056 VHCFLPvaegwagEPRSassrrvsssseldLPsgdhceaGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1135
Cdd:cd14896 550 IHCLNP-------NPGK-------------LP-------GL--FDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
....*.
gi 1093953565 1136 RFDVLA 1141
Cdd:cd14896 601 RFGALG 606
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
432-1147 |
1.81e-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: 1.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 501
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 502 QDQSIILLGSSGSGKTTSCQHLVQYLATI-----AGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSL 574
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 575 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAE---NNVFGIVPLAKPEEKQKAA 651
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 652 QQFSKLQAAMKVLGISPDEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 729
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGnvNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 730 HKGGtlQRSTSFRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVN---------RALKSSQHSLCSMMIV 800
Cdd:cd14902 322 IKAG--VEVMVLKLTPEQ------------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 801 DTPGFQNPEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEPPtddsvaavDQASHQSLVr 880
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGID--WKNISYP--------SNAACLALF- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 881 slarTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEgdkkgqspllhsskphHFLLGHSHGTnwVEYNVTGWLNy 960
Cdd:cd14902 451 ----DDKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVEQFVE- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 961 TKQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLCIQMKL 1039
Cdd:cd14902 508 KNTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVSAQFKS 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1040 QVDALIDTIKKSKLHFVHCFLPvaeGWAGEPRSassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRM 1119
Cdd:cd14902 568 QLDRLIVQIGRTEAHYVRCLKP---NEVKKPGI--------------------------FDRERMVEQMRSVGVLEAVRI 618
|
730 740
....*....|....*....|....*...
gi 1093953565 1120 YRQGYPDHMVFSEFRRRFDVLAPHLTKK 1147
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
432-1185 |
2.02e-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: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIILL 509
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 510 GSSGSGKTTSCQHLVQYLATIAGISGNkvfsVEKWQALYT-LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaeNNVFGIVPLAKPEEKQKA--AQQFSKLQAAMKVLGI 666
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGS-----SAAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 667 SPDEQKACWFILAAIYHLG----AAGATKEAAEAgrKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFR 742
Cdd:cd14872 231 DDADINNVMSLIAAILKLGniefASGGGKSLVSG--STVANRDVLKEVATLLGVDAATLEEAL---------TSRLMEIK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 743 QgpeesglGDGTGPKLSALECLEG---MAAGLYSELFTLLVSLVNRALKSSQHSL-CSMMIVDTPGFQNPEQGgsargaS 818
Cdd:cd14872 300 G-------CDPTRIPLTPAQATDAcdaLAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------S 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 819 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsvaavdqashqsLVRSlaRTDearGLLWLL 895
Cdd:cd14872 367 FEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-------------LIEK--KQP---GLMLAL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 896 EEEALVPGASEDTLLERLfsyyGPQEGDKKGQSPLLHSSKPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQ 975
Cdd:cd14872 429 DDQVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLLS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 976 DSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHF 1055
Cdd:cd14872 502 SSKNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPHY 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1056 VHCFLPVAEGWAgeprsassrrvsssselDLPSGDHCeaglLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1135
Cdd:cd14872 549 IRCVKPNQEKRA-----------------RLFDGFMS----LE--------QLRYAGVFEAVKIRKTGYPFRYSHERFLK 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1136 RFDVLAPHLTKKHGRnyivvDERRAVEELLECLDLEKSSCCMGLSRVFFR 1185
Cdd:cd14872 600 RYRFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
428-870 |
3.54e-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: 3.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 428 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLGPRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 500 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGIS--GNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFD 577
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 578 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF---GIVPL-AKPEEKQkaAQQ 653
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 654 FSKLQAAMKVLGISPDEQKACWFILAAIYHLgaagatkeaaeaGRKQFA-----RHEWA--------QKAAYLLGCSLEE 720
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL------------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 721 LSSAI---FKHQHKggtlQRSTSFrqgpeesgLgdgtGPKLSAL--ECLegmAAGLYSELFTLLVSLVNRALKSSQHSLC 795
Cdd:cd14879 305 LETSLtykTKLVRK----ELCTVF--------L----DPEGAAAqrDEL---ARTLYSLLFAWVVETINQKLCAPEDDFA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 796 SMM-IVDTPGFQNpeQGGSArGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAfddlEPPTDDSVAAV 870
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 ... |
432-1142 |
1.18e-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: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIIL 508
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 509 LGSSGSGKTTSCQHLVQYLATiAGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQ-------- 578
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 579 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC----GDGTLRTELHLNHLAENNvfGIVPLAKPEEKQKAAQQ 653
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareaKNTGLSYEENDEKLAKGA--DAKPISIDMSSFEPHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 654 FSKLQ--------------------AAMKVLGISPDEQKACWFILAAIYHLGAAG-ATKEAAEAGRKQFA-RHEWAQKAA 711
Cdd:cd14888 236 FRYLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVVSAsCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 712 YLLGCSLEELSSAIFKHqhkggTLQRSTSFRQGPEESGlgdgtgpklSALECLEGMAAGLYSELFTLLVSLVNRAL-KSS 790
Cdd:cd14888 316 SLLGVDAEDLLNALCYR-----TIKTAHEFYTKPLRVD---------EAEDVRDALARALYSCLFDKVVERTNESIgYSK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 791 QHSLCSMMIVDTPGFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEPPTDDSVAAV 870
Cdd:cd14888 382 DNSLLFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDFPDNQDCVDL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 871 DQASHQSLvrsLARTDEargllwlleeEALVPGASEDTLLERLFSYYGpqeGDKKGQSPllhSSKPHHFLLGHSHGTnwV 950
Cdd:cd14888 454 LQEKPLGI---FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP--V 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 951 EYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVKK 1030
Cdd:cd14888 513 KYCSDGFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKKF 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1031 KSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAgeprsassrrvsssSELDLPSgdhceagllqldvplLRTQLRG 1110
Cdd:cd14888 565 VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFDRIS---------------VNEQLKY 615
|
730 740 750
....*....|....*....|....*....|..
gi 1093953565 1111 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1142
Cdd:cd14888 616 GGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
432-1145 |
2.48e-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: 2.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGIS-----GNKVFSVEkwQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 582
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVE--QAILEsspIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 583 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDGTLRTELHLNHLAEN----NVFGIVPLAKPEEKqkaaQQFSKLQ 658
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLA-GLEHEEREEFYLSTPENyhylNQSGCVEDKTISDQ----ESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 659 AAMKVLGISPDEQKACWFILAAIYHLGAAgatkEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRS 738
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGNI----EFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL---------TQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 739 TSFRqgpeesglGDGTGPKLS---ALECLEGMAAGLYSELFTLLVSLVNRALKSSQHsLCSMMIVDTPGFQNPEQGgsar 815
Cdd:cd14873 302 MFLR--------GEEILTPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 816 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEpptddsvaAVDQASHQSLVRS----LARTDEargl 891
Cdd:cd14873 369 --HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLV--WEDID--------WIDNGECLDLIEKklglLALINE---- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 892 lwlleeEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLnytKQNPAT--QN 969
Cdd:cd14873 433 ------ESHFPQATDSTLLEKLHS--------QHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrDD 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 970 APRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQMKLQVDALIDTI 1048
Cdd:cd14873 496 LLNLLRESRFDFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMATL 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1049 KKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHM 1128
Cdd:cd14873 551 SSSNPFFVRCIKPNMQ--------------------KMPD---------QFDQAVVLNQLRYSGMLETVRIRKAGYAVRR 601
|
730
....*....|....*..
gi 1093953565 1129 VFSEFRRRFDVLAPHLT 1145
Cdd:cd14873 602 PFQDFYKRYKVLMRNLA 618
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
434-1141 |
8.24e-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: 8.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 434 LHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 504
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 505 SIILLGSSGSGKTTSCQHLVQYLATIAGIsGNKVFSVEKWQALY-----------TLLEAFGNSPTIINGNATRFSQILS 573
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATASKL-AKGASTSKGAANAHesieecvllsnLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 574 LDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAEnnvFGIVPLAKPEEKQKA--A 651
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 652 QQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQH 730
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFaQSADGVNVAKAAGLLGVDAAELMFKLVTQTT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 731 KGGtlqRSTSFRQ--GPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAlkSSQHSLCSMMIVDTP----- 803
Cdd:cd14892 318 STA---RGSVLEIklTARE------------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtfspf 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 804 -------GFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsvaaVDQA 873
Cdd:cd14892 381 igildifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----LIQK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 874 SHQSLVRSLartdEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQ-EGDkkgqspllhsskphHFLLGHSHGTnwVEY 952
Cdd:cd14892 450 KPLGLLPLL----EEQMLLKRKTTDKQLLTIYHQTHLDKHPHYAKPRfECD--------------EFVLRHYAGD--VTY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 953 NVTGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktFTTgmaavkkks 1032
Cdd:cd14892 510 DVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------FRT--------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1033 lciqmklQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGDHCEagllqldvpLLRTQLRGSR 1112
Cdd:cd14892 539 -------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQLIYSG 582
|
730 740
....*....|....*....|....*....
gi 1093953565 1113 LLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1141
Cdd:cd14892 583 VLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
432-1142 |
7.17e-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: 7.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGisGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDE 670
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 671 QKACWFILAAIYHLGAAGATKEAAEAGRKQfaRHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFRQGPEESGL 750
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENGSRIS--NGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 751 GdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALkSSQHSLCSMMI--VDTPGFQNPEQGGsargasFEELCHNYTQ 828
Cdd:cd14904 309 A-----PVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFCINYAN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 829 DRLQRLFHERTFVQELERYKEENieLAFDDLEPPTDDSVAAVdqashqslvrslarTDEARGLLWLLEEEALVPGASEDT 908
Cdd:cd14904 377 EKLQQKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEV--------------IDGKMGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 909 LLERLFSYYGPQEGDKKGQSPllhSSKPHHFLLGHSHGTnwVEYNVTGWLNytKQNPATQN-APRLLQDSQKKIISNLFl 987
Cdd:cd14904 441 LVNKIRTNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTELF- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 988 graGSATVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWA 1067
Cdd:cd14904 513 ---GSSEAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSP 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1068 GEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1142
Cdd:cd14904 571 TE-----------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
431-1185 |
1.44e-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: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQaGQVASASIQTM 590
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTE---------LHLNHLAENNVFGivplakpeekQKAAQQFSKLQAAM 661
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 662 KVLGISPDEQKACWFILAAIYHLG-------AAGATKEAAEAGRKqfARHEWaqkAAYLLGCSLEELSSAIfkhqhkggt 734
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGnvyfhkrQLRHGQEGVSVGSD--AEIQW---VAHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 735 LQRSTSFRQGPEESGLG-DgtgpklSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgs 813
Cdd:cd01387 294 TFKVTETRRERIFTPLTiD------QALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 814 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPptddsvaavdqashqsLVRSLARtdEARG 890
Cdd:cd01387 366 ----SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQP----------------VINLISK--KPVG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 891 LLWLLEEEALVPGASEDTLLERLFSYYGPQEgdkkgqspllHSSKPH----HFLLGHSHGTNWveYNVTGWLNYTKqNPA 966
Cdd:cd01387 424 ILHILDDECNFPQATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 967 TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQMKLQ--VDAL 1044
Cdd:cd01387 491 RQDVLELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQL 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1045 IDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQGY 1124
Cdd:cd01387 551 LEKMERCNPWFVRCLKP---------------------------NHKKEPML--FDMDVVMAQLRYSGMLETIRIRKEGY 601
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1125 PDHMVFSEFRRRFDvlapHLTKKHGRNYIVVDERRAVeELLECLDLEKSSCCMGLSRVFFR 1185
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 ... |
433-1140 |
1.85e-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: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 433 VLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIIL 508
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 509 LGSSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQaLYTLLEAFGNSPTIINGNATRFSQILSLDFdQAGQVASASIQ 588
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGD-------GTLRTELH--LNHLAENNvfgivplakpEEKQKAAQQFSKLQA 659
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISaedrenyGLLDPGKYryLNNGAGCK----------REVQYWKKKYDEVCN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqhkgGTLQRST 739
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTCTV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 SFRQGPEESGLGDgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNPEQGgsarg 816
Cdd:cd14889 299 TFTRGEQIQRHHT----KQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPPTDDSVAavdqashqSLVRSLARTDEargllw 893
Cdd:cd14889 370 -RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLN--------KPIGILSLLDE------ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 894 lleeEALVPGASEDTLLERLFSYYG--PQEGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGWLNYTKQN-PATQNA 970
Cdd:cd14889 435 ----QSHFPQATDESFVDKLNIHFKgnSYYGKSRSKSPK--------FTVNHYAGK--VTYNASGFLEKNRDTiPASIRT 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 971 prLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQMKLQVDALIDTIKK 1050
Cdd:cd14889 501 --LFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEKMFA 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1051 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1130
Cdd:cd14889 564 ASPHFVRCIKP--------------------NHVKVPG---------QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
730
....*....|
gi 1093953565 1131 SEFRRRFDVL 1140
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 |
2.64e-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: 2.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLRRTTMLDRGPE-GQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 1093953565 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 ... |
432-1142 |
4.20e-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: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 511
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLATIAGISGNKvfSVEkwQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01385 82 SGSGKTESTNFLLHHLTALSQKGYGS--GVE--QTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGivplakpEEKQKAAQQFSKLQAAMK 662
Cdd:cd01385 158 KYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 663 VLGISPDEQKACWFILAAIYHLGaagatkeAAEAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF--KHQHKG 732
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLG-------NIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTtkKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 733 GTLQRSTSFrqgPEesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAL---KSSQHSLC-SMMIVDTPGFQNP 808
Cdd:cd01385 304 ETLILPYKL---PE-------------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 809 EQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEE-----NIELAfddlepptdDSVAAVDQASHQ--SLVRS 881
Cdd:cd01385 368 GNN------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEgiswhNIEYT---------DNTGCLQLISKKptGLLCL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 882 LartDEargllwlleeEALVPGASEDTLLERLFS-------YYGPQEgdkkgqspllhssKPHHFLLGHSHGTnwVEYNV 954
Cdd:cd01385 433 L---DE----------ESNFPGATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQI 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 955 TGW----LNYTKQNPATqnaprLLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRR 1013
Cdd:cd01385 485 KDFreknLDLMRPDIVA-----VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1014 ATSMRktfttGMAAVKKKSLCIQMKLQV--DALIDTIKKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPsgdh 1091
Cdd:cd01385 560 TTKSL-----LHLHKKKKPPSVSAQFQTslSKLMETLGQAEPFFIRCIKSNAE--------------------KKP---- 610
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1092 ceaglLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1142
Cdd:cd01385 611 -----LRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
431-1140 |
7.06e-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: 7.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 501
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 502 QDQSIILLGSSGSGKTTSCQHLVQYLATiagISGNKVFSVEKWQALYT--------------------LLEAFGNSPTII 561
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQ---LSQQEQNSEEVLTLTSSiratskstksieqkilscnpILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 562 NGNATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL-NHLAENNVFgiv 639
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 640 PLAKPE----EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARH-EWAQKAAYLL 714
Cdd:cd14907 235 YLKKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNkETLQIIAKLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 715 GCSLEELSSAIFKHQHKGGtlqrstsfrqgpeesglGDGTGPKLSALEC---LEGMAAGLYSELFTLLVSLVNRAL---- 787
Cdd:cd14907 315 GIDEEELKEALTTKIRKVG-----------------NQVITSPLSKKECinnRDSLSKELYDRLFNWLVERLNDTImpkd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 788 ----KSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPT 863
Cdd:cd14907 378 ekdqQLFQNKYLSIGLLDIFGFEVFQNN------SFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLNQLSYTD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 864 DDSVAAVDQASHQSLVRSLartDEargllwlleeEALVPGASEDTLLERLFSyygpQEGDKKGQSPLLHSSKPhHFLLGH 943
Cdd:cd14907 452 NQDVIDLLDKPPIGIFNLL---DD----------SCKLATGTDEKLLNKIKK----QHKNNSKLIFPNKINKD-TFTIRH 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 944 SHGTnwVEYNVTGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrratsmrktf 1021
Cdd:cd14907 514 TAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK------------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1022 ttgmAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAGLLQLDV 1101
Cdd:cd14907 570 ----SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KADLFIQGY 618
|
730 740 750
....*....|....*....|....*....|....*....
gi 1093953565 1102 PLLrtQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1140
Cdd:cd14907 619 VLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
432-850 |
1.88e-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: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAGISGNKVFS--VEKwqalYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENnvfgivplakpeekqkaAQQFSKLQAAMKVLGISP 668
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 669 DEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAIfkhqhkggtlqrSTSFRQGP 745
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGniEFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSL------------TTRVMQTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 746 EESGLGDGTGPKLSALECLEG---MAAGLYSELFTLLVSLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npeqggsarg 816
Cdd:cd01382 289 RGGAKGTVIKVPLKVEEANNArdaLAKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN--------- 356
|
410 420 430
....*....|....*....|....*....|....
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEE 850
Cdd:cd01382 357 -SFEQFCINYCNEKLQQFFNERILKEEQELYEKE 389
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
483-853 |
2.25e-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: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 483 APHIYAVAQTAYRAMLMSR---QDQSIILLGSSGSGKTTSCQHLVQYLAT-----IAGISGNKVFSVEKWQALYT----- 549
Cdd:cd14891 52 PPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSKKRKLSVTslder 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 550 ------LLEAFGNSPTIINGNATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLR 622
Cdd:cd14891 132 lmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 623 TELHlnhlaennvfgivpLAKPEEKQKAAQ-------------QFSKLQAAMKVLGISPDEQKACWFILAAIYHLG---- 685
Cdd:cd14891 212 KELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGnief 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 686 -----AAGATKEAAEAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFRqgpeesglGDGTGPKLSA 760
Cdd:cd14891 278 deedtSEGEAEIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR--------GETFTIKRNA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 761 LECL---EGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEqggsaRGASFEELCHNYTQDRLQRLFHE 837
Cdd:cd14891 335 REAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYANEALQATFNQ 409
|
410
....*....|....*.
gi 1093953565 838 RTFVQELERYKEENIE 853
Cdd:cd14891 410 QVFIAEQELYKSEGID 425
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
432-1141 |
1.06e-45 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 177.84 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 499
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 500 --SRQDQSIILLGSSGSGKTTSCQHLVQYLA-----TIAGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQ 570
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 571 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNvFGIVPLAKPE 645
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 646 EKQKAAQ---QFSKLQAAMKVLGISPDEQKACWFILAAIYHLG-----------------AAGATKEAAEAGRKQFARHE 705
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngAASAPCRLASASPSSLTVQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 706 WAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrstsfrqgpeesglGDGTGPKLSALECLE---GMAAGLYSELFTLLVSL 782
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKISVG-----------------GETFHANLSLAQCGDardAMARSLYAFLFQFLVSK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 783 VNRALKSSQHSLCS-----------MMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEEN 851
Cdd:cd14895 377 VNSASPQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 852 IELAFDDLEpptDDSVAAVDQASHQSLVRSLarTDEargllwlleeEALVPGASEDTLLERLFSYY---GPQEGDKKGQS 928
Cdd:cd14895 451 IKWNAVDYE---DNSVCLEMLEQRPSGIFSL--LDE----------ECVVPKGSDAGFARKLYQRLqehSNFSASRTDQA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 929 PLLhsskphhFLLGHSHGTnwVEYNVTGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQ 1008
Cdd:cd14895 516 DVA-------FQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1009 LALRRATSMRKTFTTGMaavkkkslciQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlps 1088
Cdd:cd14895 579 PKLRRRSSVLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRCIKPNDESASD-------------------- 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1089 gdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1141
Cdd:cd14895 629 ---------QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
432-1158 |
5.27e-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: 174.34 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 497
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 498 LMSR----QDQSIILLGSSGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQALYTLLEAFGNSPTIINGNA 565
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAGdnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 566 TRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLlacgdgtlrtelhlnhlaennvfgivpLAKPE 645
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEM---------------------------AIGAS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 646 EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGaaGATKEAAEAGrkqfarHEWAQKAAYLLGCSLEELSSAI 725
Cdd:cd14900 213 EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIG--NLTFEHDENS------DRLGQLKSDLAPSSIWSRDAAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 726 FKHQHKGGTLQRSTS---FRQGPEESGLgdgtgpKLSALEC---LEGMAAGLYSELFTLLVSLVNRALK-----SSQHSL 794
Cdd:cd14900 285 TLLSVDATKLEKALSvrrIRAGTDFVSM------KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddssKSHGGL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 795 CSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafddlepptdDSVAAVDQAS 874
Cdd:cd14900 359 HFIGILDIFGFEVFPKN------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDW----------KYVEFCDNQD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 875 HQSLVrslarTDEARGLLWLLEEEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKPHH----FLLGHSHGTnwV 950
Cdd:cd14900 423 CVNLI-----SQRPTGILSLIDEECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVHYAGH--V 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 951 EYNVTGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrktfttgmaavkk 1030
Cdd:cd14900 488 EYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------------------ 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1031 kslCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLLQLDVPLlrTQLRG 1110
Cdd:cd14900 513 ---GLQFKEQLTTLLETLQQTNPHYVRCLKP---------------------------NDLCKAGIYERERVL--NQLRC 560
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1111 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHGrnYIVVDER 1158
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 ... |
1236-1930 |
7.87e-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: 7.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1236 NIKKNKGVKDWPWWKLFTTVRPLIEVQLSEEQIRNKDE-EIQQLRSKLEKAEKERNELrlnsdrlESRISELTSELtder 1314
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1315 ntgESASQLLDAETAERLRAEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1391
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1392 REVDF----TKKRLQQEFEdKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1467
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1468 LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSqeSKDEA 1547
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 --SLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1625
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLrKDLKRTKALLADAQLMLDHLKNS-----APSKREIAQL 1700
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1701 KN------QLEESeftCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1774
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1775 KAAVAQ---------ASRDLAQIND-LQAQLEEANKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1844
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1845 FERtqvkRLESLASRLKENMEKLTEERDQRIAAENREKEQNK-----------RLQRQLRDTKEEMgelarKEAEASRKK 1913
Cdd:pfam01576 985 QES----RERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdqaekgnsrmkQLKRQLEEAEEEA-----SRANAARRK 1055
|
730
....*....|....*..
gi 1093953565 1914 heLEMDLESLEAANQSL 1930
Cdd:pfam01576 1056 --LQRELDDATESNESM 1070
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
434-1185 |
4.50e-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: 4.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 434 LHTLRQRYGA--------SLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 505
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 506 IILLGSSGSGKTTSCQHLVQYLATIA----GISGNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 581
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVSdrrhGADSQGL--EARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDGTLRTELHLNhlaennvfgivplakPEEKQKAAQQFSKLQAAM 661
Cdd:cd14887 162 LTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQKSS---------------AGEGDPESTDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 662 KVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARH-------EWAQKAAYLLgcSLEELSSAIFKHQHKGGT 734
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceETAADRSHSS--EVKCLSSGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 735 LQRSTSFRQGPEESGLGDGTGPKLSALEC--------LEGMAAG-------LYSELFTLLVSLVNRALKSSQHSLCSMMI 799
Cdd:cd14887 303 LKTVARLLGLPPGVEGEEMLRLALVSRSVretrsffdLDGAAAArdaacknLYSRAFDAVVARINAGLQRSAKPSESDSD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 800 VDTP--------------GFQNPEQGGSARgasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDD 865
Cdd:cd14887 383 EDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 866 SVAAVDQASHQSlVRSLARTDEARGLLWLLEEEALVpgaSEDTLLERLFSYYGPQEGDKKGqSPLLHSSKphhfllghsh 945
Cdd:cd14887 460 PLASTLTSSPSS-TSPFSPTPSFRSSSAFATSPSLP---SSLSSLSSSLSSSPPVWEGRDN-SDLFYEKL---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 946 gtnwvEYNVTGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLALRRATS 1016
Cdd:cd14887 525 -----NKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYTRLVGS 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1017 MRKTFTTGMAAvKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAGL 1096
Cdd:cd14887 593 KKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ---------------------------EAGI 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1097 LQLDvpLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDERRAVEELLECLDLEKSSCC 1176
Cdd:cd14887 645 FEDA--YVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEINSNSYT 716
|
....*....
gi 1093953565 1177 MGLSRVFFR 1185
Cdd:cd14887 717 FGKTKIFFR 725
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
432-1142 |
4.61e-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: 160.46 E-value: 4.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 501
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 502 QDQSIILLGSSGSGKTTSCQHLVQYLATIA---------GISGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQIL 572
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 573 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGivplakPEEKQKAAQ 652
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 653 -------------QFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAG--ATKEAAEAGRKQFARHEWAQKAAYLLGCS 717
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEfeSKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 718 LEELSSAIFKHQHKGGTLQRSTSFRqgPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALK--SSQHSLC 795
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLT--PHK------------AYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 796 SMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddLEPPTDDSVAAVDQASH 875
Cdd:cd14908 382 SVGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF--IEFPDNQDCLDTIQAKK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 876 QSLVRSLarTDEARGLLWlleeealvpgASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHH----FLLGHSHGTnwVE 951
Cdd:cd14908 454 KGILTML--DDECRLGIR----------GSDANYASRLYETYLPEKNQTHSENTRFEATSIQKtkliFAVRHFAGQ--VQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 952 YNV-TGWLnytkqnpatqnaprllqDSQKKIISNlflgragSATVLsgsiagleggsqlalrratsmrktFTTGMaavkk 1030
Cdd:cd14908 520 YTVeTTFC-----------------EKNKDEIPL-------TADSL------------------------FESGQ----- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1031 kslciQMKLQVDALIDTIKKSKLHFVHCFLPvaeGWAGEPRSASSRRvsssseldlpsgdhceagllqldvplLRTQLRG 1110
Cdd:cd14908 547 -----QFKAQLHSLIEMIEDTDPHYIRCIKP---NDAAKPDLVTRKR--------------------------VTEQLRY 592
|
730 740 750
....*....|....*....|....*....|..
gi 1093953565 1111 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1142
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
431-843 |
6.53e-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: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSII 507
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 508 LLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSveKWQALYTLLEAFGNSPTIINGNATRFSQILSLDF-DQAGQVASAS 586
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 587 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVfgiVPLAKPEEKQKAA-----QQFSKLQAAM 661
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 662 KVLGISPDEQKACWFILAAIYHLGAAGATKeAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFK--HQHKGGTLQRST 739
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTA-LTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTdiQYFKGDMIIRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 SFRQGPEESGLgdgtgpklsaleclegMAAGLYSELFTLLVSLVNRALKsSQHSLCSMM-----IVDTPGFQNPEQGgsa 814
Cdd:cd14878 315 TIQIAEFYRDL----------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEEFQKN--- 374
|
410 420
....*....|....*....|....*....
gi 1093953565 815 rgaSFEELCHNYTQDRLQRLFHERTFVQE 843
Cdd:cd14878 375 ---EFEQLCVNMTNEKMHHYINEVLFLQE 400
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
432-1153 |
1.13e-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: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILL 509
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 510 GSSGSGKTTSCQHLVQYLATIAGIS-------GNKVFSVEKwqALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQA 579
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnNNNNNSIEK--DILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 580 -GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDGTLRTELHLNH--------LAENNVFGIV------PLAK 643
Cdd:cd14906 160 dGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 644 PEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEA--AEAGRKQFARHEWAQKAAYLLGCSLEEL 721
Cdd:cd14906 240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfSKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 722 SSAIFKHQHKGGTlqRSTSFRQgPEESGLGDGTGPKLSaleclegmaAGLYSELFTLLVSLVNR-----------ALKSS 790
Cdd:cd14906 320 KQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTRDALS---------KSLYVRLFKYIVEKINRkfnqntqsndlAGGSN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 791 QHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELA---FDDleppTDDSV 867
Cdd:cd14906 388 KKNNLFIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----NKECI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 868 AAVDQASHQSLvrSLArTDEArgllwlleeeaLVPGASEDTLLERLFSYYgpqegdKKGQSPLLHSSKPHHFLLGHSHGT 947
Cdd:cd14906 458 ELIEKKSDGIL--SLL-DDEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGD 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 948 nwVEYNVTGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGMAA 1027
Cdd:cd14906 518 --VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTVSG 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1028 vkkkslciQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvssSSELDLPSGDHCEagllqldvplLRTQ 1107
Cdd:cd14906 576 --------QFLEQLNQLIQTINSTSVHYIRCIKP-------------------NQTMDCNNFNNVH----------VLSQ 618
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1108 LRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1153
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
431-856 |
2.16e-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: 154.62 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 506
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 507 ILLGSSGSGKTTSCQHLVQYLATIAG----ISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAG 580
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAsptsWESHKIAERIEQRILNSnpVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLacgDGTLRTELHLNHLAENNVFGIVPlakPEEKQKAAQQFSKLQAA 660
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPEGAAFSWLP---NPERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 661 MKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFA--RHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRs 738
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQ- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 739 tSFRQgpeesglgdgtgpKLSALEC---LEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQN-PEQggs 813
Cdd:cd14880 314 -VFKK-------------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPEN--- 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1093953565 814 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAF 856
Cdd:cd14880 377 ----SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
432-867 |
5.65e-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: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPrgAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIILLGS 511
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNP--YETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 512 SGSGKTTSCQHLVQYLatIAGISGNKvfSVEK-WQALYTLLEAFGNSPTIINGNATRFSQILSLDFDqaGQVASASIQTM 590
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLakpeekqkaAQQFSKLQAAMKVLGISpdE 670
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQL---------SEKYKMTCSAMKSLGIA--N 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 671 QKACWFILAAIYHLGAAGATKEaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QHKGGTLQRSTSFRQgpees 748
Cdd:cd14898 221 FKSIEDCLLGILYLGSIQFVND----GILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTLKQ----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 749 glgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALK-SSQHSLCsmmIVDTPGFQNPEQGGsargasFEELCHNYT 827
Cdd:cd14898 292 -----------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQLCINWT 351
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1093953565 828 QDRLQRLFHERTFVQELERYKEENIElaFDDLEPPTDDSV 867
Cdd:cd14898 352 NEKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC 389
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
397-1061 |
1.26e-36 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 150.95 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 397 DGAILDVDEDDVEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFK 475
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 476 GCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLAtiAGISGNKVFSVEK--WQAlYTLLE 552
Cdd:PTZ00014 155 DAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLKIQNaiMAA-NPVLE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 553 AFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAE 632
Cdd:PTZ00014 232 AFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 633 ----NN----VFGIVPlakpeekqkaAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLG-------AAGATKEAAEAG 697
Cdd:PTZ00014 312 ykyiNPkcldVPGIDD----------VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveiegkEEGGLTDAAAIS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 698 RKQFarhEWAQKAAYLLGCSLEELS-SAIFKHQHKGGtlQRSTSFRQGPEESGLgdgtgpKLSaleclegMAAGLYSELF 776
Cdd:PTZ00014 382 DESL---EVFNEACELLFLDYESLKkELTVKVTYAGN--QKIEGPWSKDESEML------KDS-------LSKAVYEKLF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 777 TLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIelaf 856
Cdd:PTZ00014 444 LWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNN------SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGI---- 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 857 ddlepptddSVAAVDQASHQSLVRSLarTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEGDKKGQspllhSSKP 936
Cdd:PTZ00014 514 ---------STEELEYTSNESVIDLL--CGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAK-----VDSN 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 937 HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIAgleggsqlalrrats 1016
Cdd:PTZ00014 578 KNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDLFEG----VEVEKGKLA--------------- 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1093953565 1017 mrktfttgmaavKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLP 1061
Cdd:PTZ00014 636 ------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP 668
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
431-1137 |
7.39e-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: 7.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 500 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT---------------LLEAFGNSPTIINGN 564
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASpsrttieeqvlqsnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 565 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDGTLRTELHLNHLAEN-NVFGI 638
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 639 VPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAA-----------GATKEAAEAGRKQFARHEWA 707
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVdfeqiphkgddTVFADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 708 QKAAYLLGCSLEELSSAIFKHQhkggtLQRSTSFRQGPEESGLGDGTGPKLSaLEClegmaaglYSELFTLLVSLVNRAL 787
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRW-----LHASNETLVVGVDVAHARNTRNALT-MEC--------YRLLFEWLVARVNNKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 788 K---------------SSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI 852
Cdd:cd14899 387 QrqasapwgadesdvdDEEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 853 ELAFDDLEpptdDSVAAVDQASHQSLvrslartdearGLLWLLEEEALVPGASEDTLLERlfsYYgpQEGDKKGQSPLLH 932
Cdd:cd14899 461 RWSFVDFP----NNRACLELFEHRPI-----------GIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 933 SS----KPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQ 1008
Cdd:cd14899 521 SApliqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1009 LALRRATSmrktfttgmaAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlps 1088
Cdd:cd14899 595 RTRRRAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP--------------------------- 637
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1089 GDHCEAGLLQldVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1137
Cdd:cd14899 638 NDSHVGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
431-1143 |
6.24e-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: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 500
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 501 RQDQSIILLGSSGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQAL--YTLLEAFGNSPTIINGNATRFSQ 570
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGdeteprpdSEGASGVLHPIGQQILhaFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 571 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDGTLRTELHLNHLAENnvFGIVPLAKPEEKQ 648
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 649 KA--AQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAyllGCSLEELSSAIF 726
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQ---SCALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 727 -KHQHKGGTLQRSTSFRQGPEESGLGDGTGPKLSALECLEGMAA------GLYSELFTLLVSLVN--------RALKS-- 789
Cdd:cd14893 316 aAKLLEVEPVVLDNYFRTRQFFSKDGNKTVSSLKVVTVHQARKArdtfvrSLYESLFNFLVETLNgilggifdRYEKSni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 790 ---SQhslcSMMIVDTPGFQN--PEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEE------------NI 852
Cdd:cd14893 396 vinSQ----GVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDEsqqvenrltvnsNV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 853 ELAFDD---LEPPTDDSVAAVDQASHQSLVRS----------LARTDEARGLLWlleeealvPGASEDTLLERLfsyygp 919
Cdd:cd14893 466 DITSEQekcLQLFEDKPFGIFDLLTENCKVRLpndedfvnklFSGNEAVGGLSR--------PNMGADTTNEYL------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 920 qeGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLS 997
Cdd:cd14893 532 --APSKDWRLL--------FIVQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAA 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 998 GSIAglEGGSQLALRRATS--MRKTFTTGMAAVK-KKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsas 1074
Cdd:cd14893 592 ASSE--KAAKQTEERGSTSskFRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVCIKP------------- 656
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1075 srrvssssELDLPSGdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1143
Cdd:cd14893 657 --------NETLEEG--------VFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1275-1963 |
2.63e-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: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1275 IQQLRSKLEKAEKERNELRLNSDRLESRISELTSE---LTDERNTGESASQLL----DAETAERLR----AEKEMKELQT 1343
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1344 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQEFEDKLEVEQQNK 1416
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKL 1496
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1497 QREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1569
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQAGTIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1616
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1617 QKKLKQME----------------------------------VQLEEEYEDKQK-VLR---------EKRELEGK--LAT 1650
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyVFGdtlvvedieAARRLMGKyrMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1651 LSDQ--------------------VNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSA--------PSKREIAQLKN 1702
Cdd:TIGR02169 644 LEGElfeksgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1703 QLEESEFTcAAAVKAR--------KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1769
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1770 LMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1845
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1846 ERTQVKRLESLAS---RLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS------------ 1910
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelsledv 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1911 -RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINS 1963
Cdd:TIGR02169 957 qAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEE 1011
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
432-1141 |
3.53e-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: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAgiSGNKVfSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLG--DGNRG-ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTLRteLHLNHLAENNVFGIVPLAKPEEKQKA----------AQQFSKLQAA 660
Cdd:cd14882 158 QLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 661 MKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgrkQFARHEWAQKAAYLLGCSLEELSSAIFKH-QHKGGTLQRSt 739
Cdd:cd14882 236 LKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYA---ELENTEIASRVAELLRLDEKKFMWALTNYcLIKGGSAERR- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 sfRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVN------RALKSSQHSLcsmMIVDTPGFQNPEQGGs 813
Cdd:cd14882 312 --KHTTEE------------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFECFHRNR- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 814 argasFEELCHNYTQDRLQRLFHERTFVQELERYKEENI----------ELAFDDLEPPTDDSVAAVDQASHQslvrsla 883
Cdd:cd14882 374 -----LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIptinlrfydnKTAVDQLMTKPDGLFYIIDDASRS------- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 884 rtdeargllwlleeealvpGASEDTLLERLfsyygpqegdKKGQSPLLHSSKPHHFLLGHshgtnwveynVTGWLNYTKQ 963
Cdd:cd14882 442 -------------------CQDQNYIMDRI----------KEKHSQFVKKHSAHEFSVAH----------YTGRIIYDAR 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 964 NPATQN----APRL---LQDSQKKIISNLFlgragsatvlsgsiagleGGSQlaLRRATSMRKTFttgmaavKKKSLCIQ 1036
Cdd:cd14882 483 EFADKNrdfvPPEMietMRSSLDESVKLMF------------------TNSQ--VRNMRTLAATF-------RATSLELL 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1037 MKLQVDAlidtiKKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPSGDHCEagllqldvpLLRTQLRGSRLLDA 1116
Cdd:cd14882 536 KMLSIGA-----NSGGTHFVRCIRSDLE--------------------YKPRGFHSE---------VVRQQMRALAVLDT 581
|
730 740
....*....|....*....|....*
gi 1093953565 1117 MRMYRQGYPDHMVFSEFRRRFDVLA 1141
Cdd:cd14882 582 AKARQKGFSYRIPFQEFLRRYQFLA 606
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1259-1974 |
6.94e-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: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEM 1338
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1339 KELQTQYDALKKQMEV--MEMEVMEARLIRAAEIngevddddaggEWRLKYERAVREVDFtkkrlqQEFEDKLEVEQQNK 1416
Cdd:TIGR02168 305 QILRERLANLERQLEEleAQLEELESKLDELAEE-----------LAELEEKLEELKEEL------ESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQR--E 1494
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQAelE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1495 KLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEskdeASLAKVKKQLRDLEAKVKDQEEELDEQA 1574
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1575 GTIQMLEQ-----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEG 1646
Cdd:TIGR02168 520 GILGVLSElisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1647 KLATLSDQVnrrdfESEKRLRKDLKrtkALLA------DAQLMLDHLKNSAPSKReIAQLKNQLEESEFTCAAAVKARKA 1720
Cdd:TIGR02168 600 FLGVAKDLV-----KFDPKLRKALS---YLLGgvlvvdDLDNALELAKKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1721 ----MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1796
Cdd:TIGR02168 671 sileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1797 EANKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRI 1875
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1876 AAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMES 1954
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKR 910
|
730 740
....*....|....*....|
gi 1093953565 1955 DENEDLINSEGDSDVDSELE 1974
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 ... |
1273-1950 |
9.98e-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: 132.61 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1273 EEI-QQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDErntgESASQLLDAEtaeRLRAEKEMKELQTQYDALKKQ 1351
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1352 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQEFEDKLEVEQqNKRQLERRLGDLQ 1427
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1428 ADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEA 1507
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1508 FSLKQQLEEkdmdiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQagt 1576
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1577 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS- 1652
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1653 --DQVNRRDFESEK---RLRKDLKRTKALLADAQLML-------------------------DHLKNSAPSKREI----- 1697
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1698 ------AQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1761
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1762 EDQEDMNELMKKHKAAVAQAS--RDLAQIN---------DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1828
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1829 VSRQEAKiRELETRLEFERTQVKRLESLAS-------RLKENMEKLTEERDQRIAAENREKEQNKR-LQRQLRDTKEEMG 1900
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELEDELQatedaklRLEVNMQALKAQFERDLQARDEQGEEKRRqLVKQVRELEAELE 759
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1901 ELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1950
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 ... |
433-853 |
1.57e-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: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 433 VLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 506
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 507 ILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALytLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASAS 586
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNP--LLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 587 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF--GIVPLAKPEEKQKaaqQFSKLQAAMKVL 664
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnaSKCYDAPGIDDQK---EFAPVRSQLEKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 665 gISPDEQKACWFILAAIYHLG--------AAGATKEAAEAGRKQFarhewaQKAAYLLGCSLEELSSAIfkhqhkggtLQ 736
Cdd:cd14886 238 -FSKNEIDSFYKCISGILLAGniefseegDMGVINAAKISNDEDF------GKMCELLGIESSKAAQAI---------IT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 737 RSTSFRQGPEESGLgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 816
Cdd:cd14886 302 KVVVINNETIISPV-----TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN----- 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE 853
Cdd:cd14886 372 -TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1398-1949 |
2.17e-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: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1398 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1477
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1557
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1558 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKV 1637
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1638 LREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLD-----HLKNSAPSKREIAQLKNQLEESEFTCA 1712
Cdd:COG1196 462 LELLAELLEEAALLEAALAELL-EELAEAAARLLLLLEAEADYEGFLEgvkaaLLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1713 AAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQ 1792
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1793 AQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD 1872
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1873 QRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1949
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
431-1142 |
2.12e-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: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIILL 509
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 510 GSSGSGKTTSCQHLVQYLATiagiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS----QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 590 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLaeNNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPD 669
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 670 EQKACWFILAAIYHLG--------AAGATKEAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQHKGGTLQRStsf 741
Cdd:cd14874 225 HCISIYKIISTILHIGniyfrtkrNPNVEQDVVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 742 rqgpeesglgdgtgpklSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSlCSMMIVDTPGFQNPEQGGsargasFEE 821
Cdd:cd14874 297 -----------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 822 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLarTDEARgllwlleeealV 901
Cdd:cd14874 353 FLINSVNERIENLFVKHSFHDQLVDYAKDGISVDYKVPNSIENGKTVELLFKKPYGLLPLL--TDECK-----------F 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 902 PGASEDTLLERL------FSYYGPQEGDKKGQspllhsskphhFLLGHSHGTNWveYNVTGWLNYTKQNpATQNAPRLLQ 975
Cdd:cd14874 420 PKGSHESYLEHCnlnhtdRSSYGKARNKERLE-----------FGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLR 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 976 DSQKKIISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqmklqvdaLIDTIKKSKLHF 1055
Cdd:cd14874 486 SSKNPIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHF 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1056 VHCflpvaegwageprsassrrvsssseldLPSGDHCEAGllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1135
Cdd:cd14874 533 VRC---------------------------IKSNNERQPK--KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583
|
....*..
gi 1093953565 1136 RFDVLAP 1142
Cdd:cd14874 584 QYRCLLP 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1265-1965 |
4.67e-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: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1344
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKKQMevmemevmearliraAEINGEVDdddaggewrlkyeravrevdftkkrlqqEFEDKLEVEQQNKRQLERRLG 1424
Cdd:TIGR02168 339 LAELEEKL---------------EELKEELE----------------------------SLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1425 DLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQR--EKLQREKDM 1502
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQAelEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1503 LLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ 1582
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQAR----LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1583 -----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ 1654
Cdd:TIGR02168 528 lisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1655 VnrrdfESEKRLRKDLkrtKALLA------DAQLMLDHLKNSAPS-------------------------------KREI 1697
Cdd:TIGR02168 608 V-----KFDPKLRKAL---SYLLGgvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1698 AQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA 1777
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1778 VAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLEFERTQVKRLESL 1856
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1857 ASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKL 1936
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
730 740 750
....*....|....*....|....*....|
gi 1093953565 1937 AFKRIGDLQAAIED-EMESDENEDLINSEG 1965
Cdd:TIGR02168 920 LREKLAQLELRLEGlEVRIDNLQERLSEEY 949
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1278-1963 |
4.75e-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: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1278 LRSKLEKAEKERNELRLNSDRLESRISELtseltdERNTGESASQlldAETAERLRaekemkELQTQYDALKKQMEVMEM 1357
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLEDILGEL------ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1358 EVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRA 1436
Cdd:COG1196 235 RELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1437 LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEE 1516
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1517 KDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ 1596
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1597 THSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDK-QKVLREKRELEGKLATLSDQVNRRDfesEKRLRKDLkrtkA 1675
Cdd:COG1196 471 EAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFlEGVKAALLLAGLRGLAGAVAVLIGV---EAAYEAAL----E 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1676 LLADAQLMLDHLKNSAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKN 1754
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1755 EIQNRLEEDQEDM-NELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEklqalqsqvefleqsmvdkslvsRQE 1833
Cdd:COG1196 622 LLGRTLVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL-----------------------EAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1834 AKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrkK 1913
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE---E 755
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1914 HELEMDLESLEAANQSLQADLklafKRIGDL-QAAIE--DEME------SDENEDLINS 1963
Cdd:COG1196 756 LPEPPDLEELERELERLEREI----EALGPVnLLAIEeyEELEerydflSEQREDLEEA 810
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
484-1147 |
5.36e-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: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 484 PHIYAVAQTAYRAMLM-SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGI-SGN--------KVFSVEKWQAlyTLLEA 553
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMhSSNtsqrsiadKIDENLKWSN--PVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 554 FGNSPTIINGNATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGD-------GTLRTEL 625
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSpeekkelGGLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 626 HLNHLAENNVFgiVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaaeagrkQFARHE 705
Cdd:cd14875 214 DYKCLNGGNTF--VRRGVDGKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-------QNDKAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 706 WAQKAAYLLGCSLEELSSAIFKHQHkggtLQRS-----TSFRQGPEESGLGDgtgpklsalecleGMAAGLYSELFTLLV 780
Cdd:cd14875 285 IADETPFLTACRLLQLDPAKLRECF----LVKSktslvTILANKTEAEGFRN-------------AFCKAIYVGLFDRLV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 781 SLVNRALKSSQH-SLCSMM-IVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LA 855
Cdd:cd14875 348 EFVNASITPQGDcSGCKYIgLLDIFGFENFTRN------SFEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 856 FddlePPTDDSVAAVDQAShqslVRSLARTDEargllwlleeEALVPGASEDTLLERLFSYYGpqegdkkGQSPLL---H 932
Cdd:cd14875 422 F----PDNSECVNMFDQKR----TGIFSMLDE----------ECNFKGGTTERFTTNLWDQWA-------NKSPYFvlpK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 933 SSKPHHFllGHSHGTNWVEYNVTGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagleggsqlal 1011
Cdd:cd14875 477 STIPNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1012 RRatsmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsgdH 1091
Cdd:cd14875 535 RR----------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKP-----------------------------N 569
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1092 CEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1147
Cdd:cd14875 570 MEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
433-1061 |
2.96e-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: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 433 VLHTLRQRYGASLLHTYAGPSLLVLGP---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 497
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 498 LMSRQDQSIILLGSSGSGKTTSCQHLVQYLAtiAGISGNKVFSVEKW-QALYTLLEAFGNSPTIINGNATRFSQILSLDF 576
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 577 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENN--------VFGIVPLAkpeekq 648
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDVA------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 649 kaaqQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSL-----EELSS 723
Cdd:cd14876 221 ----DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK-TEQGVDDAAAISNESLEVFKEACSLlfldpEALKR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 724 AIF-KHQHKGGtlQRSTSFRQGPEESGLgdgtgpKLSaleclegMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDT 802
Cdd:cd14876 296 ELTvKVTKAGG--QEIEGRWTKDDAEML------KLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 803 PGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPPTD------DSVAAV--D 871
Cdd:cd14876 361 FGFEVFKNN------SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSIleD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 872 QAshqslvrsLArtdeargllwlleeealvPGASEdtllERLFSYYGPQEGDKKGQSPLLHSSKpHHFLLGHSHGTnwVE 951
Cdd:cd14876 435 QC--------LA------------------PGGSD----EKFVSACVSKLKSNGKFKPAKVDSN-INFIVVHTIGD--IQ 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 952 YNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkk 1030
Cdd:cd14876 482 YNAEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK------------ 537
|
650 660 670
....*....|....*....|....*....|.
gi 1093953565 1031 kslciqmklQVDALIDTIKKSKLHFVHCFLP 1061
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 ... |
1250-1934 |
9.92e-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: 9.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1250 KLFTTVRPLIEVQLSEEQIRNKDEEiqQLRSKLEKA----EKERNELRLNSDRLESRISELTSELTDERNTGESASQLLD 1325
Cdd:pfam01576 176 KSLSKLKNKHEAMISDLEERLKKEE--KGRQELEKAkrklEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1326 AETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIR----------AAEINGEVDDDDAGGEWRLKYERAVREVd 1395
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRrdlgeelealKTELEDTLDTTAAQQELRSKREQEVTEL- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1396 ftKKRLQQE---FEDKL-EVEQQNKRQLErrlgDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK 1471
Cdd:pfam01576 333 --KKALEEEtrsHEAQLqEMRQKHTQALE----ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1472 QRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1551
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1552 VKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEY 1631
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1632 EDKQKVLREKRELEGKLATLS-DQVNRRDFES--EKRLRK---DLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQL 1704
Cdd:pfam01576 566 AAYDKLEKTKNRLQQELDDLLvDLDHQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARAL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1705 EESEFTCAAAVKARKAMEVEIEDLHLQIDDIAK-------AKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA 1777
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1778 VAQASRdlaqinDLQAQlEEANKEKQelqeklQALQSQVefleqsmvdkslvsrqeakiRELETRLEFERTQvkrlESLA 1857
Cdd:pfam01576 726 KAQFER------DLQAR-DEQGEEKR------RQLVKQV--------------------RELEAELEDERKQ----RAQA 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1858 SRLKENMEKLTEERDQRIAAENREKE----QNKRLQRQLRDTKEEMGE--LARKEAEASRKkhELEMDLESLEAANQSLQ 1931
Cdd:pfam01576 769 VAAKKKLELDLKELEAQIDAANKGREeavkQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQ 846
|
...
gi 1093953565 1932 ADL 1934
Cdd:pfam01576 847 EDL 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1403-1988 |
2.25e-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: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1403 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1482
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1483 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEA--------------S 1548
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqlelQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1549 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEM---------------ESRDEEVEEAR 1613
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeelerleealEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1614 QSCQKK-------------LKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVN-RRDFES--EKRLRKDL------- 1670
Cdd:TIGR02168 475 QALDAAerelaqlqarldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAaiEAALGGRLqavvven 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1671 ----KRTKALLADAQ------LMLDHLKNSAPSKREIAQLKNQlEESEFTCAAAVKARKAMEVEIEDL--HLQI-DDIAK 1737
Cdd:TIGR02168 555 lnaaKKAIAFLKQNElgrvtfLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYLlgGVLVvDDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1738 A----------------------------KTALEEQLSRLQREKN--EIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ 1787
Cdd:TIGR02168 634 AlelakklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1788 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSL-VSRQEAKIRELETRLEFERTQVKRLEslasrlkENMEK 1866
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeLTELEAEIEELEERLEEAEEELAEAE-------AEIEE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1867 LTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQA 1946
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1093953565 1947 A---IEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNK 1988
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 ... |
432-872 |
4.30e-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: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 503
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 504 QSIILLGSSGSGKTTSCQHLVQYLATIAGISgNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQ----- 578
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 579 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDgtlrTELHLNHLAEN-NVFGIVPLAK--------- 643
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSD----EDLARRNLVRNcGVYGLLNPDEshqkrsvkg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 644 ------------PEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAgATKEAAEagrkqfarhewaqkaa 711
Cdd:cd14884 237 tlrlgsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNR-AYKAAAE---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 712 yLLGCSLEELSSAIfkhqhKGGTLQRSTSFRQGPEEsglgdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQ 791
Cdd:cd14884 300 -CLQIEEEDLENVI-----KYKNIRVSHEVIRTERR---------KENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 792 HSLCSM------------MIVDTPGFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIeLAFDDL 859
Cdd:cd14884 365 EKDESDnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDV 437
|
490
....*....|...
gi 1093953565 860 EPPTDDSVAAVDQ 872
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 ... |
431-986 |
2.53e-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: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 431 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYsekvMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLatIAGISGNKVFSVEKWQALYtLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 591 LLEKLRVARRPASEATFNVFYYLLACGDGTL------RTELHLNHLAENNVfgIVPlakpeeKQKAAQQFSKLQAAMKVL 664
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELknkykiRSENEYKYIVNKNV--VIP------EIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 665 GISpDEQKACWFILAAIYHLG-------AAGATKEAAEAGRKQFarhEWAQKAAYLLGCSLEEL-SSAIFKHQhkgGTLQ 736
Cdd:cd14937 226 NMH-DMKDDLFLTLSGLLLLGnveyqeiEKGGKTNCSELDKNNL---ELVNEISNLLGINYENLkDCLVFTEK---TIAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 737 RSTSFRQGPEESglgdgtgpklsaLECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 816
Cdd:cd14937 299 QKIEIPLSVEES------------VSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN----- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 817 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafDDLEPPTDDSVaaVDQASHQSLVRSLARtDEARGllwlle 896
Cdd:cd14937 362 -SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILI--ESVKYTTNESI--IDLLRGKTSIISILE-DSCLG------ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 897 eealvPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSskphhFLLGHShgTNWVEYNVTGWLNYTKQNPATqNAPRLLQD 976
Cdd:cd14937 430 -----PVKNDESIVSVYTNKFSKHEKYASTKKDINKN-----FVIKHT--VSDVTYTITNFISKNKDILPS-NIVRLLKV 496
|
570
....*....|
gi 1093953565 977 SQKKIISNLF 986
Cdd:cd14937 497 SNNKLVRSLY 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1260-1874 |
1.80e-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: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1339
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALKKQMEVMEMEVMEARlIRAAEINGEVD--DDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKleveQQNKR 1417
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLE-ARLERLEDRRErlQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1418 QLERRLGDLQADSEESQRALQQLKKKCQRLTAE---LQDTKLHLEGQQ--VRNHELEKKQR-----------RFDSELSQ 1481
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSegVKALLKNQSGLsgilgvlseliSVDEGYEA 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1482 AHEEAQREKLQREKLQREKDMLLAEAFsLKQ-----------------QLEEKDMDI-------AGFTQKVVSLEAELQD 1537
Cdd:TIGR02168 538 AIEAALGGRLQAVVVENLNAAKKAIAF-LKQnelgrvtflpldsikgtEIQGNDREIlkniegfLGVAKDLVKFDPKLRK 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1538 --------------------------------------------ISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1573
Cdd:TIGR02168 617 alsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1574 AGTIQMLEQAKLRLEMEME-------RMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE 1640
Cdd:TIGR02168 697 EKALAELRKELEELEEELEqlrkeleELSRQISalrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1641 KRELEGKLATLSDQVNR--RDFESEKR----LRKDLKRTKALLADAQLML-DHLKNSAPSKREIAQLKNQLEESEFTCAA 1713
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQlkEELKALREaldeLRAELTLLNEEAANLRERLeSLERRIAATERRLEDLEEQIEELSEDIES 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1714 AVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA---VAQASRDLAQI-N 1789
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELrekLAQLELRLEGLeV 936
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1790 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslVSRQEAKI--------------RELETRLEFERTQVKRLES 1855
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR--LKRLENKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTE 1014
|
730
....*....|....*....
gi 1093953565 1856 LASRLKENMEKLTEERDQR 1874
Cdd:TIGR02168 1015 AKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1185-1968 |
2.94e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.16 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1185 RAGTLARLEEQRDEQTSRNLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1257
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1258 LIEVQLSEEQIR----NKDEEIQQLRSKLEKAEKERNE---LRLNSDRLESRISELTSELTDERNTGESASQLLDAETAE 1330
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1331 RLRAEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLE 1410
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1411 VEQQNKRQLERRLGDLQADSEESQRAlQQLKKKCQRLTAELQDTKlHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQR 1488
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1489 EKLQREKLQREKdmllaEAFSLKQQLEEKDmdiagftqkvvsleaelqdiSSQESKDEASLAKVKKQLRDLEAKVKDQEE 1568
Cdd:PTZ00121 1446 ADEAKKKAEEAK-----KAEEAKKKAEEAK--------------------KADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1569 ELDEQAGTIQMLEQAKlrlEMEMERMRQTHSKEMESRdeEVEEARQSCQKKlKQMEVQLEEEY---EDKQKVLREKRELE 1645
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEAK--KADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAEE 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1646 GKL-----ATLSDQVNRRDFESEKRLRKDLKRTKALLA----DAQLMLDHLKNSAPSKREIAQLKNQLEES--------- 1707
Cdd:PTZ00121 1575 DKNmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelkk 1654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1708 ---EFTCAAAVKARKAME--VEIEDLHLQIDDIAKAktalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVA 1779
Cdd:PTZ00121 1655 aeeENKIKAAEEAKKAEEdkKKAEEAKKAEEDEKKA----AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKI 1730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTqVKRLESLASR 1859
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIFDNFAN 1809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1860 LKE---------NMEKLTE--ERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQ 1928
Cdd:PTZ00121 1810 IIEggkegnlviNDSKEMEdsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1093953565 1929 SLQADLKlafkrigDLQAAIEDEMESDENEDLINSEGDSD 1968
Cdd:PTZ00121 1890 IEKIDKD-------DIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1260-1981 |
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 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRL--ESRISELTSELTDERNTgESASQLLDAETAERLRAEKE 1337
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1338 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQEFEDKLEVEQQnKR 1417
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEAV-KK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1418 QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQREKLQREK 1495
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1496 LQREKdmllAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQA 1574
Cdd:PTZ00121 1312 EEAKK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1575 GTIQMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ 1654
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1655 VNRRDFESEKRLRKDLKR----TKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEIEDLH 1729
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1730 LQIDDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQ 1806
Cdd:PTZ00121 1546 KKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1807 EKLQALQSQVEFLEQSMVDKslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1886
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1887 RLQR-------------QLRDTKEE----MGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1949
Cdd:PTZ00121 1703 KAEElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
730 740 750
....*....|....*....|....*....|...
gi 1093953565 1950 DEM-ESDENEDLINSEGDSDVDSELEDRVDGVK 1981
Cdd:PTZ00121 1783 EELdEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1386-1911 |
3.54e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.84 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1386 KYERAVREVDFTKKRLQqEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1465
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1466 hELEKKQRRFDSELSQAHEEAQ--REKLQ-REKLQREKDMLLAEAFSLKQQLEEKDMDIAGFtQKVVSLEAELQDISSQE 1542
Cdd:PRK03918 304 -EYLDELREIEKRLSRLEEEINgiEERIKeLEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1543 SkdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQK 1618
Cdd:PRK03918 382 T--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1619 KLKQMEVQLEEEYEDKQKVLREKRELEGKLatlsdqvnrrdfESEKRLRKDLKrtkalladaqlMLDHLKN--SAPSKRE 1696
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1697 IAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMN 1768
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1769 ELMKKH------KAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETR 1842
Cdd:PRK03918 596 ELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1843 LEFERTQVKRLESLASRLKENMEKLTEERDQRiaaeNREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1911
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 ... |
432-860 |
5.31e-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: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 510
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 511 SSGSGKTTSCQHLVQYLATIAgisgnkvFSVEKWQALYTL-----LEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 585
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTD-------LSRSKYLRDYILesgiiLESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 586 SIQTMLLEKLRVARRPASEATFNVFYYLLacgDGTLRTELHLNHLAENNVF------GIVPLAKPEEKqkaaQQFSKLQA 659
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFL---KGITDEEKAAYQLGDINSYhylnqgGSISVESIDDN----RVFDRLKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 660 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEwaqkaayllgcsleelssaifkhqhkggTLQRST 739
Cdd:cd14905 226 SFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIE----------------------------SLSHNI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 740 SFRQGPEESGL-GDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLcSMMIVDTPGFQNPEQGGsargas 818
Cdd:cd14905 278 TFDSTKLENILiSDRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------ 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1093953565 819 FEELCHNYTQDRLQRLFHERTFVQELERYKEENI----ELAFDDLE 860
Cdd:cd14905 351 YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNE 396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1402-1987 |
1.07e-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: 105.87 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1402 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1479
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1480 SQAHEEAQREKLQREKLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1559
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1560 EAKVKDQEEELDEQAGTIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1636
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1637 VLREKRElegKLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESeftCAAAVK 1716
Cdd:TIGR04523 247 EISNTQT---QLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 AR-KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDL-AQ 1787
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1788 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFERTQVKR 1852
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1853 LESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1932
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1933 DLKLAF--KRIGDLQAAIEDEMESDENEDLINSEGDSDVDsELEDRVDGVKSWLSKN 1987
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEK 608
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1260-1842 |
1.52e-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: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1339
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQEFEDKLEVEQQNKRQL 1419
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1420 ERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQRE 1499
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1500 KDMLLAEAFSLKQQLEEKDmdiaGFTQKVVSLEAELQdissqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQM 1579
Cdd:COG1196 486 LAEAAARLLLLLEAEADYE----GFLEGVKAALLLAG---------LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1580 LEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRD 1659
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1660 FESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEIEDLHLQIDDIAKAK 1739
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1740 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK----AAVAQASRDLAQINDLQAQLEEANK--------------E 1801
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEReiealgpvnllaieE 789
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1093953565 1802 KQELQEKLQALQSQVEFLEQSMvdKSLVSRqeakIRELETR 1842
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 ... |
1260-1889 |
2.56e-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: 104.72 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1339
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQL 1419
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1420 E----------RRLGDLQADSEESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1482
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1483 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1562
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1563 VKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEE---EYED 1633
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1634 -KQKVLREKRELEGKLATLsDQVNRRDFESEKRLrKDLKRTKALLADAQLMLDHLKNSApsKREIAQLKNQLEESEFTca 1712
Cdd:TIGR04523 480 iKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKEK--ESKISDLEDELNKDDFE-- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1713 aavkarkameveiedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQ 1792
Cdd:TIGR04523 554 -----------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1793 AQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFERTQVKRLESLASRLKEN 1863
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELSLHYKKY 696
|
650 660
....*....|....*....|....*...
gi 1093953565 1864 MEKLTEERDQRIAAENRE--KEQNKRLQ 1889
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 ... |
1416-1949 |
3.55e-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: 101.41 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREK 1495
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1496 LQREKDMllaeafslkqqleekdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1575
Cdd:pfam01576 150 LSKERKL----------------------------LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1576 TIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDqv 1655
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE-- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1656 nrrDFESEKRLRKDLKRTK-----ALLADAQLMLDHLKNSAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAME 1722
Cdd:pfam01576 279 ---DLESERAARNKAEKQRrdlgeELEALKTELEDTLDTTAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1723 VEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdlAQINDLQAQLEEANKEK 1802
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE-------GQLQELQARLSESERQR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1803 QELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEtrlefertqvKRLESLASRLKENMEKLTEERDQRIAAENR-- 1880
Cdd:pfam01576 429 AELAEKLSKLQSELESV------SSLLNEAEGKNIKLS----------KDVSSLESQLQDTQELLQEETRQKLNLSTRlr 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 1881 --EKEQNKrLQRQLRDTKEEMGELAR-------KEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1949
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 ... |
1256-1974 |
9.94e-21 |
|
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: 9.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1256 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTseLTDERNTGESASQLLDAETAERLRAE 1335
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1336 KEMKELQTQYDALKKQMEVMemevmearLIRAAEINGEVDDDDAGGEWRLKYERAVREvdfTKKRLQQEFEDKLEVEQQN 1415
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKE--------NKEEEKEKKLQEEELKLLAKEEEELKSELL---KLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREK 1495
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1496 LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1575
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1576 TIQMLEQAKLRLEMEMeRMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS 1652
Cdd:pfam02463 483 QEQLELLLSRQKLEER-SQKESKARSGLKVLLALikdGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1653 DQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLH--- 1729
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesa 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1730 ------------LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1797
Cdd:pfam02463 642 kakesglrkgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1798 ANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA 1877
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1878 ENRE--KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGdLQAAIEDEMESD 1955
Cdd:pfam02463 802 ELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL-LQELLLKEEELE 880
|
730
....*....|....*....
gi 1093953565 1956 ENEDLINSEGDSDVDSELE 1974
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 ... |
1532-1975 |
1.35e-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: 99.48 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1532 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS----------KE 1601
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1602 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTK 1674
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1675 ALLAD--AQL--------MLDHLKNSAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEE 1744
Cdd:pfam01576 159 ERISEftSNLaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1745 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVE-FLEQSM 1823
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1824 VDKSLVSRQEAKIRELETRLEFE-RTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGEL 1902
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1903 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIED---EMESDENEDLINSEGDSDVDSELED 1975
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQD 472
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1490-1949 |
1.59e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 99.37 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1490 KLQREKLQREKDMLLAEAfSLKQQLEEKDmdiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEE 1569
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTE-NIEELIKEKE-------KELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQagtIQMLEQAKLRLEmemERMRQTHS--KEMESRDEEVEEARQSCqKKLKQMEVQLEEEYEDKQKVLREKRELEGK 1647
Cdd:PRK03918 243 LEKE---LESLEGSKRKLE---EKIRELEEriEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1648 LATLSDQVN--RRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEseftcaaaVKARKAMEvEI 1725
Cdd:PRK03918 316 LSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTGL-TP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1726 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmKKHKAAVAQASRDLAQ------INDLQAQLEEAN 1799
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRELTEehrkelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1800 KEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEA---KIRELETRL-------------EFERT---------QVKRLE 1854
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeQLKELEEKLkkynleelekkaeEYEKLkekliklkgEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1855 SLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQ----LRDTKEEMGELA---RKEAEASRKKHELEMDLESLEaan 1927
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyNEYLELKDAEKELEREEKELK--- 622
|
490 500
....*....|....*....|..
gi 1093953565 1928 qSLQADLKLAFKRIGDLQAAIE 1949
Cdd:PRK03918 623 -KLEEELDKAFEELAETEKRLE 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1365-1958 |
3.73e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1365 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQEFEDKLEVEQQNKRQlERRLGDLQA 1428
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1429 DSEESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDMLLA 1505
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1506 EAfslkQQLEEKDMDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGTIQMLEQ 1582
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1583 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRrdFES 1662
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1663 EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEIEDLHLQidDIAKAKTAL 1742
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1743 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQS 1822
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1823 MVDKSlvsrqEAKIRELETRLEfERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGEl 1902
Cdd:PRK03918 586 SVEEL-----EERLKELEPFYN-EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE- 658
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1903 aRKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEdEMESDENE 1958
Cdd:PRK03918 659 -EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKE 712
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
462-580 |
5.38e-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: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 462 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNK---- 537
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 538 ---------VFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAG 580
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1534-1910 |
1.11e-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: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1534 ELQDISSQESKDEASLAK---VKKQLRDLEAKVkdqeEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1610
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEEleeVEENIERLDLII----DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1611 EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQlmldhlkns 1690
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE--------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1691 apskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1770
Cdd:TIGR02169 308 ----RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1771 MKKHKAAVaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQV 1850
Cdd:TIGR02169 384 RDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1851 KRLESLASRLKENMEKLTEERDQRiaaenreKEQNKRLQRQLRDTKEemgELARKEAEAS 1910
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQR---ELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1661-1991 |
1.33e-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: 96.66 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1661 ESEKRLRK---DLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAA-----AVKARKAMEVEIEDLHLQI 1732
Cdd:TIGR02168 176 ETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVlrleeLREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1733 DDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL----------MKKHKAAVAQASRDL----AQINDLQAQLEEA 1798
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrleqqKQILRERLANLERQLeeleAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1799 NKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEferTQVKRLESLASRLKENMEKLTEERDQRIAAE 1878
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEA------ELEELEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1879 NREKEQNKRLQRQLRDTKEEMGELARKE-AEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIeDEMESDEN 1957
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELA 485
|
330 340 350
....*....|....*....|....*....|....
gi 1093953565 1958 EDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPS 1991
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
432-1158 |
5.94e-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: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGP---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIIL 508
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 509 LGSSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQaGQVASASIQ 588
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 589 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLN--------HLAENNVFgivplakpEEKQKAAQQFSKLQAA 660
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 661 MKVLGISpdeqkacwF-----ILAAIYHLG----AAGATKEAAEAGRKQFarhewaQKAAYLLGCSleelSSAIFKhqhk 731
Cdd:cd14881 224 LGILGIP--------FldvvrVLAAVLLLGnvqfIDGGGLEVDVKGETEL------KSVAALLGVS----GAALFR---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 732 gGTLQRSTSFRQGPEESgLGDgtgPKLSALEClEGMAAGLYSELFTLLVSLVNrALKSSQHSLC------SMMIVDTPGF 805
Cdd:cd14881 282 -GLTTRTHNARGQLVKS-VCD---ANMSNMTR-DALAKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFGF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 806 QNPeqggsaRGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafdDLEPPTDDSVAAVDqashqsLVRSLaRT 885
Cdd:cd14881 355 EDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID------LISSL-RT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 886 dearGLLWLLEEEALVPGASEdtllerlfSYYGPQEGDKKgQSPLLHSSKPHH---FLLGHSHGTnwVEYNVTGWLnytk 962
Cdd:cd14881 419 ----GLLSMLDVECSPRGTAE--------SYVAKIKVQHR-QNPRLFEAKPQDdrmFGIRHFAGR--VVYDASDFL---- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 963 qnpatqnaprllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQMKLQVD 1042
Cdd:cd14881 480 -------------DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLD 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1043 ALIDTIKKSKLHFVHCflpvaegwageprsassrrvsssseldLPSGDHCEAGllQLDVPLLRTQLRGSRLLDAMRMYRQ 1122
Cdd:cd14881 516 NLLRTLVHARPHFVRC---------------------------IRSNTTETPN--HFDRGTVVRQIRSLQVLETVNLMAG 566
|
730 740 750
....*....|....*....|....*....|....*.
gi 1093953565 1123 GYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDER 1158
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1274-1898 |
7.10e-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: 93.88 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1274 EIQQLRSKLEK--AEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETaERLRAEKEM-------KELQTQ 1344
Cdd:TIGR00618 197 ELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLkqlrariEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKR---------------LQQEFEDKL 1409
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAahvkqqssieeqrrlLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1410 EVEQQNKRQ------------LERRLGDLQADSEESQRALQQLKKKCQRLTAE-------------LQDTKLHLEGQQVR 1464
Cdd:TIGR00618 356 HIRDAHEVAtsireiscqqhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrtsafrdLQGQLAHAKKQQEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1465 NHELEKKQRRFDSElsQAHEEAQREKLQREKLQ--REKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISS-- 1540
Cdd:TIGR00618 436 QQRYAELCAAAITC--TAQCEKLEKIHLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhp 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1541 -QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSC 1616
Cdd:TIGR00618 514 nPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNIT 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1617 QKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRK-DLKRTKALLADAQLMLDHLKNSAPSKR 1695
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1696 EIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1775
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1776 AAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFErTQVKRLES 1855
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE-TLVQEEEQ 832
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1093953565 1856 LASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEE 1898
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1254-1813 |
8.36e-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: 93.98 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1254 TVRPLIEVQLSEEQIRNKD--EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAER 1331
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1332 LRAEKEMKELQTQYDALKKQMEVMEMEVMEARLiRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLE- 1410
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKE-EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQg 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1411 ----------VEQQNKRQLERRLGD-LQA----DSEESQRALQQLK-KKCQRLT---------AELQDTKLHLEGQQ--- 1462
Cdd:TIGR02169 523 vhgtvaqlgsVGERYATAIEVAAGNrLNNvvveDDAVAKEAIELLKrRKAGRATflplnkmrdERRDLSILSEDGVIgfa 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1463 -----------------------VRNHELEKKQ-------------------------RRFDSELSQAHEEAQREKLQR- 1493
Cdd:TIGR02169 603 vdlvefdpkyepafkyvfgdtlvVEDIEAARRLmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLREr 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1494 -EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1572
Cdd:TIGR02169 683 lEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1573 QAGTIQMLEQ--AKLRLEMEMERMRQTHSKEMESRDE--EVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1648
Cdd:TIGR02169 763 LEARIEELEEdlHKLEEALNDLEARLSHSRIPEIQAElsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1649 ATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQLEESEftcaaavKARKAMEVEIED 1727
Cdd:TIGR02169 843 IDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRlGDLKKERDELEAQLRELE-------RKIEELEAQIEK 914
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1728 LHLQIDDIAKAKTALEEQLSRLQREKNEIQnrlEEDQEDMN-ELMKKHKAAVAQASRDLAQINDLQAQ-LEEANKEKQEL 1805
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE---EIPEEELSlEDVQAELQRVEEEIRALEPVNMLAIQeYEEVLKRLDEL 991
|
....*...
gi 1093953565 1806 QEKLQALQ 1813
Cdd:TIGR02169 992 KEKRAKLE 999
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1400-1905 |
8.72e-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: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1400 RLQQEFEDKLEVEQQNKRQLERR--LGDLQADSEESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1477
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQREKLQREKDMLLAEAFS--------LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASL 1549
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1550 AKVKKQLRDLEAKVKDQEEELDEQA----GTIQMLEQAKLRLEMEMERMRQTHSkemeSRDEEVEEARQSCQKKLKQME- 1624
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEIASLERRKS----NIPARLLALRDALAEALGLDEa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1625 --------VQLEEEYEDKQ----KVLR-EKREL---EGKLATLSDQVNRRDFesekRLRKDLKRTKALLADAQLMLDHlK 1688
Cdd:COG4913 459 elpfvgelIEVRPEEERWRgaieRVLGgFALTLlvpPEHYAAALRWVNRLHL----RGRLVYERVRTGLPDPERPRLD-P 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1689 NSAPSKREIAQ------LKNQLEES-EFTCAAAVKA----RKAMEVE-----IEDLHlQIDD--------------IAKA 1738
Cdd:COG4913 534 DSLAGKLDFKPhpfrawLEAELGRRfDYVCVDSPEElrrhPRAITRAgqvkgNGTRH-EKDDrrrirsryvlgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1739 KtALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA------------VAQASRDLAQINDLQAQLEEANKEKQELQ 1806
Cdd:COG4913 613 A-ALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1807 EKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFERTQVK----RLESLASRLKENMEKLTEERDQRIAAENREK 1882
Cdd:COG4913 692 EQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
570 580
....*....|....*....|...
gi 1093953565 1883 EQNKRLQRQLRDTKEEMGELARK 1905
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEE 788
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1265-1936 |
2.17e-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: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSE---LTDERNTGESASQLLDaETAERlRAEKEMKel 1341
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLK-ETCAR-SAEKTKK-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1342 qTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggEWRLKYERAVREVDFtkkRLQQEFEDKLEVEQQNKRQL-- 1419
Cdd:pfam05483 174 -YEYEREETRQVYMDLNNNIEKMILAFE------------ELRVQAENARLEMHF---KLKEDHEKIQHLEEEYKKEInd 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1420 ---------------ERRLGDLQADSEESQRALQQLKKKCQ--------------RLTAELQDTKLHLEGQQVRNHELEK 1470
Cdd:pfam05483 238 kekqvsllliqitekENKMKDLTFLLEESRDKANQLEEKTKlqdenlkeliekkdHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1471 KQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagftqkvvsLEAELQDISSQESKDEASLA 1550
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL-------------LRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1551 KVKKQLRDLE--AKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthSKEMESRDEEVEEARQSCQKKLKQMEVQLE 1628
Cdd:pfam05483 385 ELQKKSSELEemTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKI----AEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1629 EEYEDKQKVLREKRELEGKLatlsdqvnrrdfESEKrlrkdLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEse 1708
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED-- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1709 ftcaaaVKARKAMEveiEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1784
Cdd:pfam05483 522 ------IINCKKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1785 LAQINDLQAQLEEANKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELEtrLEFERTQVKRLESLASRLKE-- 1862
Cdd:pfam05483 593 ENKCNNLKKQIENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLE--LELASAKQKFEEIIDNYQKEie 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1863 ----NMEKLTEERDQRIA----AENREKEQNKRLQRQL------------------RDTKEEMGELARKEAEASRKKHEL 1916
Cdd:pfam05483 665 dkkiSEEKLLEEVEKAKAiadeAVKLQKEIDKRCQHKIaemvalmekhkhqydkiiEERDSELGLYKNKEQEQSSAKAAL 744
|
730 740
....*....|....*....|
gi 1093953565 1917 EMDLESLEAANQSLQADLKL 1936
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLEI 764
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
7.93e-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: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLRRTTMLDRGPegqacrrVVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 1093953565 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. ... |
1262-1973 |
2.37e-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: 89.02 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1262 QLSEEQIRNKDEEIQQLRSKLEKAEKERNELrLNSDRLESRISEltseltDERNTGESASQLLDAEtaeRLRAEKEMKEL 1341
Cdd:pfam15921 99 ELHEKQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRRESQSQE------DLRNQLQNTVHELEAA---KCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1342 QTQYDALKKQMEVMEMEVMEAR--LIRAAEINGE-VDDDDAGGEWRLK-----YERAVREVD----FTKKRLQqEFEDKL 1409
Cdd:pfam15921 169 NTQIEQLRKMMLSHEGVLQEIRsiLVDFEEASGKkIYEHDSMSTMHFRslgsaISKILRELDteisYLKGRIF-PVEDQL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1410 EV---EQQNK-----RQLERRLGDLQADSEESQRALQQlKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1472
Cdd:pfam15921 248 EAlksESQNKielllQQHQDRIEQLISEHEVEITGLTE-KASSARSQANSIQSQLEIIQEQARNQnsmymrqlsDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1473 RRFDSELSQAheeaqrEKLQREKLQR-EKDMLLAEAfSLKQQLEEKDMdiagFTQKVVSLEAELQDISSQESKDEASLAK 1551
Cdd:pfam15921 327 SQLRSELREA------KRMYEDKIEElEKQLVLANS-ELTEARTERDQ----FSQESGNLDDQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1552 VKKQLRDLeakvkdqeeeLDEQAGTiqmleqaklrlEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEY 1631
Cdd:pfam15921 396 EKEQNKRL----------WDRDTGN-----------SITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1632 EDKQKVLREKRELEGKLATLSDQVnrrdfESEKRLrkdLKRTKALLADAQLMLDHlknsapSKREIAQLKNQLEESE--- 1708
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKErai 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1709 -FTCAAAVKARKAMEVEIEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDL 1785
Cdd:pfam15921 513 eATNAEITKLRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 AQINDLQAQLE-EANKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETRL-EFERTQVKRLESLASRLKEn 1863
Cdd:pfam15921 586 GAMQVEKAQLEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARVsDLELEKVKLVNAGSERLRA- 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1864 MEKLTEERDQRI-------AAENREKEQNKRLQRQLRDTKEEMGELARK-EAEASRKKHELEM---DLESLEAAN----- 1927
Cdd:pfam15921 648 VKDIKQERDQLLnevktsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamk 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1928 --QSLQADLKLAFKRIGDLQAAI---EDEMESDENEDLINSEGDSDVDSEL 1973
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 |
2.74e-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: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGdFGFSLRRttmlDRGPEGQACRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06768 1 RLCHLVKGPEG-YGFNLHA----EKGRPGHFIREV----DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKA 69
|
....*....
gi 1093953565 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 ... |
432-614 |
4.80e-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: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 432 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIILL 509
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 510 GSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQAL---------------------YTLLEAFGNSPTIINGNATRF 568
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1093953565 569 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 614
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1260-1924 |
5.74e-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: 87.38 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESasqlLDAET---AERLRAEK 1336
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1337 EMK-ELQTQYDALKKQMEVMEMEVmearliraAEINGEVDdddaggewRLKYERAVREVDFTK-KRLQQEFEDKLEVEQQ 1414
Cdd:TIGR04523 117 EQKnKLEVELNKLEKQKKENKKNI--------DKFLTEIK--------KKEKELEKLNNKYNDlKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1415 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTaELQDTKLHLEGQqvrNHELEKKQRRFDSELSQAHEEAQREKLQRE 1494
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQ---NNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1495 KLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1569
Cdd:TIGR04523 257 QLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQAGTIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLA 1649
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1650 TLSDQVNRRD-----FESEKR-LRKDLKRTKALLADaqlmldhlknsapSKREIAQLKNQleeseftcaaavkarkamev 1723
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKElLEKEIERLKETIIK-------------NNSEIKDLTNQ-------------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1724 eIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdlaqindlqaQLEEANKEKQ 1803
Cdd:TIGR04523 449 -DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEKK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1804 ELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKR--LESLASRLKENMEKLTEERDQRIAAENR 1880
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1881 ------EKEQNKR---------------LQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLE 1924
Cdd:TIGR04523 587 kqelidQKEKEKKdlikeieekekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1478-1884 |
8.82e-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: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQR--EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1555
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthskEMESRDEEVEEARQScqkklkqmevqleeeyedKQ 1635
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL------EARLSHSRIPEIQAE------------------LS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1636 KVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLmldhlkNSAPSKREIAQLKNQLEEseftcaaav 1715
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKE------QIKSIEKEIENLNGKKEE--------- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1716 karkaMEVEIEDLHLQIDDiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMkkhkaavAQASRDLAQINDLQAQL 1795
Cdd:TIGR02169 866 -----LEEELEELEAALRD-------LESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELKAKL 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1796 EEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELE-----TRLEFERTQVKRLEslasrLKENMEKLTEE 1870
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDE-----LKEKRAKLEEE 1001
|
410
....*....|....*..
gi 1093953565 1871 RDQ---RIAAENREKEQ 1884
Cdd:TIGR02169 1002 RKAileRIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1413-1801 |
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 1093953565 1413 QQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQ 1492
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1493 REKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASlaKVKKQLRDLEAKVKDQEEELDE 1572
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS--KLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1573 QAGTIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLEE------EYEDKQKVLREKR-ELE 1645
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRI--------DLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERdELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1646 GKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEseftcaaAVKARKAMEVEI 1725
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-------VQAELQRVEEEI 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1726 EDLH----LQIDD---IAKAKTALEEQLSRLQREKNEIQNRLEE-DQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1797
Cdd:TIGR02169 968 RALEpvnmLAIQEyeeVLKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAINENFNEIFAELSGGTGELIL 1047
|
....
gi 1093953565 1798 ANKE 1801
Cdd:TIGR02169 1048 ENPD 1051
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1273-1935 |
1.60e-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: 85.84 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1273 EEIQQLRSKLEKAEKERNEL--RLNSDR------------LESRISELTSELTDERNTGESasqlLDAET---AERLRAE 1335
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLdkNLNKDEekinnsnnkikiLEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1336 KEMK-ELQTQYDALKKQMEVMEMEVmearliraAEINGEVDdddaggewRLKYERAVREVDFTK-KRLQQEFEDKLEVEQ 1413
Cdd:TIGR04523 116 KEQKnKLEVELNKLEKQKKENKKNI--------DKFLTEIK--------KKEKELEKLNNKYNDlKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1414 QNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTaELQDTKLHLEGQqvrNHELEKKQRRFDSELSQAHEEAQREKLQR 1493
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQ---NNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1494 EKLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEE 1568
Cdd:TIGR04523 256 NQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1569 ELDEQAGTIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1648
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1649 ATLSDQVNRRD-----FESEKR-LRKDLKRTKALLADaqlmldhlknsapSKREIAQLKNQleeseftcaaavkarkame 1722
Cdd:TIGR04523 401 QNQEKLNQQKDeqikkLQQEKElLEKEIERLKETIIK-------------NNSEIKDLTNQ------------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1723 veIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdlaqindlqaQLEEANKEK 1802
Cdd:TIGR04523 449 --DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1803 QELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKR--LESLASRLKENMEKLTEERDQRIAAen 1879
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKK-- 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1880 rekeqNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1935
Cdd:TIGR04523 584 -----QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1639-1980 |
1.81e-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: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1639 REKRELEGKLATLS--DQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcaAAVK 1716
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAV--------AQASRDLAQI 1788
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1789 NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFERTQVKRLESLASRL 1860
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1861 KENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1940
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1941 IGDLQA---AIEDEMESDENEdLINSE-----------GDSDVDSELEDRVDGV 1980
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-LAEAEaqaraseervrGGRAVEEVLKASIQGV 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1447-1947 |
4.75e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1447 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQ 1526
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1527 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1606
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1607 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQvnrrdfesekrlrKDLKRTKALLADAQLMLdh 1686
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1687 lknsapskrEIAQLKNQLEESEFTCAAAVKARKAMeveiedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1766
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1767 MNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1846
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1847 RTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQnkRLQRQLRDTKEEMGELARKEAEASRKKHELEMD--LESLE 1924
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 1093953565 1925 AANQSLQADLKLAFKRIGDLQAA 1947
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1256-1972 |
6.01e-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: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1256 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKER---------NELRLNSDRLESR---ISELTSELTD-ERNTGESASQ 1322
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfserqikNFHTLVIERQEDEaktAAQLCADLQSkERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1323 LLDAETA-------ERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1392
Cdd:TIGR00606 431 IRDEKKGlgrtielKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1393 -EVDFTKKRLQQEFE-----------------DKLEVEQQ--------------------NKRQLERRLGDLQADSEESQ 1434
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQirkiksrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1435 RALQQLKKKCQRLtaELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-EAQREKLQREKLQREKDMLLAEAFSLKQ- 1512
Cdd:TIGR00606 591 DRLAKLNKELASL--EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQf 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1513 --QLEEKDMDIAGFTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEME 1590
Cdd:TIGR00606 669 itQLTDENQSCCPVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1591 MERMR---QTHSKEMESRDEEVE-------------EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS-D 1653
Cdd:TIGR00606 746 IPELRnklQKVNRDIQRLKNDIEeqetllgtimpeeESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvQ 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1654 QVNRRDFESEKRLRK---DLKRTKALLADAQLMLDHLKNSApskreiaqlkNQLEESEFTCAAAVKARKAME-------V 1723
Cdd:TIGR00606 826 QVNQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsT 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1724 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDL--------------- 1785
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDIenkiqdgkddylkqk 975
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 -AQINDLQAQLEEANKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLasRLK 1861
Cdd:TIGR00606 976 eTELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMK 1053
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1862 ENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrKKHELEMDLESLEAANQSL--------QAD 1933
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAI 1131
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1093953565 1934 LKLAFKRIGDLQAAIEDEMESDEN-EDLINSEGDSDVDSE 1972
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 ... |
1330-1968 |
6.66e-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: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1330 ERLRAEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1403
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1404 EFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1483
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1484 EEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1563
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1564 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRE 1643
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1644 LEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREI-AQLKNQLEESEFTCAAAVKARK--A 1720
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGrIISAHGRLGDLGVAVENYKVAIstA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1721 MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDLAQINDLQAQLE 1796
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1797 EANKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRlefERTQVKRLESLASRLKENMEKLTEERDQRIA 1876
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELT---KELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1877 AENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDE 1956
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650
....*....|..
gi 1093953565 1957 NEDLINSEGDSD 1968
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 ... |
1258-1899 |
7.01e-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: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1258 LIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAErlraEKE 1337
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE----EKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1338 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFE--DKLEVEQQN 1415
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRL 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEEAQREKLQREK 1495
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1496 LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEE 1569
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQAGTIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLA 1649
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1650 TLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLH 1729
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1730 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA------QASRDLAQINDLQAQLEEANKEKQ 1803
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEekkeleEESQKLNLLEEKENEIEERIKEEA 927
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1804 ELQEKLQALQsqvefLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKE 1883
Cdd:pfam02463 928 EILLKYEEEP-----EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
650
....*....|....*.
gi 1093953565 1884 QNKRLQRQLRDTKEEM 1899
Cdd:pfam02463 1003 EKKKLIRAIIEETCQR 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1259-1802 |
9.07e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLES---------RISELTSELTDERNTGE-------SASQ 1322
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1323 LLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1402
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1403 QEFEDKLEVEQQnKRQLERRLGDLQADSEESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1479
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1480 SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMdiagfTQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1558
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL-----AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1559 LEAKVKDQEEELDEQagtiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1634
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1635 QKVLREKRELEGKLATLSDQvnRRDFESEKRLRKDLKRTkalLADAQLMLDHLKNSAPSKR-EIAQLKNQLEESEFTCAA 1713
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDA--EKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1714 AVKARKAMEV-----EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ--NRLEEDQEDMNELMKKHKAAVAQASrdLA 1786
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYKALLKERA--LS 743
|
570
....*....|....*..
gi 1093953565 1787 QINDLQAQL-EEANKEK 1802
Cdd:PRK03918 744 KVGEIASEIfEELTEGK 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1512-1957 |
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 1093953565 1512 QQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAsLAKVKKQLRDLE-----AKVKDQEEELDEQAGTIQmleqaklr 1586
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAER-YKELKAELRELElallvLRLEELREELEELQEELK-------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1587 lemEMERMRQTHSKEMESRDEEVEEARqscqkkLKQMEvqLEEEYEDKQKVL----REKRELEGKLATLSdqvnrrdfES 1662
Cdd:TIGR02168 250 ---EAEEELEELTAELQELEEKLEELR------LEVSE--LEEEIEELQKELyalaNEISRLEQQKQILR--------ER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1663 EKRLRKDLKRTKALLADAQLMLDHLK-NSAPSKREIAQLKNQLEeseftcaaavkarkameveiedlhlqiddiakaktA 1741
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAeELAELEEKLEELKEELE-----------------------------------S 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1742 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQ 1821
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETL----RSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1822 SMvdkslvsrQEAKIRELETRLEfertqvkrleslasRLKENMEKLTEERDQRIAAEnrekeqnKRLQRQLRDTKEEMGE 1901
Cdd:TIGR02168 429 KL--------EEAELKELQAELE--------------ELEEELEELQEELERLEEAL-------EELREELEEAEQALDA 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1902 LARKEAEASRKKHELEMDLESLEAANQSLQAdLKLAFKRIGDLQAAIEDEMESDEN 1957
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1259-1605 |
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 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNE-------LRLNSDRLESRISELTSELTDERNTGESASQLLDAETAER 1331
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1332 LRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQEFEDKLE 1410
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1411 VEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1490
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1491 LQREKLQREKDmllaeafSLKQQLEEKdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1564
Cdd:TIGR02168 929 LRLEGLEVRID-------NLQERLSEE-------------YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1565 --------DQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthSKEMESR 1605
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1266-1753 |
4.09e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.97 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELtseltderntgESASQLLDAEtAERLRAEKEMKELQTQY 1345
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----------EKLLQLLPLY-QELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1346 DALKKQMEVMEmevmearliraaeingevddddaggEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD 1425
Cdd:COG4717 149 EELEERLEELR-------------------------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1426 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQvrnhelekkqrrfdselsqaheeaqreklQREKLQREKDMLLA 1505
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-----------------------------LEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1506 EA-----FSLKQQLEEKDMDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1580
Cdd:COG4717 255 AAallalLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1581 EQAKL-RLEMEMERMRQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQV 1655
Cdd:COG4717 332 PDLSPeELLELLDRIEELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1656 NRR--------DFESEKRLRKDLKRTKALLADAQLMLDHLknsapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEI 1725
Cdd:COG4717 412 EELlgeleellEALDEEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAEL 485
|
490 500
....*....|....*....|....*...
gi 1093953565 1726 EDLHLQIDDIAKAKTALEEQLSRLQREK 1753
Cdd:COG4717 486 RELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1426-1871 |
9.74e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.81 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1426 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheEAQREKLQREKLQREKdmlLA 1505
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREELEKLEK---LL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1506 EAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEskdeaslakvkKQLRDLEAKVKDQEEELDEQagtiqmLEQAKL 1585
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELE-----------EELEELEAELAELQEELEEL------LEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1586 RLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMEVQLEEeYEDKQKVLREKRELEGK------------------ 1647
Cdd:COG4717 189 ATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEArlllliaaallallglgg 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1648 ------------------LATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLK-----NSAPSKREIAQLKNQL 1704
Cdd:COG4717 267 sllsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalglPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1705 EESEFTCAAAVKARKamEVEIEDLHLQIDDI-AKAKTALEEQLSRL---QREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1780
Cdd:COG4717 347 EELQELLREAEELEE--ELQLEELEQEIAALlAEAGVEDEEELRAAleqAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1781 ASRD--LAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkSLVSRQEAKIRELETRLEFERTQVKRLESLAS 1858
Cdd:COG4717 425 LDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEED----GELAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 1093953565 1859 RLKENMEKLTEER 1871
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1269-1856 |
1.04e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.08 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1269 RNKDEEIQQLRSKLEkaEKERNEL--RLNSdrLESRISELTSELTDERNTGESASQLLDaETAERLraeKEMKELQTQYD 1346
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLheRLNG--LESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1347 ALKkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFED---KLEVEQQNKRQLERRL 1423
Cdd:PRK02224 255 TLE------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1424 GDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDml 1503
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE-- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1504 laeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGT 1576
Cdd:PRK02224 395 -----ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1577 IQMLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkvLREKRELEGKLatLSDQVN 1656
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEEL--IAERRE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1657 RRDfesEKRLRKDLKRTKAlladaqlmlDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-------IEDLH 1729
Cdd:PRK02224 531 TIE---EKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1730 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDLAQINDLQAQLEEankEKQELQEK 1808
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREE 675
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1093953565 1809 LQALQSQVEFLEQSMvdkslvsrqeAKIRELETRLEFERTQVKRLESL 1856
Cdd:PRK02224 676 RDDLQAEIGAVENEL----------EELEELRERREALENRVEALEAL 713
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1260-1810 |
1.10e-14 |
|
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: 80.16 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKE-RNELRLNSDRLESRISELTSELTderntgESASQLLDAETaERLRAEKEM 1338
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQlRSELREAKRMYEDKIEELEKQLV------LANSELTEART-ERDQFSQES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1339 KELQTQYdalkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERavREVDFTKKRLQQEFEDKLEVEQQNKRQ 1418
Cdd:pfam15921 373 GNLDDQL-----QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR--RELDDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1419 LERRLGDLQADSEESQRA------LQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEEAQR 1488
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVssltaqLESTKEMLRKVVEELTAKKMTLESSERTvsdlTASLQEKERAIEATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1489 EKLQREKLQR---EKDMLL---AEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAK 1562
Cdd:pfam15921 526 VDLKLQELQHlknEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1563 VKDQEEELDEQAGTIQMLEQAKLRLEMEM--------ERMRQTHSKEMEsRDEEVEEARqSCQKKLKQmevqLEEEYEDK 1634
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKvklvnagsERLRAVKDIKQE-RDQLLNEVK-TSRNELNS----LSEDYEVL 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1635 QKVLREKRElEGKLATlsdqvnrrdfeseKRLRKDLKRTKAlladaqlmldhlknsapskrEIAQLKNQLEESEFTCAAA 1714
Cdd:pfam15921 680 KRNFRNKSE-EMETTT-------------NKLKMQLKSAQS--------------------ELEQTRNTLKSMEGSDGHA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1715 VKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSR-------LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ 1787
Cdd:pfam15921 726 MKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
570 580
....*....|....*....|...
gi 1093953565 1788 INDLQAQLEEANKEKQELQEKLQ 1810
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQ 828
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1312-1902 |
3.17e-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: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1312 DERNTGESASQLLDaETAERLRAEKEMKELQTQYDALKKqmevmeMEVMEARLIRAAEINGEVDDDDAggewRLKYERAV 1391
Cdd:COG4913 219 EEPDTFEAADALVE-HFDDLERAHEALEDAREQIELLEP------IRELAERYAAARERLAELEYLRA----ALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1392 REVDFTKKRLQQEfEDKLEVEQQNKRQLERRLGDLQADSEESQRA--------LQQLKKKCQRLTAELQDTKLHLEGQQV 1463
Cdd:COG4913 288 RRLELLEAELEEL-RAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1464 R----NHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDIs 1539
Cdd:COG4913 367 LlaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1540 sqeskdeasLAKVKKQLRDLEA---------KVKDQEEE--------LDEQAGTI-----------QMLEQAKLRLEMEM 1591
Cdd:COG4913 446 ---------RDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervLGGFALTLlvppehyaaalRWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1592 ERMRQTHSKEMESRDEE------------------------------VEEARQ----------SCQKKL------KQMEV 1625
Cdd:COG4913 517 ERVRTGLPDPERPRLDPdslagkldfkphpfrawleaelgrrfdyvcVDSPEElrrhpraitrAGQVKGngtrheKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEY------EDKQKVLREKR-ELEGKLATLSDQVNRRdfeseKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIA 1698
Cdd:COG4913 597 RIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1699 QLKNQ---LEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnelmkkhk 1775
Cdd:COG4913 672 ELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------------- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1776 aavAQASRDLAQINDLQAQLEEANKEKQE------LQEKLQALQSQVEFLEQSMVDK--SLVSRQEAKIRELETRLEFER 1847
Cdd:COG4913 739 ---AEDLARLELRALLEERFAAALGDAVErelrenLEERIDALRARLNRAEEELERAmrAFNREWPAETADLDADLESLP 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1848 TQVKRLESL-ASRLKENMEKLteeRDQRIAAENREKEQ-NKRLQRQLRDTKEEMGEL 1902
Cdd:COG4913 816 EYLALLDRLeEDGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1390-1925 |
5.61e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1390 AVREVDFTKKRLQQEFEDklEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1469
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1470 kkqrrfdsELSQAHEEAQREKLQREklqREKDMLLAEAFSLKQQLEEkdmdiagftqkvvsLEAELQDISSQESKDEASL 1549
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1550 AKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQaklrlemEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLEE 1629
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNE-------EAESLRED-ADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1630 EYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSApskREIAQLKNQ------ 1703
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE-LREERDELREREAELEATLRTARERV---EEAEALLEAgkcpec 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1704 ---LEESEFTCAAAVK--ARKAMEVEIEDLHLQIDDI------AKAKTALEEQLSRLQREKNEIQ-------NRLEEDQE 1765
Cdd:PRK02224 458 gqpVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVeerlerAEDLVEAEDRIERLEERREDLEeliaerrETIEEKRE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1766 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdKSLVSRQEAKIRELETRLEf 1845
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI---RTLLAAIADAEDEIERLRE- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1846 ertqvkRLESLASRLKENMEKLTEERDQR--IAAENRE------KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE 1917
Cdd:PRK02224 614 ------KREALAELNDERRERLAEKRERKreLEAEFDEarieeaREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
....*...
gi 1093953565 1918 MDLESLEA 1925
Cdd:PRK02224 688 NELEELEE 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1694-1874 |
6.83e-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: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1773
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 --------------HKAAVAQASRDL-----------AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KS 1827
Cdd:COG4942 113 lyrlgrqpplalllSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAAlEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1828 LVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQR 1874
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1736-1965 |
7.74e-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: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1736 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1815
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1816 VEFLEQ---SMVDKSLVSRQEAKIREL---ETRLEFERTqVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQ 1889
Cdd:COG4942 99 LEAQKEelaELLRALYRLGRQPPLALLlspEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1890 RQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEG 1965
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 ... |
1265-1746 |
1.28e-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: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDernTGESASQLldaETAERLrAEKEMKELQTQ 1344
Cdd:pfam01576 628 EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDD---VGKNVHEL---ERSKRA-LEQQVEEMKTQ 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKKQMEVMEMevmeARL-----IRAAEINGEVD---DDDAGGEWRLKYERAVREvdftkkrLQQEFEDKLEVEQQ-- 1414
Cdd:pfam01576 701 LEELEDELQATED----AKLrlevnMQALKAQFERDlqaRDEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQav 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1415 -NKRQLERRLGDLQADSEESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEA 1486
Cdd:pfam01576 770 aAKKKLELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDL 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1487 QREKLQREKLQREKDmllaeafslkqqleekdmdiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQ 1566
Cdd:pfam01576 850 AASERARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQL 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1567 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKVLREKRELE 1645
Cdd:pfam01576 895 EEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALE 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1646 GKLATLSDQVnrrdfESEKRLR----KDLKRTKALLADAQLMLDHLKNSAPSKREIA--------QLKNQLEESEFTCAA 1713
Cdd:pfam01576 974 AKIAQLEEQL-----EQESRERqaanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASR 1048
|
490 500 510
....*....|....*....|....*....|...
gi 1093953565 1714 AVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1746
Cdd:pfam01576 1049 ANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1397-1956 |
2.32e-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: 75.78 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1397 TKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEES---QRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHEL 1468
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1469 EKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQ--LEEKDMDIAGFTQKVVSLEAELQDISSQESKDE 1546
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1547 ASLAKVKKQLRDLEAKVK---DQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQM 1623
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1624 EVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRL-------RKDLKRTKALLADAQLMLDHLKNSAPSKR- 1695
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRg 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1696 --EIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKK 1773
Cdd:TIGR00618 534 eqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 HKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ--------------------- 1832
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrqlalqkmqseke 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1833 ------------EAKIRELETRLEFERTQVKRLESLASRLKENME-----------KLTEERDQRIAAENREKEQN---- 1885
Cdd:TIGR00618 691 qltywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAaredalnqslkELMHQARTVLKARTEAHFNNneev 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1886 --------------KRLQRQLRDTKEEMGELARKEAE--ASRKKHELEMDLESLEAANQSLQADLKLAFKriGDLQAAIE 1949
Cdd:TIGR00618 771 taalqtgaelshlaAEIQFFNRLREEDTHLLKTLEAEigQEIPSDEDILNLQCETLVQEEEQFLSRLEEK--SATLGEIT 848
|
....*..
gi 1093953565 1950 DEMESDE 1956
Cdd:TIGR00618 849 HQLLKYE 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1266-1750 |
2.63e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntGESASQLLDAETAERLRAEKEMKELQTQY 1345
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1346 DALKKQMEVMEMEVMEARLIRAAEingevDDDDAGGEWRLKYERAVREVDFTKKRLqQEFEDKLEVEQQNKRQLERRLGD 1425
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDAD-----DLEERAEELREEAAELESELEEAREAV-EDRREEIEELEEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1426 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDS----ELSQAHEEAQR-EKLQREKLQREK 1500
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARER---VEEAEALLEAgkcpECGQPVEGSPHvETIEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1501 dmLLAEAFSLKQQLEEKDMDIagftqkvvsleAELQDISSQESKDEaslaKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1580
Cdd:PRK02224 480 --LEAELEDLEEEVEEVEERL-----------ERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1581 EQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------EEYEDKQKVLREKRElegKL 1648
Cdd:PRK02224 543 RERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiADAEDEIERLREKRE---AL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1649 ATLSDQvnRRDFESEKRLRK-------DLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavKARKAM 1721
Cdd:PRK02224 619 AELNDE--RRERLAEKRERKreleaefDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ----------AEIGAV 686
|
490 500
....*....|....*....|....*....
gi 1093953565 1722 EVEIEDLhlqiDDIAKAKTALEEQLSRLQ 1750
Cdd:PRK02224 687 ENELEEL----EELRERREALENRVEALE 711
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1266-2015 |
2.78e-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: 75.65 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAErLRAEKEMkELQTQY 1345
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE-KRDELNG-ELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1346 DALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVD-FTKK--RLQQEFED-KLEVEQQNKRQLER 1421
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKhqDVTAKYNRrRSKIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1422 RLGDLQADSEESQRALQQLKKKCQRLTAELqdtklhlegqqvrNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKD 1501
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEDDLQALESEL-------------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1502 MLLaeafslkqQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE-------QA 1574
Cdd:pfam12128 462 LLL--------QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpQA 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1575 GTIQmleqAKLRLEMEM--ERMRQTHSKEMESR---DEEVEEARQSCQKKLKQMEVQLEE----EYEDKQKVLREKRE-L 1644
Cdd:pfam12128 534 GTLL----HFLRKEAPDweQSIGKVISPELLHRtdlDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLDkA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1645 EGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAqlmLDHLKNSapsKREIAQLKNQLEESEFTCAAAVKARKAMEVE 1724
Cdd:pfam12128 610 EEALQSAREKQAAAE-EQLVQANGELEKASREETFA---RTALKNA---RLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 iedlhlQIDDIAKAKTALEeqlsrlqrekNEIQNRLEEDQEDMNElmkkHKAAVAQASRDLaqINDLQAQLEEANKEKQE 1804
Cdd:pfam12128 683 ------RLNSLEAQLKQLD----------KKHQAWLEEQKEQKRE----ARTEKQAYWQVV--EGALDAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1805 LQEKLQALQSQVEF-----LEQSMVDKSLVSRQEAKIRELETRLEfertQVKRLESLASRLKENMEKLTEERDQRIAAEN 1879
Cdd:pfam12128 741 RRSGAKAELKALETwykrdLASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRYFDWYQETWLQRRPRLATQL 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1880 REKEQNkrlQRQLRDtkeemgELARKEAEASRKKHELEMDLESLEAANQSLQADLklafKRIGDLQAAIEDEMESDENED 1959
Cdd:pfam12128 817 SNIERA---ISELQQ------QLARLIADTKLRRAKLEMERKASEKQQVRLSENL----RGLRCEMSKLATLKEDANSEQ 883
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1960 LinsegdsdvDSELEDRVDGVKSWLSKNKGPSKAAS-----DDGSLKS---SSPTSYWKSLAPD 2015
Cdd:pfam12128 884 A---------QGSIGERLAQLEDLKLKRDYLSESVKkyvehFKNVIADhsgSGLAETWESLREE 938
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1723-1884 |
6.24e-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: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1723 VEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASrdlAQINDLQAQLEEAN 1799
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1800 KEKQelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAEN 1879
Cdd:COG1579 87 NNKE-----YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 1093953565 1880 REKEQ 1884
Cdd:COG1579 156 AELEE 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1479-1681 |
8.26e-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: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1479 LSQAHEEAQREKlQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1558
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1559 LEAKVKDQEEELDEQAGTIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1631
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1632 EDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQ 1681
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1709-1929 |
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 1093953565 1709 FTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQI 1788
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1789 NDLQAQLEEankEKQELQEKLQALQ---------------SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRL 1853
Cdd:COG4942 93 AELRAELEA---QKEELAELLRALYrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1854 ESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQS 1929
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1441-1983 |
3.88e-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: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1441 KKKCQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQAHEEAQREKLQREKLQREKDMLLAEafsLKQQL 1514
Cdd:pfam12128 217 RLNRQQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1515 EEKDMDIagftqkvvsleaelqdissQESKDEASLakvkkQLRDLEAKVKDQEEEL---DEQAGTIQMLEQAKLRLEMEM 1591
Cdd:pfam12128 293 RTLDDQW-------------------KEKRDELNG-----ELSAADAAVAKDRSELealEDQHGAFLDADIETAAADQEQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1592 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFES-EKRLRKDL 1670
Cdd:pfam12128 349 LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1671 KRTKALLADAQLM----LDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQL 1746
Cdd:pfam12128 429 EAGKLEFNEEEYRlksrLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1747 SRLQREK---NEIQNRLEEDQE-------DMNELMKKHKAAVAQ-----ASRDLAQINDLQAQLEEANKeKQELQeklqa 1811
Cdd:pfam12128 506 EALRQASrrlEERQSALDELELqlfpqagTLLHFLRKEAPDWEQsigkvISPELLHRTDLDPEVWDGSV-GGELN----- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1812 LQSQVEFLEQSMVDKSLVSRQEAKIR--ELETRLEFERTQVKRLESLASRLKENMEKLT-EERDQRIAAENREKEQnKRL 1888
Cdd:pfam12128 580 LYGVKLDLKRIDVPEWAASEEELRERldKAEEALQSAREKQAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1889 ---QRQLRDTKEEMGELARKEAEASRKK--HELEMDLESLEAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINS 1963
Cdd:pfam12128 659 fdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKHQAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLKA 736
|
570 580
....*....|....*....|
gi 1093953565 1964 EGDSdVDSELEDRVDGVKSW 1983
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 |
4.88e-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: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGdFGFSLRRT---------TMLDRGPEGQACRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSR 289
Cdd:cd06746 7 RTVVLQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASH 79
|
90
....*....|....*...
gi 1093953565 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06746 80 EQVVNLIRQSGNTLVLKV 97
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1260-1880 |
5.81e-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: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRN-KDEEIQQLRSKLEKAEKERNELRLNSDRL--------------ESRISELTSELTD--ERNTGESASQ 1322
Cdd:pfam12128 323 ELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdvtakyNRRRSKIKEQNNRdiAGIKDKLAKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1323 lldAETAERLRAEKEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKK 1399
Cdd:pfam12128 403 ---REARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1400 RLQQEFedkleveqQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRfDSEL 1479
Cdd:pfam12128 479 EQEAAN--------AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP-DWEQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1480 SQAhEEAQREKLQREKLQREKDMLLAEA----FSLKQQLEEkdMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1555
Cdd:pfam12128 550 SIG-KVISPELLHRTDLDPEVWDGSVGGelnlYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ 1635
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1636 KVLREkrelegklATLSDQVNRRDFESEKRLRkdLKRTKALLADAQlmldhlknsAPSKREIAQLKNQLEESEFTCAAAV 1715
Cdd:pfam12128 707 EQKRE--------ARTEKQAYWQVVEGALDAQ--LALLKAAIAARR---------SGAKAELKALETWYKRDLASLGVDP 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1716 KARKAMEVEIEDLHLQIDDIAKAKTALEE----QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDL 1791
Cdd:pfam12128 768 DVIAKLKREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEME 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1792 QAQLEEANKEKQELQEKLQALQSQVEFLeqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1871
Cdd:pfam12128 848 RKASEKQQVRLSENLRGLRCEMSKLATL-----------KEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
....*....
gi 1093953565 1872 DQRIAAENR 1880
Cdd:pfam12128 917 KNVIADHSG 925
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1264-1490 |
8.72e-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: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1264 SEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELtderntgESASQLLDAETAERLRAEKEMKELQT 1343
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1344 QYDALKKQmevmemevmEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDftKKRLQQEFEDKLEVEQQN 1415
Cdd:COG4942 98 ELEAQKEE---------LAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1416 KRQLERR--LGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1490
Cdd:COG4942 167 AELEAERaeLEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1274-1811 |
9.03e-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: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1274 EIQQLRSKLEKAEKERNELRLNSDR----LESRISELTSELTDERNTGE------SASQLLDAETAERLRAEKEMKELQT 1343
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRarieLEKKASALKRQLDRESDRNQelqkriRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1344 QY-DALKKQMEVMEMEVMEARLIRAAeINGEVddddagGEWRLKYERAVREVDFTKKRLQqEFEDKLEVEQQNKRQLERR 1422
Cdd:pfam05557 83 KYlEALNKKLNEKESQLADAREVISC-LKNEL------SELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1423 LGDLQADSEESQRALQQLKKKCQRLTAELQDTKL--HLEGQQVRNHELEKKQRRFDSELSQAHE--------EAQREKLQ 1492
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvkNSKSELARIPELEKELERLREHNKHLNEnienklllKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1493 ReKLQREKDMLlAEAFSL---KQQLEEK-------DMD--------------IAGFTQKVVSLEAELQDISSQESKDEAS 1548
Cdd:pfam05557 235 R-KLEREEKYR-EEAATLeleKEKLEQElqswvklAQDtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1549 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSC 1616
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1617 QKKLKQMEVQLEeeyedkqKVLREKRELEGKLATLSDQVnrrdfesekrlrkDLKRTKALLADaqlmldhlknSAPSKRE 1696
Cdd:pfam05557 393 QAHNEEMEAQLS-------VAEEELGGYKQQAQTLEREL-------------QALRQQESLAD----------PSYSKEE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1697 IAQLKNQLEESEFTCAAAVKARKAMEVEIED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE 1762
Cdd:pfam05557 443 VDSLRRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKK 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1763 DQEDMNELMKKHKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQA 1811
Cdd:pfam05557 523 LEDDLEQVLRLPETTSTMNFK---EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1402-1823 |
1.20e-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: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1402 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRrfdsELSQ 1481
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE-------ELEEKYK----ELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1482 AHEEaqreklqrekLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEA 1561
Cdd:pfam07888 109 SSEE----------LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1562 KVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDeeveearqSCQKKLKQMEVQLEEEYEDKQKVLREK 1641
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT--------TAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1642 RELEGKLATLSDQVNRRDfesekrlrkdlkRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAAVKA-RKA 1720
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRD------------RTQAELHQARLQAAQLTL------QLADASLALREGRARWAQERETlQQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1721 MEVEIEDLHLQIDDIAKAKTALEEQlsRLQREKNEIqnrleedqedmnELMKKHKAAVAQASRDLAQINDLQAQLEEANK 1800
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEE--RMEREKLEV------------ELGREKDCNRVQLSESRRELQELKASLRVAQK 378
|
410 420
....*....|....*....|...
gi 1093953565 1801 EKQELQEKLQALQSQVEFLEQSM 1823
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 |
1.59e-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: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 218 LRELELQRRPTGdFGFSLRRTTMLDRGPEgqacrrVVHFAEPGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:smart00228 2 PRLVELEKGGGG-LGFSLVGGKDEGGGVV------VSSVVPGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLK 71
|
90
....*....|..
gi 1093953565 298 QSGDSVRLKVQP 309
Cdd:smart00228 72 KAGGKVTLTVLR 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1731-1964 |
1.95e-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: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1731 QIDDIAKAK-----TALEEQ--LSRLQREKNEIQNRLEEDQEDM-------NELMK-----KHKAAVAQASRDL------ 1785
Cdd:TIGR02168 145 KISEIIEAKpeerrAIFEEAagISKYKERRKETERKLERTRENLdrledilNELERqlkslERQAEKAERYKELkaelre 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 --------------AQINDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLVSRQE------AKIRELETRL 1843
Cdd:TIGR02168 225 lelallvlrleelrEELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEEEIEELQKelyalaNEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1844 EFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1923
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1093953565 1924 EAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 1964
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1588-1928 |
2.63e-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: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1588 EMEMERMRQTH---SKEMESRD--EEVEEARQScqkklkQMEVQLEEEYEDKQKVLREKRELEgklaTLSDQVNRRDFES 1662
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQA------EMDRQAAIYAEQERMAMERERELE----RIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1663 --EKRLRKDLKRTKALladAQLMLDHLKNSAPSKREI-AQLKNQLEESEftcaaavKARKAMEVEIEDLHLQiddiAKAK 1739
Cdd:pfam17380 365 irQEEIAMEISRMREL---ERLQMERQQKNERVRQELeAARKVKILEEE-------RQRKIQQQKVEMEQIR----AEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1740 TALEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdlaQINDLQAQLEEANKEKQELqEKLQALQSQVEFL 1819
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMVDKSLVSRQEAKIRELETRLEFERtqvkrleslasRLKENMEKLTEERDQRIAAENREKEQN----KRLQRQLRDT 1895
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|....*
gi 1093953565 1896 KEEMGEL--ARKEAEASRKKHELEMDLESLEAANQ 1928
Cdd:pfam17380 562 TEERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1739-1954 |
3.76e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.16 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1739 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMkkhkaavaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEf 1818
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN--------------EEYNELQAELEALQAEIDKLQAEIAEAEAEIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1819 LEQSMVDKSLVS--RQEAKIRELETRLEfertqVKRLESLASRLkENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTK 1896
Cdd:COG3883 83 ERREELGERARAlyRSGGSVSYLDVLLG-----SESFSDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 1897 EemgELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES 1954
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 ... |
1385-1937 |
6.06e-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: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1385 LKYERAVREVDFTKKRLQQEfedKLEVEQQNKRQLERRLGDLQaDSEESQRALQQL----KKKCQRLTAELQDTKLHLEG 1460
Cdd:pfam10174 41 LKKERALRKEEAARISVLKE---QYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1461 QQVRNHELEKKQRRFDSELSQAHEE------AQREKL--QREKLQREKDMLLAEAFSLKQQLEEKDMD--IAGFTQKVVS 1530
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1531 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1610
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1611 --EARQSCQKKLKQMEVQLEEEYEDKQKvlrEKRELEGKLATLSDQV--NRRDFE--------SEKR----------LRK 1668
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQNsdCKQHIEvlkesltaKEQRaailqtevdaLRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1669 DLKRTKALLADAQLMLDHLKNSAPSKR-EIAQLKNQLEeseftcaaaVKARKAMEVE--IEDLHLQIDDIAKAKTALEEQ 1745
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAgEIRDLKDMLD---------VKERKINVLQkkIENLQEQLRDKDKQLAGLKER 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1746 LSRLQREKNEIQNRL---EE---DQEDMNELMKKHKAAVAQASRDlaqindlqaQLEEANKEKQELQEKLQALQSQVEFL 1819
Cdd:pfam10174 424 VKSLQTDSSNTDTALttlEEalsEKERIIERLKEQREREDRERLE---------ELESLKKENKDLKEKVSALQPELTEK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMVD-----KSLVSR---QEAKIRELETRLEFERTQVKRLESLASRLKEnmekltEERDQRIAAENREKEQNkrLQRq 1891
Cdd:pfam10174 495 ESSLIDlkehaSSLASSglkKDSKLKSLEIAVEQKKEECSKLENQLKKAHN------AEEAVRTNPEINDRIRL--LEQ- 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1892 lrdtkeemgELARKEAEASRKKHELEMDLESL-EAANQSLQADLKLA 1937
Cdd:pfam10174 566 ---------EVARYKEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1413-1636 |
1.07e-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: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1413 QQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheEAQREKLQ 1492
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1493 REKLQREKDM--LLAEAFSLKQQLEEKD-MDIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEE 1569
Cdd:COG4942 97 AELEAQKEELaeLLRALYRLGRQPPLALlLSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQAGTIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQK 1636
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1931 |
1.17e-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: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1726 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdlaQINDLQAQLEEANKEKQEL 1805
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1806 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFERT-------QVKRLESLASRLKENMEKLT 1868
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1869 EERDQRIAAENRE-KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQ 1931
Cdd:COG3206 312 QRILASLEAELEAlQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1265-1728 |
1.56e-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: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKD-EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDE-----------RNTGESASQLLDAETAERL 1332
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1333 RAEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1385
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1386 ---------KYERAVRE-VDFTKKRLQQEFE--------------------DKLEVEQQN-----KRQLERRLGDLQADS 1430
Cdd:COG4913 487 faltllvppEHYAAALRwVNRLHLRGRLVYErvrtglpdperprldpdslaGKLDFKPHPfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1431 EEsqralqQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEEAQREKLQR 1493
Cdd:COG4913 567 PE------ELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1494 EKLQRekdmlLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1573
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1574 AGTIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKVLREKRE-LEGKLATLS 1652
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1653 DQVNR------RDFESEKRlrkDLKRTKALLADAQLMLDHLKNSA-PSKRE-IAQLKNQLEESEFT--CAAAVKARKAME 1722
Cdd:COG4913 787 EELERamrafnREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
....*.
gi 1093953565 1723 VEIEDL 1728
Cdd:COG4913 864 ERIDPL 869
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1251-1953 |
1.67e-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: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1251 LFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEKA--------EKERNELRLNS--DRLESRISELTSELtDERN--TGE 1318
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhlNLVQTALRQQEkiERYQEDLEELTERL-EEQEevVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1319 SASQLLDAEtAERLRAEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVD-DDDAGGEWrlkyera 1390
Cdd:COG3096 373 AAEQLAEAE-ARLEAAEEEVDSLKSQladyqqaLDVQ--QTRAIQYQQAVQALEKARALCGLPDlTPENAEDY------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1391 vrevdftkkrlQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKkcqrLTAELQDTKLHLEGQQV-RNHELE 1469
Cdd:COG3096 443 -----------LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK----IAGEVERSQAWQTARELlRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1470 KKQRRFDSELSQAHEEAQREKLQREKLQRekdmlLAEAF--SLKQQLEEKDMdiagFTQKVVSLEAELQDISSQESKDEA 1547
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAER-----LLEEFcqRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 SLAKVKKQLRDLEAKVKdqeeELDEQAGTIQMLEQAKLRLememermrQTHSKEMESRDEEVEEARQSCQKKLKQMEVQL 1627
Cdd:COG3096 579 QRSELRQQLEQLRARIK----ELAARAPAWLAAQDALERL--------REQSGEALADSQEVTAAMQQLLEREREATVER 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1628 EEEYEDKQKVLREKREL-------EGKLATLSDQVN-------RRDFESEKR---------LRK-----DLKRTKALLAD 1679
Cdd:COG3096 647 DELAARKQALESQIERLsqpggaeDPRLLALAERLGgvllseiYDDVTLEDApyfsalygpARHaivvpDLSAVKEQLAG 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1680 AQLMLDHL----------KNSAPSKRE-----IAQLKN-QLEESEFTcAAAVKARKAMEVEIEDLHLQIDDIAK--AKTA 1741
Cdd:COG3096 727 LEDCPEDLyliegdpdsfDDSVFDAEEledavVVKLSDrQWRYSRFP-EVPLFGRAAREKRLEELRAERDELAEqyAKAS 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1742 L----------------------------EEQLSRLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLAQINDLQA 1793
Cdd:COG3096 806 FdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQ----EQQLRQQLDQLKEQLQLLNKLLP 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1794 QLEEANKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL----------EFERTQVKRLESLASRLKEN 1863
Cdd:COG3096 882 QANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLVavlqsdpeqfEQLQADYLQAKEQQRRLKQQ 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1864 MEKLTEERDQR----------IAAENRekEQNKRLQRQLRDTKEEMGElARKEAEASRKKH-ELEMDLESLEAANQSLQA 1932
Cdd:COG3096 957 IFALSEVVQRRphfsyedavgLLGENS--DLNEKLRARLEQAEEARRE-AREQLRQAQAQYsQYNQVLASLKSSRDAKQQ 1033
|
810 820
....*....|....*....|.
gi 1093953565 1933 DLKLAFKRIGDLQAAIEDEME 1953
Cdd:COG3096 1034 TLQELEQELEELGVQADAEAE 1054
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1266-1882 |
1.74e-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: 67.00 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEE-IQQLRSKLEKAEKERNELRLNSD--RLESRISELTSELTDERNTGESASQLLDaETAErlrAEKEmkelQ 1342
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1343 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQEFEDKLEVEQQNKRQLEr 1421
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1422 rlgdlqadseesQRALQQLKKKCQRLTAELQDTKLhlegQQVRNHELEKKQRRF-DSELSQAHEEAQREKLQREKLQREK 1500
Cdd:TIGR01612 1278 ------------TFNISHDDDKDHHIISKKHDENI----SDIREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1501 DMLLAEAFSLKQQLEEKDM-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1573
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1574 AGTIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEG 1646
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1647 KLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEE--SEFTCAAAVKARKAMEVE 1724
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEIK 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAqleeaNK 1800
Cdd:TIGR01612 1576 KEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSI-----DS 1640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1801 EKQELQEKLQALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENR 1880
Cdd:TIGR01612 1641 QDTELKENGDNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
..
gi 1093953565 1881 EK 1882
Cdd:TIGR01612 1714 EE 1715
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1626-1972 |
2.51e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQlmldhlknsapskREIAQLKNQLE 1705
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1706 ESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1785
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1865
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1866 KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1945
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340
....*....|....*....|....*..
gi 1093953565 1946 AAIEDEMESDENEDLINSEGDSDVDSE 1972
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLE 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1260-1538 |
2.53e-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: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAE---- 1335
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskl 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1336 -KEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqEFEDKLEVEQQ 1414
Cdd:TIGR02169 804 eEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1415 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEEAQREK 1490
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealEEELSEIEDPKGEDEEIPEEELSLED 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1491 LQREKLQREKDMLLAEAFSLK--QQLEEKDMDIAGFTQKVVSLEAELQDI 1538
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1527-1933 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1527 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgtiqmleQAKLRLEMEMERMRQTHSKEMESRD 1606
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1607 EEVEEARQscQKKLKQMEVQLEEEYEDKQKVLRE-KRELEGKLATLSDQVNRRDFEsekrlrkdLKRTKALLADAQLMLD 1685
Cdd:pfam05557 73 EQAELNRL--KKKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1686 HLKNSApskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEdlhLQIDDIAKAKTALEEQLS--RLQREkneiQNRLEED 1763
Cdd:pfam05557 143 LLKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipELEKE----LERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1764 QEDMNELMKKH---KAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQ-----------------ALQSQVEFLEQSm 1823
Cdd:pfam05557 213 NKHLNENIENKlllKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1824 vDKSLVSRQ-----------------EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD-QRIAAENREKEQN 1885
Cdd:pfam05557 292 -EIVLKEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELT 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1886 -KRLQRQLRDTKEEMGELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1933
Cdd:pfam05557 371 mSNYSPQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1260-1840 |
2.72e-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: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGEsasqlLDAETAERLRAEKE-M 1338
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1339 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QEFEDKLEVEQQN 1415
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQADS-------EESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1477
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE---------------------AELQ 1536
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1537 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGTIQMLEQAKLRLEM-------EMERMRQTHSKEM 1602
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1603 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE--KRELEGKLATLSDQVNRRDFESEKRlRKDLKRTKALLAD 1679
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSK-AEDKGRAPSLGAL 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1680 AQLMLDHLKNSAPSKREIAQLKNQLE----ESEFTCAAAVKARKAMevEIEDLHLQIDDIAKAKTALEEQLSR---LQRE 1752
Cdd:pfam15921 939 DDRVRDCIIESSLRSDICHSSSNSLQtegsKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPK 1016
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1753 KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDlaQINDLQAQ-LEEANKEKQELQEKLQALQSQVEFLE---QSMvdKSL 1828
Cdd:pfam15921 1017 KSPVHSLLTSSAEGSIGSSSQYRSAKTIHSPD--SVKDSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSM 1092
|
650
....*....|..
gi 1093953565 1829 VSRQEAKIRELE 1840
Cdd:pfam15921 1093 IRNQEKRIQKVK 1104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1607-1832 |
2.78e-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: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1607 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESE------KRLRKDLKRTKALLADA 1680
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaelAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1681 QLMLDHLKNSAPSKREIAQLKNQLEESEFtcAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ--- 1757
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEall 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1758 NRLEEDQEDMNELMKKHKAAVAQASRDLAQindLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1832
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1477-1823 |
3.94e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 64.86 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1477 SELSQAHEEAQREKLQREKLQRE--KDmLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS---LEAE--LQDISSQE 1542
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1543 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1614
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1615 SCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ----------------VNRRDFESEKRLRKDLKRTKALLa 1678
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelkeeidrvkqsytLNESELESVRQLEKQLESLEKQY- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1679 daqlmLDHLKNSAPSKREIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1758
Cdd:PRK04778 365 -----DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKR 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1759 RLE--------EDQEDMNELMKKHkaaVAQASRDLAQ----INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1823
Cdd:PRK04778 433 YLEksnlpglpEDYLEMFFEVSDE---IEALAEELEEkpinMEAVNRLLEEATEDVETLEEETEELVENATLTEQLI 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1389-1937 |
4.83e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1389 RAVREVDFTKKRLQQEFEDKLEVEQQNKRQ------LERRLGDLQADSEESQRALQQLKKKCQRLTA------ELQDTkl 1456
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELearlesLSESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDA-- 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1457 hlegqqvrnheLEKKQRRFDSEL--SQAHEEAQREKLQREK-LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLeA 1533
Cdd:PRK04863 612 -----------LARLREQSGEEFedSQDVTEYMQQLLEREReLTVERDELAARKQALDEEIERLSQPGGSEDPRLNAL-A 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1534 E------LQDISSQESKDEA-----------------SLAKVKKQLRDLEAKVKD----------------QEEELDE-- 1572
Cdd:PRK04863 680 ErfggvlLSEIYDDVSLEDApyfsalygparhaivvpDLSDAAEQLAGLEDCPEDlyliegdpdsfddsvfSVEELEKav 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1573 --QAGTIQML---------------EQaklRLEmEMERMRQTHSKEMESRDEEVeearQSCQKKLKQME--------VQL 1627
Cdd:PRK04863 760 vvKIADRQWRysrfpevplfgraarEK---RIE-QLRAEREELAERYATLSFDV----QKLQRLHQAFSrfigshlaVAF 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1628 EEEYEDKQKVLREKR-ELEGKLATLSDQvnrrdfesEKRLRKDLKRTKALLADAQLMLDHLKNSAPSK--REIAQLKNQL 1704
Cdd:PRK04863 832 EADPEAELRQLNRRRvELERALADHESQ--------EQQQRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVEEIREQL 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1705 EESEFtcAAAVKARKAMEVEiedlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE---DMNELM-KKHKAAVAQ 1780
Cdd:PRK04863 904 DEAEE--AKRFVQQHGNALA------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVqRRAHFSYED 975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1781 ASRDLAQINDLQAQLEEANKEKQELQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFERtqvkRLESLAS 1858
Cdd:PRK04863 976 AAEMLAKNSDLNEKLRQRLEQAEQERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGV 1048
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1859 RLKENME-KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1937
Cdd:PRK04863 1049 PADSGAEeRARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1391-1996 |
5.00e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1391 VREVDFTKKRLQQEfedKLEVEQQNKR--QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHEL 1468
Cdd:PRK01156 182 ISNIDYLEEKLKSS---NLELENIKKQiaDDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1469 EKKQRRFDSELSQAHE----EAQREKLQREKLQREKDMLLaEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEsK 1544
Cdd:PRK01156 259 KTAESDLSMELEKNNYykelEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ-K 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1545 DEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLE---MEMERMRQTHS---KEMESRDEEVEEARQSCQK 1618
Cdd:PRK01156 337 DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEeysKNIERMSAFISeilKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1619 KLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ----VNRRDFESEK--RLRKDLKRTKALLADAqlmLDHLKNSAP 1692
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKsnHIINHYNEKKSRLEEK---IREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1693 S----KREIAQLKNQLEESEFT-CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIqnrLEEDQEDM 1767
Cdd:PRK01156 494 DidekIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED---LDSKRTSW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1768 NELMkkhkaavaqASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvSRQEAKIRELETRLEFER 1847
Cdd:PRK01156 571 LNAL---------AVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---------SYIDKSIREIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1848 TQVKRLESLasrlkenmeklteerdqriaaenreKEQNKRLQRQLRDTKEEmgelarkeaeaSRKKHELEMDLESLEAAN 1927
Cdd:PRK01156 633 NKYNEIQEN-------------------------KILIEKLRGKIDNYKKQ-----------IAEIDSIIPDLKEITSRI 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1928 QSLQADLKLAFKRigdLQAAIEDEMESDENEDLINSEgdsdvDSELEDRVDGVKSWLSKNKGPSKAASD 1996
Cdd:PRK01156 677 NDIEDNLKKSRKA---LDDAKANRARLESTIEILRTR-----INELSDRINDINETLESMKKIKKAIGD 737
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1402-1710 |
7.40e-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: 64.37 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1402 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQrltaELQDTKLHLEGQQVRNHELEKK------QRRF 1475
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR----EVERRRKLEEAEKARQAEMDRQaaiyaeQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1476 DSELSQAHEEAQREKLQREkLQREKDMLLAEAFSLKQQLEEKDMDiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1555
Cdd:pfam17380 343 AMERERELERIRQEERKRE-LERIRQEEIAMEISRMRELERLQME---RQQKNERVRQELEAARKVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELDEQagtIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQSCQKKLKQMEVQLEEEY 1631
Cdd:pfam17380 419 KVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1632 ----------EDKQKVLREKR-------ELEGKLATLSDQVNRRDFESEKRLRKDLKRTKAL------LADAQLMLDHLK 1688
Cdd:pfam17380 493 rrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIqeqmrkATEERSRLEAME 572
|
330 340
....*....|....*....|..
gi 1093953565 1689 NSAPSKREIAQLKNQLEESEFT 1710
Cdd:pfam17380 573 REREMMRQIVESEKARAEYEAT 594
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1604-1956 |
8.07e-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: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1604 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLM 1683
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKN--------ALQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1684 LDHLKNSAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL-------------------- 1742
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1743 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQE--------------LQE 1807
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1808 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQ----VKRLESLASRLKENMEKLTEERDQRIAAEnreke 1883
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1884 qnkrlqRQLRDTKEEMGELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDE 1956
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHE 344
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1273-1530 |
9.60e-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: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1273 EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQM 1352
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1353 EVMEMEVmeARLIRAAEINGEVDdddaggewrlkyeravrevdftkkrlqqefEDKLEVEQQNKRQLERRLGDLQADSEE 1432
Cdd:COG4942 100 EAQKEEL--AELLRALYRLGRQP------------------------------PLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1433 SQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQ 1512
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250
....*....|....*...
gi 1093953565 1513 QLEEKDMDIAGFTQKVVS 1530
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1265-1810 |
1.03e-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: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1344
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDAlkkqmevmeMEVMEARLIRAAEINGEVDDDdaggewRLKyeraVREVDFTKKRLQQE----FEDKLEVEQQNKRQLE 1420
Cdd:pfam05483 354 FEA---------TTCSLEELLRTEQQRLEKNED------QLK----IITMELQKKSSELEemtkFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1421 RRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREK 1500
Cdd:pfam05483 415 AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1501 DMLLAEAFSLKQqlEEKDMdiagftqkVVSLEAELQDISSQESKDEASLAKVkKQLRDLEAKVKDQEEELDEQagTIQML 1580
Cdd:pfam05483 495 DKLLLENKELTQ--EASDM--------TLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELESVREE--FIQKG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1581 EQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKVLREKRELEGK-LATLSDQVNR 1657
Cdd:pfam05483 562 DEVKCKLDKSEENARSI-EYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENKqLNAYEIKVNK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1658 RDFEsekrlrkdlkrtkalLADAQLMLDHLKNSAPSKREIAQLknqleeSEFTCAAAVKARKAMEVEIEDLHLQIDDIAK 1737
Cdd:pfam05483 641 LELE---------------LASAKQKFEEIIDNYQKEIEDKKI------SEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1738 AKTAleEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVA---QASRDLAQINDLQAQLEEANKEKQELQEKLQ 1810
Cdd:pfam05483 700 HKIA--EMVALMEKHKHQYDKIIEERDSELglykNKEQEQSSAKAAleiELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1262-1784 |
1.18e-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: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1262 QLSEEQiRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1333
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1334 AEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGgewRLKYERAVREVDFTKKRLQQEfEDKLEVEQ 1413
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAK---KMTLESSERTVSDLTASLQEK-ERAIEATN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1414 QNKRQLERR----LGDLQADSEESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNhelekkQRRFDSELSQAHEEAQ 1487
Cdd:pfam15921 517 AEITKLRSRvdlkLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIEN------MTQLVGQHGRTAGAMQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1488 REKLQREKLQREKDMLLAEAFSLKqqlEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1567
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1568 EELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1616
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1617 QKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSAPSKRE 1696
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1697 IAQLKNQ---------------LEESEFTCAAAVKARKAMEVEIEDLHLQIddiaKAKTALEEQLSRLQREKNEIQnrlE 1761
Cdd:pfam15921 826 IIQRQEQesvrlklqhtldvkeLQGPGYTSNSSMKPRLLQPASFTRTHSNV----PSSQSTASFLSHHSRKTNALK---E 898
|
570 580
....*....|....*....|...
gi 1093953565 1762 EDQEDMNELMKKHKAAVAQASRD 1784
Cdd:pfam15921 899 DPTRDLKQLLQELRSVINEEPTV 921
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1258-1615 |
1.57e-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: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1258 LIEVQLSEEQIRNKDEEIQQLRSKLEKaEKERNElrlnsdRLESRISELTSELTDERntgesasqlldaetAERLRAEKE 1337
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEK-LKERLE------ELEEDLSSLEQEIENVK--------------SELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1338 MKELQTQYDALKKQMEVMEMEVMEARLiraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQEfedkLEVEQQNKR 1417
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLE---EEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1418 QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQ 1497
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1498 REKDMLLAEAFSLKQQLEEkdmdiagftqkvvsLEAELQDISSqESKDEASLAKVKKQLRDLEAKVKDQEeelDEQAGTI 1577
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSE--------------IEDPKGEDEE-IPEEELSLEDVQAELQRVEEEIRALE---PVNMLAI 978
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1093953565 1578 QMLEQAKLRL-EMEMERMR-QTHSKEMESRDEEVEEARQS 1615
Cdd:TIGR02169 979 QEYEEVLKRLdELKEKRAKlEEERKAILERIEEYEKKKRE 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1382-1750 |
2.52e-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: 62.66 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1382 EWRLKYERAV--REVDFTKKRLQQEFEDKL-----EVEQQNKRqlERRLG-DLQADSEESQRALQ--QLKKKCQRLTAEL 1451
Cdd:COG3096 279 ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAR--ESDLEqDYQAASDHLNLVQTalRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1452 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDML-------------LAEAfslKQQLEEKD 1518
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKA---RALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1519 MDIAGF--------------TQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGTIQMLEQA 1583
Cdd:COG3096 434 LTPENAedylaafrakeqqaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVErSQAWQTARELLRRYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1584 KLRLEMEMERMRQthskeMESRDEEVEEARQSCQKKLKQmEVQLEEEYEDKQKvlrekrELEGKLATLSDQVNRrdfESE 1663
Cdd:COG3096 514 LQQLRAQLAELEQ-----RLRQQQNAERLLEEFCQRIGQ-QLDAAEELEELLA------ELEAQLEELEEQAAE---AVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1664 KR--LRKDLKRTKALLADaqlmldhLKNSAPSKREIAQLKNQLEE---SEFTCAAAVKArkAMEVEIEDLH---LQIDDI 1735
Cdd:COG3096 579 QRseLRQQLEQLRARIKE-------LAARAPAWLAAQDALERLREqsgEALADSQEVTA--AMQQLLEREReatVERDEL 649
|
410
....*....|....*
gi 1093953565 1736 AKAKTALEEQLSRLQ 1750
Cdd:COG3096 650 AARKQALESQIERLS 664
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1698-1962 |
3.47e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 60.70 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1698 AQLKNQLEESEFTCAAAVKARKAM-EVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1776
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1777 AvaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFERTQVkrlESL 1856
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNV---EMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1857 ASRLKENMEKLTEERDQ--RIAAENRE------KEQNKRLQRQ-------LRDTKEEMGELarkeaeaSRKKHELEMDLE 1921
Cdd:pfam00038 162 AARKLDLTSALAEIRAQyeEIAAKNREeaeewyQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1922 SLEAANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1962
Cdd:pfam00038 235 SLKKQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1694-1910 |
3.83e-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: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEftcaAAVKARKAmEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1773
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 HKAAVAQASRDlAQINDLQAQLEEANKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1846
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1847 RTQVKRLESLASRLKENMEKLTEERDQRiaaenrekeqnKRLQRQLRDTKEEMGELARKEAEAS 1910
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAEL-----------RRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1752-1951 |
4.29e-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: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1752 EKNEIQNRLEEDQEDMNELMKKHKAAV-AQASRD-LAQINDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdkslv 1829
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEdAREQIElLEPIRELAERYAAARERLAELEYLRAALRLW-------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1830 sRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQ-RIAAENREKEQNKRLQRQLRDTKEEMGELARKEAE 1908
Cdd:COG4913 285 -FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1093953565 1909 ASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDE 1951
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1635-1811 |
4.36e-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: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1635 QKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAA 1714
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1715 VKAR--KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdlaqinDLQ 1792
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 1093953565 1793 AQLEEANKEKQELQEKLQA 1811
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1690-1886 |
6.31e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1690 SAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1769
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1770 L---MKKHKAAVAQ-----------------------ASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1823
Cdd:COG3883 91 RaraLYRSGGSVSYldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1824 VD-KSLVSRQEAKIRELETRlefERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1886
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 |
6.72e-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: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGDFGFSL---RrtTMLDRGPEGQACRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGHNVESKSRDEI 292
Cdd:cd06671 3 RRVELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEA 77
|
90
....*....|....*...
gi 1093953565 293 VEMIRQSGDSVRLKVQPI 310
Cdd:cd06671 78 VEAIRNAGNPVVFLVQSL 95
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1466-1824 |
7.13e-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: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1466 HELEKKQRRFDSELSQ--AHEEAQREKLQ--REKLQREKDMLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS---L 1531
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1532 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1604
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1605 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQvnrrdfesEKRLRKDLKRTK------- 1674
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ--------NKELKEELERVQqsytlne 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1675 ---ALLADAQLMLDHLknsapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALE-------E 1744
Cdd:pfam06160 326 nelERVRGLEKQLEEL------EKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRkdelearE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1745 QLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDLAQ----INDLQAQLEEANKEKQELQEKLQALQSQ 1815
Cdd:pfam06160 400 KLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
....*....
gi 1093953565 1816 VEFLEQSMV 1824
Cdd:pfam06160 480 ATLAEQLIQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1718-1932 |
7.81e-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: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1718 RKAMEVEIEDLHLQIDDIAKAKTALE---EQLSRLQ--REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ--IND 1790
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdarEQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEaeLEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1791 LQAQLEEANKEKQELQEKLQALQSQVEFLEQSM--VDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKenmekLT 1868
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIrgNGGDRLEQLEREIERLERELEERERRRARLEALLAALG-----LP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1869 EERDQRIAAENREkeqnkRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1932
Cdd:COG4913 375 LPASAEEFAALRA-----EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1695-1873 |
8.05e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.40 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1695 REIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1774
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1775 kaavaqasRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFERtqvKRLE 1854
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170
....*....|....*....
gi 1093953565 1855 SLASRLKENMEKLTEERDQ 1873
Cdd:COG1579 149 EELAELEAELEELEAEREE 167
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLrrttmldrGPEGQACRRVVHFAEPGAGTkdlalgLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd06769 1 TVEIQRDAVLGFGFVA--------GSERPVVVRSVTPGGPSEGK------LLPGDQILKINNEPVEDLPRERVIDLIREC 66
|
....*...
gi 1093953565 300 GDSVRLKV 307
Cdd:cd06769 67 KDSIVLTV 74
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1260-1953 |
1.28e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNEL---------RLNS-----------DRLESRISELTSELTDERNTGES 1319
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLeqdyqaasdHLNLvqtalrqqekiERYQADLEELEERLEEQNEVVEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1320 ASQLLDAETAERLRAEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEING--EVDDDDAGGewrlkyera 1390
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGlpDLTADNAED--------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1391 vrevdftkkrLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKK---KCQRLTA--ELQDTKLHLEGQQVRN 1465
Cdd:PRK04863 443 ----------WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagEVSRSEAwdVARELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1466 HELEKKQRRFdSELSQAHEEAQR-EKLQREKLQREKDMLLAEAFsLKQQLEEkdmdiagftqkvvsLEAELQDISSQesk 1544
Cdd:PRK04863 513 EQLQQLRMRL-SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES--- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1545 deaslakvKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQME 1624
Cdd:PRK04863 574 --------VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELT 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1625 VQLEEEYEDKQKVLREKRELEG-------KLATLSDQVN-------RRDFESEkrlrkDLKRTKAL------------LA 1678
Cdd:PRK04863 645 VERDELAARKQALDEEIERLSQpggsedpRLNALAERFGgvllseiYDDVSLE-----DAPYFSALygparhaivvpdLS 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1679 DAQLMLDHLKNSAPSKREIAQLKNQLEES-----EFTCAAAVK-----------------ARKAMEVEIEDLHLQIDDIA 1736
Cdd:PRK04863 720 DAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfsveELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1737 K--AKTA--------LEEQLSR--------------------LQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLA 1786
Cdd:PRK04863 800 EryATLSfdvqklqrLHQAFSRfigshlavafeadpeaelrqLNRRRVELERALADHESQ----EQQQRSQLEQAKEGLS 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1787 QINDLQAQL-----EEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLK 1861
Cdd:PRK04863 876 ALNRLLPRLnlladETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAK 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1862 ENMEKLTE--ERDQRIAAENREK--EQNKRLQRQLRdtkeemGELARKEAEASRKKHELEMDLESLEAANQsLQADLKLA 1937
Cdd:PRK04863 956 QQAFALTEvvQRRAHFSYEDAAEmlAKNSDLNEKLR------QRLEQAEQERTRAREQLRQAQAQLAQYNQ-VLASLKSS 1028
|
810
....*....|....*.
gi 1093953565 1938 FKRIGDLQAAIEDEME 1953
Cdd:PRK04863 1029 YDAKRQMLQELKQELQ 1044
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1408-1893 |
1.36e-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: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1408 KLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRRfdSELSQAHEEAQ 1487
Cdd:pfam10174 276 QMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQR--AAILQTEVDAL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1488 REKL------------QREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDissqesKDeaslakvkKQ 1555
Cdd:pfam10174 351 RLRLeekesflnkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD--------KQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEEEYEDKQ 1635
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1636 KVLREKRELEGKLAtlSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAV 1715
Cdd:pfam10174 496 SSLIDLKEHASSLA--SSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1716 KARKAMEVE-----IEDLHLQIDDIAKAKTALEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAVAQASR---DLAQ 1787
Cdd:pfam10174 574 SGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQLLEEARrreDNLA 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1788 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKS--LVSRQEAKIRELETRLEFER-----------TQVKRLE 1854
Cdd:pfam10174 650 DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKQeallaaisekdANIALLE 729
|
490 500 510
....*....|....*....|....*....|....*....
gi 1093953565 1855 SLASRLKENMEKlteerdqrIAAENREKEqnkRLQRQLR 1893
Cdd:pfam10174 730 LSSSKKKKTQEE--------VMALKREKD---RLVHQLK 757
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1402-1815 |
2.30e-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: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1402 QQEFEDklEVEQQNkrqLERRLGDLQADSEESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQ 1481
Cdd:pfam05667 219 AQEWEE--EWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1482 AHEEAQREKLQR-EKLQREKDMLLAEAFSLKQQLEEKDMDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDLE 1560
Cdd:pfam05667 291 DTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1561 AKVKDQEEELDEQAGTIQMLEQaklrlemEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKVLRE 1640
Cdd:pfam05667 363 SSIKQVEEELEELKEQNEELEK-------QYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1641 krelegKLATLSDQVNRRDFESEKRLR--KDLK-RTKALLADAQlmldhlknsapSKRE-IAQLKNQLEE-------SEF 1709
Cdd:pfam05667 434 ------EYRALKEAKSNKEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrSAY 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1710 TcaaavkaRKAMEVeIEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRDLA 1786
Cdd:pfam05667 497 T-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKYLA 564
|
410 420 430
....*....|....*....|....*....|....*.
gi 1093953565 1787 QINDLQAQL----EEANK---EKQELQEKLQALQSQ 1815
Cdd:pfam05667 565 ALHENCEQLiqtvEETGTimrEIRDLEEQIETESGK 600
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1636-1919 |
2.31e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 59.26 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1636 KVLREK-RELEGKLATLSDQVN--RRDFESEKRLRKDL-KRTKALLADAQLMLDHLKNSAPS-KREIAQLKNQLEEseft 1710
Cdd:PHA02562 170 KLNKDKiRELNQQIQTLDMKIDhiQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1711 caaavkarkaMEVEIEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdl 1785
Cdd:PHA02562 246 ----------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 aQINDLQAQLEEANKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENME 1865
Cdd:PHA02562 307 -KLKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIE 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1866 KLTEERdqriaaenrekeqnkrlqrqlRDTKEEMGELARKEAEASRKKHELEMD 1919
Cdd:PHA02562 369 ELQAEF---------------------VDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1766-2008 |
2.55e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1766 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEf 1845
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-------------AEIAEAEAEIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1846 erTQVKRLESLASRLKEN------MEKLTEERD-----QRIAAENREKEQNKRLQRQLRDTKEEmgeLARKEAEASRKKH 1914
Cdd:COG3883 83 --ERREELGERARALYRSggsvsyLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAE---LEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1915 ELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPSKAA 1994
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|....
gi 1093953565 1995 SDDGSLKSSSPTSY 2008
Cdd:COG3883 238 AAAAAAASAAGAGA 251
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1258-1651 |
2.57e-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: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1258 LIEVQLsEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgESASQLLDAETaerlRAEKE 1337
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1338 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---EFEDKLEVEQQ 1414
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1415 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHeeaQREKlqre 1494
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH---RKEA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1495 klqrEKDMLLAEAFSLKQQLEEKDmdiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1574
Cdd:pfam07888 231 ----ENEALLEELRSLQERLNASE-------RKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1575 GTIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKVLRE-KRELEGKLATL 1651
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 ... |
1265-1762 |
2.63e-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: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNE-------LRLNSDRLESRISELTSELTderntgesasqlldaetaerlRAEKE 1337
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1338 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERavrevdftKKRLQQEFEDKLEV 1411
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEE--------KESFLNKKTKQLQD 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1412 EQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREK- 1490
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-EEALSEKe 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1491 --LQREKLQREKD--MLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ 1566
Cdd:pfam10174 450 riIERLKEQREREdrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1567 EEE---LDEQAGTIQMLEQA---------KLR-LEMEMERMRQTHSKEMESRD------EEVEEARQSCQKKLKQMEVQL 1627
Cdd:pfam10174 530 KEEcskLENQLKKAHNAEEAvrtnpeindRIRlLEQEVARYKEESGKAQAEVErllgilREVENEKNDKDKKIAELESLT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1628 EEEYEDKQKVLREKRELE-----GKLATLSDQVNRRDFESEK--------------RLRKDLKRTKALLADAQLMLD--- 1685
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQqemkkKGAQLLEEARRREDNLADNsqqlqleelmgaleKTRQELDATKARLSSTQQSLAekd 689
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 1686 -HLKNSAPSKREiaQLKNQLEESEFTCAAAVKARKAmevEIEDLHLQiddIAKAKTALEEQLSrLQREKNEIQNRLEE 1762
Cdd:pfam10174 690 gHLTNLRAERRK--QLEEILEMKQEALLAAISEKDA---NIALLELS---SSKKKKTQEEVMA-LKREKDRLVHQLKQ 758
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1478-1668 |
3.33e-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: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1557
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1558 DLEAKVKdqeeELDEQAGTIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKv 1637
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIE--------ELEEELAELEAELAELEAELEEKKAELDEELAELEA- 156
|
170 180 190
....*....|....*....|....*....|.
gi 1093953565 1638 lrEKRELEGKLATLSDQVNRRDFESEKRLRK 1668
Cdd:COG1579 157 --ELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1465-1935 |
3.38e-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: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1465 NHELEKKQRRFDsELSQAHEeaqreklqreklqREKDMLLAEAFSLKQQLEEKDMDiagftqkvvslEAELQDISSQESK 1544
Cdd:pfam15921 84 SHQVKDLQRRLN-ESNELHE-------------KQKFYLRQSVIDLQTKLQEMQME-----------RDAMADIRRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1545 DEASLA-KVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQM 1623
Cdd:pfam15921 139 SQEDLRnQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1624 EVQLeeeyedkQKVLREKRE----LEGKLATLSDQVNRRDFESEKR----LRKDLKRTKALLADAQLMLDHLKNSAPSKR 1695
Cdd:pfam15921 219 GSAI-------SKILRELDTeisyLKGRIFPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1696 EIAQ-LKNQLEesefTCAAAVKARKAMEVEiedlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1774
Cdd:pfam15921 292 SQANsIQSQLE----IIQEQARNQNSMYMR------QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1775 KAAVAQASRDLAQIND-LQAQLEEANKEKQELQ-EKLQalqsqvefleqsmvDKSLVSRQEAK---IRELETRLEFERTQ 1849
Cdd:pfam15921 362 RTERDQFSQESGNLDDqLQKLLADLHKREKELSlEKEQ--------------NKRLWDRDTGNsitIDHLRRELDDRNME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1850 VKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKeemgELARKEAEASRKKhelEMDLESLEAANQS 1929
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK----EMLRKVVEELTAK---KMTLESSERTVSD 500
|
....*.
gi 1093953565 1930 LQADLK 1935
Cdd:pfam15921 501 LTASLQ 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1260-1655 |
3.52e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSK-------LEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDA------ 1326
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpec 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1327 ----ETAERLRAEKEMKElqtqydalkkqmevmemevmearliRAAEINGEVDDddaggewrLKYERAVREVDFTKKRLQ 1402
Cdd:PRK02224 458 gqpvEGSPHVETIEEDRE-------------------------RVEELEAELED--------LEEEVEEVEERLERAEDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1403 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegqqvrnhelekkqrrfdSELSQA 1482
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR---------------------EAAAEA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1483 HEEAQREKLQREKLQREKDMLLAEAFSLkQQLEEKDMDIAGFTQKVVSLEAELQDIssQESKDEAslakvKKQLRDLEAK 1562
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL--AELNDER-----RERLAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1563 VKDQEEELDEQAgtIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKVLRE 1640
Cdd:PRK02224 636 KRELEAEFDEAR--IEEAREDKERAEEYLE--------QVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEN 705
|
410
....*....|....*
gi 1093953565 1641 KRElegKLATLSDQV 1655
Cdd:PRK02224 706 RVE---ALEALYDEA 717
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1436-1816 |
3.64e-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: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1436 ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQRRFDSEL-SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQ 1513
Cdd:pfam15964 333 AYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQKERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1514 LEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ-----AGTIQMLEQA----- 1583
Cdd:pfam15964 412 VAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEhreyrTKTGRQLEIKdqeie 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1584 KLRLEMEMERMRqthskeMESRDEEVEEARQSCQK---KLKQMEVQLEEEYEDKQKVlreKRELEGKLATLSDQVNRRDF 1660
Cdd:pfam15964 492 KLGLELSESKQR------LEQAQQDAARAREECLKlteLLGESEHQLHLTRLEKESI---QQSFSNEAKAQALQAQQREQ 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1661 ESEKRLR-------KDLKRTKALLADAQLMLDHLKnsapskREIAQLKNQLEEseftcaAAVKARKAME---VEIEDLHL 1730
Cdd:pfam15964 563 ELTQKMQqmeaqhdKTVNEQYSLLTSQNTFIAKLK------EECCTLAKKLEE------ITQKSRSEVEqlsQEKEYLQD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1731 QIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnelMKKHKAAVAQasrDLAQINDLQAQLEeanKEKQELQEKLQ 1810
Cdd:pfam15964 631 RLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ--------LDKHCQATAQ---QLVQLLSKQNQLF---KERQNLTEEVQ 696
|
....*.
gi 1093953565 1811 ALQSQV 1816
Cdd:pfam15964 697 SLRSQV 702
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1725-1913 |
3.75e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQE 1804
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1805 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF-----------ERTQVKRLESLASRLK--ENMEKLTEER 1871
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlspeeEKELVEKIKELEKELEkaKKALEKNEKL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1093953565 1872 DQRIAAENREKEQNKRLQRQLRDTKEEMGEL------ARKEAEASRKK 1913
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELheemieLYKEADELRKE 210
|
|
| 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 |
3.77e-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: 3.77e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093953565 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1385-1974 |
4.27e-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: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1385 LKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgQQVR 1464
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN-QEKT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1465 NHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESK 1544
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1545 DEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQME 1624
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1625 VQLEEEYEDkqkVLREKRELEGKLATLSDQVNRR---------------------------------DFESEKRL----- 1666
Cdd:TIGR00606 504 KSLQNEKAD---LDRKLRKLDQEMEQLNHHTTTRtqmemltkdkmdkdeqirkiksrhsdeltsllgYFPNKKQLedwlh 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1667 --RKDLKRTKALLADAQL-------MLDHLKNSAPSKRE---------------------IAQLKNQLEESEFTCAAAVK 1716
Cdd:TIGR00606 581 skSKEINQTRDRLAKLNKelasleqNKNHINNELESKEEqlssyedklfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEVEIEDLHLQ-------IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA-------S 1782
Cdd:TIGR00606 661 ATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqsiiD 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1783 RDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL-------EQSMVDKSLVSRQEAKIRELETRLEferTQVKRLES 1855
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTIMERFQMELKDVERKIA---QQAAKLQG 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1856 L-ASRLKENMEKLTEERDQRIAAENREKEQNKRL----QRQLRDTKEEMGELARKE---AEASRKKHELEMDLESLEAAN 1927
Cdd:TIGR00606 818 SdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLiqdqQEQIQHLKSKTNELKSEKlqiGTNLQRRQQFEEQLVELSTEV 897
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1928 QSLQADLKLAFKRIGDLQAAIEDEMEsdENEDLINSEGDSDVDSELE 1974
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQ--EKEELISSKETSNKKAQDK 942
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1250-1654 |
5.70e-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: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1250 KLFTTVRPLIEVQLSEEQIRNKDE--------EIQQLRSKLEKAEKERNELRLNSDRLESRISElTSELTDERNTGESAS 1321
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1322 QLLDAETAERL----RAEKEMKELQTQYDALKKQMEVMemevmearLIRAAEINGEVDDDdaggewRLKYERAVREVD-- 1395
Cdd:pfam05483 432 EELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHY--------LKEVEDLKTELEKE------KLKNIELTAHCDkl 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1396 -FTKKRLQQEFEDK-LEVEQQNKrqlerrlgDLQADSEESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNhELEKKQR 1473
Cdd:pfam05483 498 lLENKELTQEASDMtLELKKHQE--------DIINCKKQEERMLKQIE------NLEEKEMNLRDELESVRE-EFIQKGD 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1474 RFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE----AELQDISSQE---SKDE 1546
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEikvNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1547 ASLAKVKKQL--------RDLEAKVKDQEEELDE-QAGTIQMLEQAKLRLEME-------------MERMRQTHSKEMES 1604
Cdd:pfam05483 643 LELASAKQKFeeiidnyqKEIEDKKISEEKLLEEvEKAKAIADEAVKLQKEIDkrcqhkiaemvalMEKHKHQYDKIIEE 722
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1605 RDEEV-----EEARQSCQKKLKQMEV------------QLEEEYEDKQKVLREKRElegKLATLSDQ 1654
Cdd:pfam05483 723 RDSELglyknKEQEQSSAKAALEIELsnikaellslkkQLEIEKEEKEKLKMEAKE---NTAILKDK 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1637-1976 |
6.94e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1637 VLREKRELEGKLATLSDQVNRRDfesEKRLRKDLKRTKALLADAQLMLDHLKnsapSKREIAqlKNQLEESEFTCAAAVK 1716
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKE---EKDLHERLNGLESELAELDEEIERYE----EQREQA--RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKamevEIEDLHLQIDDIAKAKTALEeqlsrlqREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1796
Cdd:PRK02224 249 RRE----ELETLEAEIEDLRETIAETE-------REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1797 EANKEKQELQEklqalqsqvefleqsmvdkslvsrqeakireletRLEFERTQVKRLESLASRLKENMEKLTEERDQ-RI 1875
Cdd:PRK02224 318 ELEDRDEELRD----------------------------------RLEECRVAAQAHNEEAESLREDADDLEERAEElRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1876 AAENREKE-QNKRlqRQLRDTKEEMGELaRKEAEASRKKHE-LEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1953
Cdd:PRK02224 364 EAAELESElEEAR--EAVEDRREEIEEL-EEEIEELRERFGdAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
330 340 350
....*....|....*....|....*....|....
gi 1093953565 1954 S-DENEDLINS----------EGDSDVDSELEDR 1976
Cdd:PRK02224 441 RvEEAEALLEAgkcpecgqpvEGSPHVETIEEDR 474
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1362-1893 |
8.27e-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: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1362 ARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFE-DKLEVEQQNKRQLERRLGDLQADSEESQRALQQL 1440
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1441 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDML---LAEAFSLKQQLEEK 1517
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1518 DMDIAGFTQKVVSLEAELQdisSQESkDEASLAKVKKQLR---DLEAKVKDQEEE---LDEQAGTIQMLEQAKLRLEMEM 1591
Cdd:pfam05557 162 QSSLAEAEQRIKELEFEIQ---SQEQ-DSEIVKNSKSELAripELEKELERLREHnkhLNENIENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1592 ERMRQTHSK--EMESRDEEVEEARQScQKKLKQME-------VQLEEEYEDKQKvlREKRELEGKLATLSD----QVNRR 1658
Cdd:pfam05557 238 EREEKYREEaaTLELEKEKLEQELQS-WVKLAQDTglnlrspEDLSRRIEQLQQ--REIVLKEENSSLTSSarqlEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1659 DFESEKR--------LRKDLKRTKALLADAQlmldhlKNSAPSKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEIEDL 1728
Cdd:pfam05557 315 ELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1729 hlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEK 1808
Cdd:pfam05557 389 ---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1809 LQALQSQVEFLEQSMvDKSLVSRQEAKIRELETRLEFERT--QVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1886
Cdd:pfam05557 464 KNELEMELERRCLQG-DYDPKKTKVLHLSMNPAAEAYQQRknQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF 542
|
....*..
gi 1093953565 1887 RLQRQLR 1893
Cdd:pfam05557 543 KEVLDLR 549
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1189-1605 |
8.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1189 LARLEEQRDEQTSRNLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIEVQLSEEQ 1267
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1268 IRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELT-SELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYD 1346
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1347 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEF 1405
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1482
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1483 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1560
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1561 -------AKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESR 1605
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1259-1783 |
8.69e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLES------RISELTSELTDERNTG--------------- 1317
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMeleknnYYKELEERHMKIINDPvyknrnyindyfkyk 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1318 ---ESASQLL---DAETAERLRAEKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERA 1390
Cdd:PRK01156 305 ndiENKKQILsniDAEINKYHAIIKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1391 VREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD---LQADSEESQRALQQLKKKCQRLTA----------ELQDTKLH 1457
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1458 LEGQQV----RNHELEKKQRR----FDSELSQAHEEAQREKLQREKLQREKDMLLaeafSLKQQLEEKDMD-IAGFTQKV 1528
Cdd:PRK01156 449 LNGQSVcpvcGTTLGEEKSNHiinhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1529 VSLEAELQDissqeskDEASLAKVKKQlrdleakvKDQEEELDEQAGTIQmLEQAKLRLEMEMERMRQTHSKEME---SR 1605
Cdd:PRK01156 525 ESARADLED-------IKIKINELKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1606 DEEVEEARQSCQKKLKQMEVQLEeeyEDKQKVLREKRELEGKLATLSDQVNrrDFESEKRLRKDLKRTkalladaqlmLD 1685
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFP---DDKSYIDKSIREIENEANNLNNKYN--EIQENKILIEKLRGK----------ID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1686 HLKNSAPSKREIAQLKNQLeeseftcaaAVKARKaMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1765
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEI---------TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
570
....*....|....*...
gi 1093953565 1766 DMnELMKKHKAAVAQASR 1783
Cdd:PRK01156 724 TL-ESMKKIKKAIGDLKR 740
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
1.13e-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: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLRRttMLDRGPEGQACRRVVHFaepGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 1093953565 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1747-1988 |
1.16e-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: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1747 SRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasRDLaqINDLQAQLE----EANKEK--QELQEKLQALQSQVEFLe 1820
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLERL------------EDI--LGELERQLEplerQAEKAEryRELKEELKELEAELLLL- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1821 qsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMG 1900
Cdd:COG1196 233 --------------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1901 ELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELEDRVDGV 1980
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
....*...
gi 1093953565 1981 KSWLSKNK 1988
Cdd:COG1196 379 EELEELAE 386
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1471-1929 |
1.17e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1471 KQRRFDSELSQahEEAQREKLQREKLQREKdmLLAEAFSLKQQLEekdmdiagftqkvvSLEAELQDISSQESKDEAS-- 1548
Cdd:PRK01156 136 GQGEMDSLISG--DPAQRKKILDEILEINS--LERNYDKLKDVID--------------MLRAEISNIDYLEEKLKSSnl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1549 -LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMermrqthsKEMESRDEEVeearqscqkklKQMEVQL 1627
Cdd:PRK01156 198 eLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLEDMK-----------NRYESEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1628 EEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRkDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEE- 1706
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKd 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1707 -SEFTcaaavkarkAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1785
Cdd:PRK01156 338 yNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM-----------------VDKSL---------VSRQEAKIREL 1839
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKSNhiinhynekKSRLEEKIREI 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1840 EtrleferTQVKRLESLASRLKENMEKLTEERDQRIAAENRekeQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE-M 1918
Cdd:PRK01156 489 E-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIKINELKDKHDKYEEIKNRYKsL 558
|
490
....*....|.
gi 1093953565 1919 DLESLEAANQS 1929
Cdd:PRK01156 559 KLEDLDSKRTS 569
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1472-1947 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1472 QRRFDSELSQAHEEAQREKLQREKLQREKDMllAEAFSLKQQLEEKDMDIAGFTQKVVSLEAEL---QDISSQESKDEAS 1548
Cdd:TIGR00606 172 KQKFDEIFSATRYIKALETLRQVRQTQGQKV--QEHQMELKYLKQYKEKACEIRDQITSKEAQLessREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1549 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLE 1628
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1629 EEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRlrkDLKRTKALLadaQLMLDHLKNSAPSKREI----------- 1697
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR---DSLIQSLAT---RLELDGFERGPFSERQIknfhtlvierq 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1698 ---AQLKNQLeESEFTCAAAVKARKAMEVEIE------DLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE--- 1765
Cdd:TIGR00606 404 edeAKTAAQL-CADLQSKERLKQEQADEIRDEkkglgrTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQElrk 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1766 DMNELMKKHKAAVAQASrdLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF 1845
Cdd:TIGR00606 483 AERELSKAEKNSLTETL--KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1846 ERTQVKRLESLASRLKENMEKLTEERDQriaAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHEL--EMDLESL 1923
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQ---TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdVCGSQDE 637
|
490 500
....*....|....*....|....
gi 1093953565 1924 EAANQSLQADLKLAFKRIGDLQAA 1947
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGA 661
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1641-1906 |
1.65e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1641 KRELEGKLATLSDQvnrRDFESEKRLrkdlkrTKALLADAQLMLDHLKNSapsKREIAQLKNQLEEseftcaAAVKARKA 1720
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAEDKL------VQQDLEQTLALLDKIDRQ---KEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1721 MEvEIEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNEL----------MKKHKAAVAQASRDLAQIN 1789
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYnsqlvslqtqPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1790 DLQAQLEEANK-----EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEferTQVKRLESLAS-- 1858
Cdd:PRK11281 177 NLLKGGKVGGKalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1859 RLKENMEKLTEERDQRIAAEN-------REKEQNKRLQRQLRDTKEEMGELARKE 1906
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 |
1.76e-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: 1.76e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1093953565 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 |
2.33e-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: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGDFGF-------------SLRRTTMLDRgpegqacrrvVHFAEPGagtkDLAlGLVPGDRLVEINGHNVE 285
Cdd:cd06713 4 RTIILEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVE 68
|
90 100
....*....|....*....|..
gi 1093953565 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 |
3.41e-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: 49.88 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 222 ELQRRPTGdFGFSLRRTTMLDRGPegqacRRVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQSG 300
Cdd:cd06735 5 ELERGPKG-FGFSIRGGREYNNMP-----LYVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELIRSGG 75
|
....*....
gi 1093953565 301 DSVRLKVQP 309
Cdd:cd06735 76 SVVRLLLRR 84
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1735-1981 |
3.87e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1735 IAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQS 1814
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1815 QVEfleqsmVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRD 1894
Cdd:COG4372 88 QLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1895 TKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 1974
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
....*..
gi 1093953565 1975 DRVDGVK 1981
Cdd:COG4372 242 LELEEDK 248
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
4.01e-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: 4.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1546-1908 |
4.09e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1546 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1621
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1622 QMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVnrrdfesekrlrkdlKRTKALLADAQLMLDHLKnsapsKREIA--Q 1699
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1700 LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSrlqrekneiqnrleedqedmneLMKKHKAAVA 1779
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS----------------------VAQAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 QASRDLAQINDlQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASR 1859
Cdd:PRK04863 477 QAYQLVRKIAG-EVSRSEAWDVARELLRRLREQRHLAEQLQQ----------LRMRLSELEQRLRQQQRAERLLAEFCKR 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1860 LK------ENMEKLTEERDQRIAAENREK----EQNKRLQRQLRDTKEEMGELARKEAE 1908
Cdd:PRK04863 546 LGknlddeDELEQLQEELEARLESLSESVsearERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| 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 |
4.73e-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: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGdFGFSLRRttmldrGPEGQACrrVVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06795 3 RKIVLHKGSTG-LGFNIVG------GEDGEGI--FISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKN 72
|
90
....*....|....
gi 1093953565 299 SGDSVRLKVQPIPE 312
Cdd:cd06795 73 AGQTVTIIAQYKPE 86
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1265-1918 |
5.17e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.22 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNkdeEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESasqllDAETAERLRAEKEMKELQTQ 1344
Cdd:PTZ00440 793 ENKISN---DINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT-----EDENLNLKELEKEFNENNQI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKKQMEvmemevmearliraaEINGEVDdddaggewrlkyerAVREVDFTKKRL---QQEFEDKLEVEQQNKRQLER 1421
Cdd:PTZ00440 865 VDNIIKDIE---------------NMNKNIN--------------IIKTLNIAINRSnsnKQLVEHLLNNKIDLKNKLEQ 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1422 RLGDLQADS----EESQRALQQLKKKCQRLTAELQDTK---LHLEGQQVRNHeLEKKQRRFDSELSQAHEEAQREKLQRE 1494
Cdd:PTZ00440 916 HMKIINTDNiiqkNEKLNLLNNLNKEKEKIEKQLSDTKinnLKMQIEKTLEY-YDKSKENINGNDGTHLEKLDKEKDEWE 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1495 KLQREKDMLLAEAFSLKQQ-------------------LEEKDMDIAGFTQKVVSLEAELQD-ISSQESKDEASL---AK 1551
Cdd:PTZ00440 995 HFKSEIDKLNVNYNILNKKiddlikkqhddiielidklIKEKGKEIEEKVDQYISLLEKMKTkLSSFHFNIDIKKyknPK 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1552 VKKQLRDLEAKVKDQEEELDEQagtiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMevqlEEEY 1631
Cdd:PTZ00440 1075 IKEEIKLLEEKVEALLKKIDEN--------------KNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSL----EKIY 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1632 EDKQKVLREKRELEGKLATLSDqVNRRDFESEKrlrkdlkrtkalladaqLMLDHLKNsapskreiaQLKNQLEESeftc 1711
Cdd:PTZ00440 1137 KQMEKTLKELENMNLEDITLNE-VNEIEIEYER-----------------ILIDHIVE---------QINNEAKKS---- 1185
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1712 aaavkarKAMEVEIEDLHLQIDDIaKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA--AVAQASRDLAQI- 1788
Cdd:PTZ00440 1186 -------KTIMEEIESYKKDIDQV-KKNMSKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGlkGEANRSTNVDELk 1257
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1789 ---NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTQ--VKRLESLASR 1859
Cdd:PTZ00440 1258 eikLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKILKeilnSTKKAEEFSNDAKKELEKTDnlIKQVEAKIEQ 1337
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1860 LKENMEKLTE-ERDQRIAAENREKEQnkrLQRQLRDTKEEMGELArKEAEASRKKHELEM 1918
Cdd:PTZ00440 1338 AKEHKNKIYGsLEDKQIDDEIKKIEQ---IKEEISNKRKEINKYL-SNIKSNKEKCDLHV 1393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1777-1961 |
6.05e-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: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1777 AVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLES- 1855
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE-------------ARLEAAKTELEDLEKEIKRLELe 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1856 ---LASRLKENMEKLTEERDQR-IAAENREKEQNKRLQRQLRD-TKEEMGELARKEAEASRKKHELEM---DLESLEAAN 1927
Cdd:COG1579 68 ieeVEARIKKYEEQLGNVRNNKeYEALQKEIESLKRRISDLEDeILELMERIEELEEELAELEAELAEleaELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|....
gi 1093953565 1928 QSLQADLKlafKRIGDLQAAIEdEMESDENEDLI 1961
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 |
6.30e-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: 6.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 219 RELELQRRPTGDFGFSLRRTTMLDRGPeGQACRRVVhfaePGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06718 1 RRVELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1548-1892 |
6.92e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 SLAKVKKQLrdleAKVKDQEEELDEQAGTIQMLEQAKLRLEmemerMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQL 1627
Cdd:PRK11281 37 TEADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLD-----KIDRQKEETEQLKQQLAQA----PAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1628 EEEYEDKQKVLREK------RELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLMLDHLKN--SAPSKReIAQ 1699
Cdd:PRK11281 104 EALKDDNDEETRETlstlslRQLESRLAQTLDQLQ--------NAQNDLAEYNSQLVSLQTQPERAQAalYANSQR-LQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1700 LKNQLEESEFTCAAAVKARKAM-EVEIEDLHLQID-------------DIAKAKTAL-EEQLSRLQREKNEIQN-----R 1759
Cdd:PRK11281 175 IRNLLKGGKVGGKALRPSQRVLlQAEQALLNAQNDlqrkslegntqlqDLLQKQRDYlTARIQRLEHQLQLLQEainskR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1760 LEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQL--------EEANK-EKQELQEKLQ---ALQSQVEFLEQSMVDK- 1826
Cdd:PRK11281 255 LTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISVLKg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1827 SLV-SR----------QEAKIREL-----ETRLE-FE----RTQVKRLESLASRL--KENMEKLTEERDQ--RIAAENRE 1881
Cdd:PRK11281 335 SLLlSRilyqqqqalpSADLIEGLadriaDLRLEqFEinqqRDALFQPDAYIDKLeaGHKSEVTDEVRDAllQLLDERRE 414
|
410
....*....|...
gi 1093953565 1882 --KEQNKRLQRQL 1892
Cdd:PRK11281 415 llDQLNKQLNNQL 427
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1265-1897 |
7.46e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKaekernelrlnsdrLESRISELTSELtderntgESASQLLDAETAERLRAEKEMKELQTQ 1344
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIAD--------------DEKSHSITLKEI-------ERLSIEYNNAMDDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKkqmevmemevmearliraaeingevddddaggewrlKYERAVREVDftkKRLQQEFEDKLEVEQQNKRqLERRLG 1424
Cdd:PRK01156 248 EDMKN------------------------------------RYESEIKTAE---SDLSMELEKNNYYKELEER-HMKIIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1425 DLQADSEESQRALQQLKKKCQRLTAELQDtklhLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQREKLQREKDMLL 1504
Cdd:PRK01156 288 DPVYKNRNYINDYFKYKNDIENKKQILSN----IDAEINKYHAIIKKL----SVLQKDYNDYIKKKSRYDDLNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1505 AEAF---SLKQQLEEKDMDIAGFTQKVVSLEAElqdISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLE 1581
Cdd:PRK01156 360 GYEMdynSYLKSIESLKKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1582 QAKLRLEMEMErMRQTHSK----EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATL-SDQVN 1656
Cdd:PRK01156 437 ENLDELSRNME-MLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEIN 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1657 R-----RDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPS-KREIAQLKNqleeSEFTCAAAVKArkamEVEIEDLHL 1730
Cdd:PRK01156 516 KsineyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKR----TSWLNALAVIS----LIDIETNRS 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1731 QIDDIAKaktaleeQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEeankekqELQEKLQ 1810
Cdd:PRK01156 588 RSNEIKK-------QLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-------KLRGKID 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1811 ALQSQVEFLEQSMVDKSLVSrqeAKIRELETRLEFERTQVKRLESLASRLKENMEKL---TEERDQRIAAENREKEQNKR 1887
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEIT---SRINDIEDNLKKSRKALDDAKANRARLESTIEILrtrINELSDRINDINETLESMKK 730
|
650
....*....|
gi 1093953565 1888 LQRQLRDTKE 1897
Cdd:PRK01156 731 IKKAIGDLKR 740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1746-1960 |
7.76e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1746 LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvd 1825
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1826 kslvsrqeakireletrLEFERTQVKRLESLASRLKENMEKLtEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARK 1905
Cdd:COG4717 124 -----------------LLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1906 EAEASRKK-HELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDL 1960
Cdd:COG4717 186 LSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1406-1959 |
7.83e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.42 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQ----LERRlGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH-ELEKKQRRFDSELS 1480
Cdd:PRK10246 232 EKQLLTAQQQQQQslnwLTRL-DELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHwERIQEQSAALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1481 QAHEE---------AQREKLqREKLQREKDMLLAEAFSLKQQLEEKDMdIAGFTQKVVSLEAELqdisSQESKDEASLAK 1551
Cdd:PRK10246 311 QQIEEvntrlqstmALRARI-RHHAAKQSAELQAQQQSLNTWLAEHDR-FRQWNNELAGWRAQF----SQQTSDREQLRQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1552 VKKQLRDLEAKVKDQEE-----ELDEQAGTI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQM 1623
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1624 EVQLEEeyedKQKVLREKRELEGKLATLSDQvnrrdfesEKRLrKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLK-- 1701
Cdd:PRK10246 460 NAALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEpg 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1702 -NQLEeseftcaaavkaRKAMEVEIEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmneLMKKHKAAVAQ 1780
Cdd:PRK10246 527 vNQSR------------LDALEKEVKKLG---EEGAALRGQLDALTKQLQRDESEAQSLRQEEQA----LTQQWQAVCAS 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1781 ASRDLAQINDLQAQLEEANKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVK-RLESLA 1857
Cdd:PRK10246 588 LNITLQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1858 SRLKENMEKLT--EERDQRIAAENREKEQNKRLQRQ------LRDTKEEMGELARKEAEAS----RKKHElemDLESLEA 1925
Cdd:PRK10246 655 LTLPQEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHS 731
|
570 580 590
....*....|....*....|....*....|....
gi 1093953565 1926 ANQSLQADLKLAFKRIGDLQAAIEDEMESDENED 1959
Cdd:PRK10246 732 QLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1272-1487 |
8.72e-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: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1272 DEEIQQLRSKLEKAEKERNELRLNSDrlesriseltseLTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQ 1351
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1352 mevmemevmearLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQ------QEFEDKL-EVEQQNKRQLERRLG 1424
Cdd:COG3206 249 ------------LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvIALRAQIaALRAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1425 DLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSeLSQAHEEAQ 1487
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES-LLQRLEEAR 378
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1678-1905 |
8.72e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 53.93 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1678 ADAQL-MLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAK------TALEEQLSRLQ 1750
Cdd:COG0497 140 PDAQReLLDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeeEELEEERRRLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1751 R-EK-----NEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFleqsmv 1824
Cdd:COG0497 220 NaEKlrealQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1825 dkslvsrQEAKIRELETRLEfertqvkRLESLASRLKENMEKLTEERD---QRIAA-ENREkEQNKRLQRQLRDTKEEMG 1900
Cdd:COG0497 294 -------DPERLEEVEERLA-------LLRRLARKYGVTVEELLAYAEelrAELAElENSD-ERLEELEAELAEAEAELL 358
|
....*
gi 1093953565 1901 ELARK 1905
Cdd:COG0497 359 EAAEK 363
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1326-1574 |
9.30e-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: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1326 AETAERLRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEF 1405
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1485
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1486 AQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1565
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1093953565 1566 QEEELDEQA 1574
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1584-1905 |
1.01e-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: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1584 KLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLsdqvnrrdfesE 1663
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASL-----------E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1664 KRLRkDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcaAAVKARKaMEVEIEDLHLQIDDIAKAKTALE 1743
Cdd:pfam15905 129 KQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKE--VMAKQEG-MEGKLQVTQKNLEHSKGKVAQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1744 EQLSRLQREKNEiqnrleedqedmnelmkkHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1823
Cdd:pfam15905 205 EKLVSTEKEKIE------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1824 vdkslvsrqEAKIRELETRLEFERTQVKRLESlasrLKENMEKLTEERDQRIAAENREkeqnkrLQRQLRDTKEEMGELA 1903
Cdd:pfam15905 267 ---------EEKEQELSKQIKDLNEKCKLLES----EKEELLREYEEKEQTLNAELEE------LKEKLTLEEQEHQKLQ 327
|
..
gi 1093953565 1904 RK 1905
Cdd:pfam15905 328 QK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1725-1966 |
1.08e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLhLQI------DDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdlaqinDLQAQLEE 1797
Cdd:PHA02562 156 VEDL-LDIsvlsemDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1798 ANKEKQELQEKLQALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeRTQVKRLESLASRLKENMEKLT-----EERD 1872
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKGGVCPTctqqiSEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1873 QRIAAEnreKEQNKRLQRQLRDTKEEMGELARKE---AEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1949
Cdd:PHA02562 299 DRITKI---KDKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260
....*....|....*....|..
gi 1093953565 1950 DEMES-----DENEDLINSEGD 1966
Cdd:PHA02562 376 DNAEElaklqDELDKIVKTKSE 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1591-1815 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1591 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEeYEDKQKVL---REKRELEGKLATLSDQVNRrdfesekrLR 1667
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-FRQKNGLVdlsEEAKLLLQQLSELESQLAE--------AR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1668 KDLKRTKALLADAQLMLDHLKNSAPSKRE---IAQLKNQLEESEFTCAAAVK-------ARKAMEVEIEDLHLQIDD-IA 1736
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1737 KAKTALEEQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1815
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1265-1934 |
1.64e-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: 53.42 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1344
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1345 YDALKKQmeVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREvdFTKKRLQQEFEDKLEVEQ--QNKRQLE-- 1420
Cdd:COG3096 594 IKELAAR--APAWLAAQDALERLREQSGE----------ALADSQEVTA--AMQQLLEREREATVERDElaARKQALEsq 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1421 -RRLgdLQADSEESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ---------- 1472
Cdd:COG3096 660 iERL--SQPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcped 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1473 --------RRFDSELSQAHEE--------------------------AQREKlQREKLQREKDML---LAEAFSLKQQLE 1515
Cdd:COG3096 734 lyliegdpDSFDDSVFDAEELedavvvklsdrqwrysrfpevplfgrAAREK-RLEELRAERDELaeqYAKASFDVQKLQ 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1516 EKDMDIAGF--TQKVVSLEAElqdissqeskDEASLAKVKKQLRDLEAKVKDQEEELDEQAgtiQMLEQAKLRLEMEMER 1593
Cdd:COG3096 813 RLHQAFSQFvgGHLAVAFAPD----------PEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKL 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1594 MRQTHSKEMESRDEEVEEARQscqkklkqmevQLEEEYEDKQKVLREK---RELEGKLATLsdqvnRRDFESEKRLRKDL 1670
Cdd:COG3096 880 LPQANLLADETLADRLEELRE-----------ELDAAQEAQAFIQQHGkalAQLEPLVAVL-----QSDPEQFEQLQADY 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1671 KRTKALLADAQLMLDHLKNsapskreiaqlknqleeseftcaaaVKARKAmeveiedlHLQIDD---IAKAKTALEEQLs 1747
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSE-------------------------VVQRRP--------HFSYEDavgLLGENSDLNEKL- 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1748 rlqREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDLAqinDLQAQLEEANKEKQELQEKLQALQSQVeflEQSMVDKS 1827
Cdd:COG3096 990 ---RARLE---QAEEARREAREQLRQAQAQYSQYNQVLA---SLKSSRDAKQQTLQELEQELEELGVQA---DAEAEERA 1057
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1828 LVSRQE---------AKIRELETRLEFERTQvkrLESLASRLKENMEKLTEERDQRIAAenreKEQNKRLQRQLRDTKEE 1898
Cdd:COG3096 1058 RIRRDElheelsqnrSRRSQLEKQLTRCEAE---MDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVE 1130
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1093953565 1899 ----MGELARKEAEASRkkhelEMDLESLEAANQSlQADL 1934
Cdd:COG3096 1131 rrlhRRELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1669 |
1.84e-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: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1317 GESASQLLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingEVDDDDaggewrLKYERAVREVDf 1396
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA------EYSWDE------IDVASAEREIA- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1397 tkkRLQQEFEDkLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQR--- 1473
Cdd:COG4913 672 ---ELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlel 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1474 --RFDSELSQAHEEAQREKLqREKLQREKDMLLAEAFSLKQQLEEK--------DMDIAGFTQKVVSLE---AELQDISS 1540
Cdd:COG4913 748 raLLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLPeylALLDRLEE 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1541 QEskdeasLAKVKKQLRDLEAKVKDQE-----EELDEQAGTI--------QMLEQAK------LRLEMEmermrqthske 1601
Cdd:COG4913 827 DG------LPEYEERFKELLNENSIEFvadllSKLRRAIREIkeridplnDSLKRIPfgpgryLRLEAR----------- 889
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1602 mESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVL---------REKRELEGKLATLSDQVNRRDFESEKRLRKD 1669
Cdd:COG4913 890 -PRPDPEVREFRQELRAVTSGASLFDEELSEARFAALkrlierlrsEEEESDRRWRARVLDVRNHLEFDAEEIDRED 965
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1273-1825 |
1.91e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1273 EEIQQLRSKLEKAEKERNELRLNSDRLES---RISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALK 1349
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1350 KqmEVMEMEVMEARLIRAAEINGEVddddAGGEWRLKyERAVREVDFTKKRLQQEFEDKLEVEqqNKRQLERRLGDLQAD 1429
Cdd:PRK01156 253 R--YESEIKTAESDLSMELEKNNYY----KELEERHM-KIINDPVYKNRNYINDYFKYKNDIE--NKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1430 SEESQRALQQLKK------KCQRLTAELQDTKLHLEGQQ------VRNHELEKKQRRfdselsqahEEAQREKLQREKLQ 1497
Cdd:PRK01156 324 YHAIIKKLSVLQKdyndyiKKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIE---------EYSKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1498 REKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEEL 1570
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1571 DEQAGTiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLEEeYEDKQKVLREKrelEG 1646
Cdd:PRK01156 475 NEKKSR---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADLED-IKIKINELKDK---HD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1647 KLATLSDQVNRRDFESekrlrKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavKARKAMEVEIE 1726
Cdd:PRK01156 547 KYEEIKNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1727 DLHLQIDDIAKAktaLEEQLSRLQREKNEIQNR-------------LEEDQEDMNELMKKHKAAVAQASRDLAQINDLQA 1793
Cdd:PRK01156 612 DDKSYIDKSIRE---IENEANNLNNKYNEIQENkilieklrgkidnYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688
|
570 580 590
....*....|....*....|....*....|..
gi 1093953565 1794 QLEEANKEKQELQEKLQALQSQVEFLEQSMVD 1825
Cdd:PRK01156 689 ALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1605-1933 |
1.92e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1605 RDEEVEEArQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEgklatlsdqvnrrdfESEKRLRKDLKRTKALLADAQLML 1684
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAELN---------------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1685 DHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1760
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1761 EEDQEdMNELMKkhkAAVAQASRDLAQindLQAQLEEANKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1834
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1835 K--IRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqriaAENREKEQNKRLQRQLRDtkeemgelarkEAEASRK 1912
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD-----------EDELEQL 559
|
330 340
....*....|....*....|.
gi 1093953565 1913 KHELEMDLESLEAANQSLQAD 1933
Cdd:PRK04863 560 QEELEARLESLSESVSEARER 580
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1597-1916 |
1.92e-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: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1597 THSKEMESRD---------EEVEEARQSCQKKLKQMEVQLEE------------EYEDKQKVLREKRELEGKLATLSDQV 1655
Cdd:pfam12128 188 MHSKEGKFRDvksmivailEDDGVVPPKSRLNRQQVEHWIRDiqaiagimkirpEFTKLQQEFNTLESAELRLSHLHFGY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1656 NrrdfESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDI 1735
Cdd:pfam12128 268 K----SDETLIASRQEERQETSAELNQLLRTLDD------QWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1736 AKAKTALE-EQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA----AVAQASRDLAQIND-LQAQLEEANKEKQELQEKL 1809
Cdd:pfam12128 338 DIETAAADqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRrrskIKEQNNRDIAGIKDkLAKIREARDRQLAVAEDDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1810 QALQSQV-EFLEQSMVDKSLVSRQ-EAKIRELETRL------EFERTQVKRLESLASRLKENMEKLTEER----DQRIAA 1877
Cdd:pfam12128 418 QALESELrEQLEAGKLEFNEEEYRlKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVerlqSELRQA 497
|
330 340 350
....*....|....*....|....*....|....*....
gi 1093953565 1878 ENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHEL 1916
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
218-307 |
2.40e-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: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 218 LRELELQRRPTGDFGFSLR------RTTMLDRGPEGQACRRVVHfaePGAGTKDlalG-LVPGDRLVEINGHNVESKSRD 290
Cdd:cd06701 4 LQELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGATHQ 77
|
90
....*....|....*..
gi 1093953565 291 EIVEMIRQSGDSVRLKV 307
Cdd:cd06701 78 EAVRILRSVGDTLTLLV 94
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1617-1929 |
2.66e-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: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1617 QKKLKQMEVQLEE---EYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPS 1693
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAME--VEIEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1769
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1770 lmkKHKAAVAQASRDLAQindLQAQLEEanKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFER 1847
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1848 TQVKRLESLASRLKENMEKLTEERDQRIaaENREKEQNKRLQR-QLRDTKEEMgelARKEAEASRKKHELEMDLESLEAA 1926
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEHL--KDVLVEQEIELQReFLQDIKEKV---EEERAGRLLKLNELLANLKGLEKA 428
|
...
gi 1093953565 1927 NQS 1929
Cdd:pfam09731 429 TSS 431
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1417-1573 |
2.76e-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: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDtklhlegqqvrnheLEKKQRRFDSELSQAHEEAQR--EKLQRE 1494
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------------LEKEIKRLELEIEEVEARIKKyeEQLGNV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1495 KLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1573
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1440-1716 |
3.00e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1440 LKKKCQRLTAELQ--DTKLHLEGQQVrnheleKKQRRFDSELsqaheeaqrEKLQREKLQREKDM---LLAEAFSLKQQL 1514
Cdd:PHA02562 172 NKDKIRELNQQIQtlDMKIDHIQQQI------KTYNKNIEEQ---------RKKNGENIARKQNKydeLVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1515 EEkdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK--DQEEELDEQAGT----IQMLEQAKLRLE 1588
Cdd:PHA02562 237 EE--------------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVcptcTQQISEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1589 MEMERMrqthsKEMESRDEEVEEARQScqkklkqmEVQLEEEYEDKQKVLRE-KRELEGKLATLSDQVNrrdfeSEKRLR 1667
Cdd:PHA02562 303 KIKDKL-----KELQHSLEKLDTAIDE--------LEEIMDEFNEQSKKLLElKNKISTNKQSLITLVD-----KAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1668 KDLKRTKALLADaqlmldhlknsapSKREIAQLKNQLEESEFTCAAAVK 1716
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 |
3.06e-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: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGdFGFSLRRTTMLDRGPEGQACRrVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTDQPYIPNDSGIY-VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAVELFRN 76
|
90
....*....|
gi 1093953565 299 SGDSVRLKVQ 308
Cdd:cd06709 77 AGEDVKLKVQ 86
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1556-1918 |
3.76e-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: 51.46 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQE--EELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEd 1633
Cdd:pfam13868 8 LRELNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1634 KQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKAlladaqlmldhlknsapsKREIAQLKNQLEESeftcaa 1713
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQAEW------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1714 avKARKAMEVEIEDLHLQ--IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDL 1791
Cdd:pfam13868 143 --KELEKEEEREEDERILeyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1792 QAQLEEANKEKQELQEKLQALQSQVEFleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1871
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIEL------------KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1872 DQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEM 1918
Cdd:pfam13868 289 LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1567-1923 |
4.14e-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: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1567 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE 1640
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREqwerqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1641 K--------------RELEGKLATLSDQVNRRDFESEkRLRKDLKRTKALLADAQlmldhlknsapskREIAQLKNQLEE 1706
Cdd:pfam07888 117 KdallaqraaheariRELEEDIKTLTQRVLERETELE-RMKERAKKAGAQRKEEE-------------AERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1707 SEFTCaaavkarKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLA 1786
Cdd:pfam07888 183 TEEEL-------RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1787 QINDLQAQLEEANKEKQEL-QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERtqvKRLESLASRLKENME 1865
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK---DRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1866 KLTEERDQRIAAE---NREKEQNKrlqRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1923
Cdd:pfam07888 333 RLQEERMEREKLEvelGREKDCNR---VQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1406-1810 |
4.62e-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: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1477
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQREKLQREKDMLLAEA-FSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1556
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1557 RDLEAKVKDQEEELDEQAGTIQMLEQAKlrlememermrqthskemESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQK 1636
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------------TDREKAEEEAKRRADAKLKEAVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1637 VLREKRELEGKLATlsdqvnrrdfesekrlrKDLKRTKALLADAQLMLDHLKN-SAPSKREIAQLKNQLEESEftcaaav 1715
Cdd:NF033838 262 KRRAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPSpSLKPEKKVAEAEKKVEEAK------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1716 kaRKAMEVEIED-----------LHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASR 1783
Cdd:NF033838 318 --KKAKDQKEEDrrnyptntyktLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR 387
|
410 420
....*....|....*....|....*..
gi 1093953565 1784 dLAQINDLQAQLEEANKEKQELQEKLQ 1810
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 |
4.87e-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: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 224 QRRPTGDFGFSLRrttmldrgpeGQAcrrVVHF--AEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGD 301
Cdd:cd06744 4 VYRGNGSFGFTLR----------GHA---PVYIesVDPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGS 68
|
....*..
gi 1093953565 302 SVRLKVQ 308
Cdd:cd06744 69 MPTLVVE 75
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1756-1950 |
5.18e-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: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1756 IQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKE----KQELQEKLQALQSQVEFLEQSMVD------ 1825
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesrVAELKEELRQSREKHEELEEKYKElsasse 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1826 -----KSLVSRQ----EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQriaaenrEKEQNKRLQRQLRDTK 1896
Cdd:pfam07888 112 elseeKDALLAQraahEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKE-------EEAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1897 EEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1950
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1446-1820 |
5.31e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1446 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFT 1525
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1526 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMErMRQTHSKEMESR 1605
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1606 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLD 1685
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1686 HLKNSAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1765
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1766 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLE 1820
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1388-1746 |
5.50e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1388 ERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERrlgdLQADSEESQRALQQLKKKCQRLTAELQdtklhlegqqvrnhE 1467
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQ--------------A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1468 LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEA 1547
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 SLAKVKKQlrDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEV 1625
Cdd:COG4372 172 ELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLE 1705
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1093953565 1706 ESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1746
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1606-1925 |
5.52e-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: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1606 DEEVEEARQScQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRrdfesekrLRKDLKRTKALLADAQLMLD 1685
Cdd:pfam19220 37 EAILRELPQA-KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE--------LVARLAKLEAALREAEAAKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1686 HLKnsapskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALE-------EQLSRLQREKNEIQN 1758
Cdd:pfam19220 108 ELR------IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgelatarERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1759 RLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQelqeklqalqsqvefleqsmvdkslvsRQEAKIRE 1838
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERE---------------------------RAEAQLEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1839 LETRLEFERT-QVKRLESLASRLKENMEKLTEERDqriaaenrekeqnkrlqrQLRDTKEEMGELARKEAEASRKKHELE 1917
Cdd:pfam19220 235 AVEAHRAERAsLRMKLEALTARAAATEQLLAEARN------------------QLRDRDEAIRAAERRLKEASIERDTLE 296
|
....*...
gi 1093953565 1918 MDLESLEA 1925
Cdd:pfam19220 297 RRLAGLEA 304
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
5.74e-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: 5.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1093953565 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 |
6.20e-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: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLRRTTMldrgPEGQACRRVVHfaEPgagtkdlALG---LVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 1093953565 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 ... |
550-831 |
6.21e-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: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 550 LLEAFGNSPTIINGNATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 618
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 619 G-----TLRTELHLNHL----------AENNVFGIVplAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYH 683
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 684 LGaaGATKEAAEAGRKQFARHEWA----QKAAYLLGC-SLEELSSAIFKhqhKGGTLQRSTSFRQGPEESGLGDGTGPKL 758
Cdd:cd14894 413 LG--NIELDYREVSGKLVMSSTGAlnapQKVVELLELgSVEKLERMLMT---KSVSLQSTSETFEVTLEKGQVNHVRDTL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 759 SALeclegmaagLYSELFTLLVSLVNRALKSS-------QHSLCS----------MMIVDTPGFQNPEQGgsargaSFEE 821
Cdd:cd14894 488 ARL---------LYQLAFNYVVFVMNEATKMSalstdgnKHQMDSnasapeavslLKIVDVFGFEDLTHN------SLDQ 552
|
330
....*....|
gi 1093953565 822 LCHNYTQDRL 831
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 |
6.43e-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: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLR----RTTMLDRGPegqacrrVVHFAEPGAGTKDLALgLVPGDRLVEINGHNVESKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 1093953565 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1408-1783 |
6.49e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1408 KLEVEQQNKRQLERRLGDLQADSEESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1483
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1484 EEAQREKLQREKLQREKDMLLAEAFSLKQQLEEkdmdiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV 1563
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1564 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmEVQLEEEYEDKQKVLREKRE 1643
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI----------ESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1644 LEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEV 1723
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1724 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR 1783
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
6.78e-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: 6.78e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1093953565 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1543-1658 |
6.80e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 51.30 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1543 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1622
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 1093953565 1623 MEVQLEE---EYEDKQKVLREKRELEGKLATLSDQVNRR 1658
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEK 618
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1461-1935 |
7.17e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.37 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1461 QQVRNHELEKKQRRFDS--ELSQAHEEAQR----EKLQREKLQREkdmLLAEAFSLKQQLeekDMDIAGFTQKVVSleae 1534
Cdd:NF041483 76 QLLRNAQIQADQLRADAerELRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQL---DQELAERRQTVES---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1535 lqDISSQESKDEASLAKVKKQLRDLeakvkdqeeeLDE-QAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEE-- 1611
Cdd:NF041483 146 --HVNENVAWAEQLRARTESQARRL----------LDEsRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAil 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1612 --ARQSCQKKLKQMEVQLEEEyEDKQKVLR-----EKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLML 1684
Cdd:NF041483 214 rrARKDAERLLNAASTQAQEA-TDHAEQLRsstaaESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1685 DHLKNSAPS---------KREIAQLKNQ-LEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEE--QLSRLQRE 1752
Cdd:NF041483 293 AKQLASAESaneqrtrtaKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTaaQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1753 KNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQ--------ELQEKLQALQSQVEFL 1819
Cdd:NF041483 373 AEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMVDKSLVSRQEAKireletrlefeRTQVKRLESLASRLKENMEKLTEERDQ--RIAAENREKEQNKRLQR--QLRDT 1895
Cdd:NF041483 453 RAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEAIERatTLRRQ 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1093953565 1896 KEEMGELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1935
Cdd:NF041483 522 AEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1499-1889 |
9.37e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1499 EKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1558
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1559 LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1622
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1623 MEVQLEEeYEDKQKVLREK-RELEGKLATLSDQVNRRD--FESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREiAQ 1699
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1700 LKNQLEESEftcaaavkarkameveiEDLHLQiddiakaktaleEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAava 1779
Cdd:PRK04863 518 LRMRLSELE-----------------QRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEA--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 qasrdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRLEFERTQV-------KR 1852
Cdd:PRK04863 566 -------RLESLSESVSEARERRMALRQQLEQLQARIQRLAA----------RAPAWLAAQDALARLREQSgeefedsQD 628
|
410 420 430
....*....|....*....|....*....|....*..
gi 1093953565 1853 LESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQ 1889
Cdd:PRK04863 629 VTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1546-1906 |
9.63e-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: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1546 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscqkklk 1621
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL--------- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1622 qmEVQLEEEyedkqkvlrekrelEGKLATLSDQVNRRDFESEkRLRKDLKRTKALLADAQLMLDHLKNSAPSKReiaQLK 1701
Cdd:COG3096 360 --TERLEEQ--------------EEVVEEAAEQLAEAEARLE-AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1702 NQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAVA-- 1779
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVErs 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 ----QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdkslvSRQEAKIRELETRLEFERTQVKRLES 1855
Cdd:COG3096 492 qawqTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQ--------------QNAERLLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1856 LASRLKENMEKLTEErdqriAAENREkeQNKRLQRQLRDTKEEMGELARKE 1906
Cdd:COG3096 558 LLAELEAQLEELEEQ-----AAEAVE--QRSELRQQLEQLRARIKELAARA 601
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1261-1656 |
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 1093953565 1261 VQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRIseltseLTDERNTGESASQLldaetaerlraEKEMKE 1340
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1341 LQTQYDalkkqmevmemevmearliRAAEINGEVDDDDAggewRLKYERAVREVDFTK----------KRLQQEFEDKLE 1410
Cdd:PRK04778 177 LEEEFS-------------------QFVELTESGDYVEA----REILDQLEEELAALEqimeeipellKELQTELPDQLQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1411 VEQQNKRQLER---RLGDLQADSEesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK--------QRRFDSEl 1479
Cdd:PRK04778 234 ELKAGYRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydilEREVKAR- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1480 SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQ--QLEEKDMDIA-GFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1556
Cdd:PRK04778 306 KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEEL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1557 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKKLKQMEVQLE 1628
Cdd:PRK04778 386 EEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELE 465
|
410 420
....*....|....*....|....*...
gi 1093953565 1629 EEYEDKQKVLREKRELEGKLATLSDQVN 1656
Cdd:PRK04778 466 EKPINMEAVNRLLEEATEDVETLEEETE 493
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1524-1591 |
1.49e-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: 1.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1524 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML--EQAKLRLEMEM 1591
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1406-1837 |
1.57e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1482
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1483 HEEAQREKLQREKLQREKDML--LAEAFSLkqqleekdMDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1560
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1561 akvkdqeEELDEQAGTIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1632
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1633 DKQKVLREKRELEGKLatlsdQVNRRDFESEK-RLRKDLKRTKALLADAQLMLDHLKNSAPSKREI-AQLKNQLEesEFT 1710
Cdd:PRK04863 975 DAAEMLAKNSDLNEKL-----RQRLEQAEQERtRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1711 CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDLAQI 1788
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1789 NDLQAQL---EEANKEKQEL-------QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIR 1837
Cdd:PRK04863 1128 NGVERRLhrrELAYLSADELrsmsdkaLGALRLAVADNEHLRDVLRLSEDPKRPERKVQ 1186
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1614-1785 |
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 1093953565 1614 QSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrDFESE-KRLRKDLKRTKALLADAQLMLDHLKNSap 1692
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE--DLEKEiKRLELEIEEVEARIKKYEEQLGNVRNN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1693 skREIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMN 1768
Cdd:COG1579 89 --KEYEALQKEIESLK-------RRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1093953565 1769 ELMKKHKAAVAQASRDL 1785
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1416-1840 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQAD-------SEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1481
Cdd:pfam05701 37 RKLVELELEKVQEEipeykkqSEAAEAAKAQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1482 ---AHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEkdmdiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1557
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1558 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKV 1637
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1638 LREKREL----EGKLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQLEEsEFTCA 1712
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1713 AAVKARKAMEveiedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDLAQINDL- 1791
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLa 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1792 QAQLEEANKEKQElQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1840
Cdd:pfam05701 401 QAAREELRKAKEE-AEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1757-1950 |
1.82e-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: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1757 QNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1836
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1837 RELETRLEFERTQvkrLESLASRLKENMEKLTEERD------QRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1910
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTrperaqQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1093953565 1911 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1950
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1551-1899 |
2.13e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1551 KVKKQLRDLEAKVKDQEEELDeqagtiQMLEqaklrlemEMERMRQTHSKEMesrdEEVEearqscqkklkqmevQLEEE 1630
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIE------QILE--------ELQELLESEEKNR----EEVE---------------QLKDL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1631 YEDKQKVLREKR--------ELEGKLATLSDQVNRRDFESEK-----------RLRKDLKRTKALLADAQLMLDHLKNSA 1691
Cdd:PRK04778 149 YRELRKSLLANRfsfgpaldELEKQLENLEEEFSQFVELTESgdyveareildQLEEELAALEQIMEEIPELLKELQTEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1692 PSkrEIAQLKN---QLEESEFtcaaaVKARKAMEVEIEDLHLQIDDiakaktaLEEQLSRLQREKNEIQNR-LEEDQEDM 1767
Cdd:PRK04778 229 PD--QLQELKAgyrELVEEGY-----HLDHLDIEKEIQDLKEQIDE-------NLALLEELDLDEAEEKNEeIQERIDQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1768 NELMKKHKAAVAQASRDLAQINDLQAQLEEANKE-KQELQ-------------EKLQALQSQVEFLE-QSMVDKSLVSRQ 1832
Cdd:PRK04778 295 YDILEREVKARKYVEKNSDTLPDFLEHAKEQNKElKEEIDrvkqsytlneselESVRQLEKQLESLEkQYDEITERIAEQ 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1833 EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEErdqriaaENREKEQNKRLQRQLRDTKEEM 1899
Cdd:PRK04778 375 EIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKD-------ELEAREKLERYRNKLHEIKRYL 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1406-1615 |
2.31e-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: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1485
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1486 AQREKLQREKLqrekDMLL-AEAFS--------LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1556
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1557 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1615
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1700-1934 |
2.32e-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: 49.12 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1700 LKNQLEESEFTCAAAVKARKAMEVEIEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1779
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSR--QEAKIRELETRLEFERTQVK 1851
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELermkerAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1852 RL--------------ESLASRLKENMEKLTeerdQRIAAENREKEQNKRLQRQLRDTKEEmgelarkeAEASRKKHE-L 1916
Cdd:pfam07888 189 SLskefqelrnslaqrDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQER--------LNASERKVEgL 256
|
250
....*....|....*...
gi 1093953565 1917 EMDLESLEAANQSLQADL 1934
Cdd:pfam07888 257 GEELSSMAAQRDRTQAEL 274
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1713-1904 |
2.72e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1713 AAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDLA------ 1786
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1787 ------QINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLAS-R 1859
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGiD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1860 LKENMEKLT--EERDQRIAAEN---REKEQNKRLQRQLRDTKEEMG---ELAR 1904
Cdd:COG1842 160 SDDATSALErmEEKIEEMEARAeaaAELAAGDSLDDELAELEADSEvedELAA 212
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1661-1934 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1661 ESEKRLRKDLKRTKALLADAQlmlDHLKNSAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEIEDLHLQIDdiaKAK 1739
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1740 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL 1819
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMVDKSLVSR-----QEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQrIAAENREKeqnkrlQRQLRD 1894
Cdd:pfam09311 167 EEKLKAEILFLKeqiqaEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQ-LENGLTEK------IRQLED 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1093953565 1895 TKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADL 1934
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 |
3.08e-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: 3.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1093953565 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1400-1580 |
3.14e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1400 RLQQEFEDKLEVEQQNKRQLER---RLGDLQADSEESQRALQQLKKKCQRLTAELQ----DTKLHLEG-------QQVrn 1465
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEEltdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkVIKMYEKGgvcptctQQI-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1466 HELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLA---EAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE 1542
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
170 180 190
....*....|....*....|....*....|....*...
gi 1093953565 1543 SKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1580
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1481-1707 |
3.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1481 QAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1560
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1561 AKVKDQEEELDEQA----------GTIQMLEQAKL------RLEMeMERMRQTHSKEMesrdEEVEEARQSCQKKLKQME 1624
Cdd:COG3883 79 AEIEERREELGERAralyrsggsvSYLDVLLGSESfsdfldRLSA-LSKIADADADLL----EELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1625 VQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQL 1704
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLA--------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
...
gi 1093953565 1705 EES 1707
Cdd:COG3883 226 AAA 228
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1607-1877 |
3.27e-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: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1607 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKVLREKRE----LEGKLATLSDQVNR-----RDFESEKRLRKD 1669
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAEsskrLNENANNLIKQFENtkekiAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1670 LKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKtALEEQLSRL 1749
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1750 QREKNEIQNRLEEDQEDMNELMKKHKAAVAQasrdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV 1829
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADR------QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1830 SRQEAK---IRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA 1877
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 |
3.55e-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: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 217 TLRELELQRRPTGDFGFSLRrttmldrGPEGQACRRVVHFAEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06737 1 KLRLVRLDRRGPESLGFSVR-------GGLEHGCGLFVSHVSPG-SQADNK-GLRVGDEIVRINGYSISQCTHEEVINLI 71
|
90
....*....|....
gi 1093953565 297 RQSgDSVRLKVQPI 310
Cdd:cd06737 72 KTK-KTVSLKVRHV 84
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1724-1978 |
3.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1724 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQ 1803
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1804 ELQEKLQALQSQVEFLEQSmvdkslvsrqeakireletrlefertqvkrleslASRLKENMEKLTEERDQRIAAENREKE 1883
Cdd:COG4372 112 ELQEELEELQKERQDLEQQ----------------------------------RKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1884 QNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINS 1963
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250
....*....|....*
gi 1093953565 1964 EGDSDVDSELEDRVD 1978
Cdd:COG4372 238 LLDALELEEDKEELL 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1694-1925 |
3.83e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1773
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 HKAAVaQASRDLAQINDLQAQLEEA--------NKEKQ------ELQEKLQALQSQVEfleqsmvdkslvsrQEAKIREL 1839
Cdd:COG1340 101 LAELN-KAGGSIDKLRKEIERLEWRqqtevlspEEEKElvekikELEKELEKAKKALE--------------KNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1840 ETRLEFERTQ-------VKRLESLASRLKENMEKLTEERDQ--------------RIAAENREKEQNKRLQRQLRDTKEE 1898
Cdd:COG1340 166 RAELKELRKEaeeihkkIKELAEEAQELHEEMIELYKEADElrkeadelhkeiveAQEKADELHEEIIELQKELRELRKE 245
|
250 260
....*....|....*....|....*..
gi 1093953565 1899 MGELARKEAEASRKKHELEMDLESLEA 1925
Cdd:COG1340 246 LKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1512-1811 |
3.93e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1512 QQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAgtiqmleqaklrlemem 1591
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK----ELREEA----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1592 ermrQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKVLREKRELEGKLATLSDQVNR---------RDFES 1662
Cdd:COG1340 60 ----QELREKRDELNEKVKELKEERDELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1663 EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL 1742
Cdd:COG1340 135 EKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1743 EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLaqindLQAQLEEANKEKQELQEKLQA 1811
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-----REKEKEELEEKAEEIFEKLKK 278
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1282-1627 |
4.61e-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: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1282 LEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRA-EKEMKELQTQYDALKKQMEVMEMEVM 1360
Cdd:pfam15964 355 LIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1361 EARLIRAAEingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQEfedkLEVEQQNKRQLERRLGDLQADSEES 1433
Cdd:pfam15964 435 EAQKQLASQ---EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGRQ----LEIKDQEIEKLGLELSESKQRLEQA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1434 QRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-SQAHEEAQREK----------LQREKLQREK 1500
Cdd:pfam15964 508 QQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkAQALQAQQREQeltqkmqqmeAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1501 DMLLAEAFSLKQQLEEKdmdiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgtIQ-- 1578
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEE----------CCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQC--VQhg 650
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1579 -MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQMEVQL 1627
Cdd:pfam15964 651 rMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1399-1901 |
4.73e-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: 48.36 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1399 KRLQQEFEDKLEVeqqnkrqLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSE 1478
Cdd:pfam15964 223 EKLKLLYEAKTEV-------LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1479 LSQAHEEAQREKLQRekLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QL 1556
Cdd:pfam15964 290 LAQTHTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQC 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1557 RDLEAKVKDQEEELDEQAGTiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqK 1636
Cdd:pfam15964 359 EQLKSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------K 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1637 VLREKRELEGKLATLSDQVNRRDFESEK---RLRKDLKRTKALLADAQLmlDHLKNSAPSKREIaQLKNQleeseftcaa 1713
Cdd:pfam15964 422 VTREKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAEK--EHREYRTKTGRQL-EIKDQ---------- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1714 avkarkamevEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNeLMKKHKAAVAQASRDLAQINDLQA 1793
Cdd:pfam15964 489 ----------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLH-LTRLEKESIQQSFSNEAKAQALQA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1794 QLEEankekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQ 1873
Cdd:pfam15964 558 QQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRS 616
|
490 500
....*....|....*....|....*...
gi 1093953565 1874 RIAAENREKEQNKRLQRQLRDTKEEMGE 1901
Cdd:pfam15964 617 EVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1429-1908 |
5.03e-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: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1429 DSEESQRALQQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEEAQREKLQREKLQ 1497
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1498 RE--KDMLLAEAFSLKQQLEE---KDMDIAGFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEakvkdqeeE 1569
Cdd:pfam05622 78 LEtaRDDYRIKCEELEKEVLElqhRNEELTSLAEEAQALKDEmdiLRESSDKVKKLEATVETYKKKLEDLG--------D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQagtIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1648
Cdd:pfam05622 150 LRRQ---VKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1649 ATLSDQVNRRDFEsekrlRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLeeseftcaaavkARKAMEVEIEdl 1728
Cdd:pfam05622 221 EALQKEKERLIIE-----RDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNL------------AAEIMPAEIR-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1729 hlqiddiakaktaleEQLSRLQREkneiqnrleedqedmNELMKkhkaaVAQASRDLAQINDLQAQLEEANKEKQELQEK 1808
Cdd:pfam05622 282 ---------------EKLIRLQHE---------------NKMLR-----LGQEGSYRERLTELQQLLEDANRRKNELETQ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1809 LQALQSQVEFLEQsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA-ENREKEQNKR 1887
Cdd:pfam05622 327 NRLANQRILELQQ-------------QVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKkEQIEELEPKQ 393
|
490 500
....*....|....*....|.
gi 1093953565 1888 LQRQLRDTKEEMGELARKEAE 1908
Cdd:pfam05622 394 DSNLAQKIDELQEALRKKDED 414
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1471-1874 |
5.28e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1471 KQRRFDSElsqaheEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMD-IAGFTQKVVSLEAELQDISSQesKDEASL 1549
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1550 AKVKKQLRdleaKVKDQEEELDEQAGT-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1628
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1629 EEYEDKQKVLREKRELEgklaTLSDQVNRRDFESEKRLRKDLKRTKALLadaqLMLDHLKNSAPS-KREIAQLKNQL--- 1704
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLS----KELDVLKEENMLlKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1705 EESEFTCAAAVKARKAMEVEIEDLHLQI----DDIAKAKT----ALEEQLSRLQREKNEIQNRLEedqedmnelmkkHKA 1776
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPlqydCWWEKVENLQDLLDRATNQVE------------KAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1777 AVAQASRDLA-QINDLQAQLEEANKEKQELqEKLQALQSQVefleqsmvdKSLVSRQEAKIRELETrlefertQVKRLES 1855
Cdd:PLN02939 321 LVLDQNQDLRdKVDKLEASLKEANVSKFSS-YKVELLQQKL---------KLLEERLQASDHEIHS-------YIQLYQE 383
|
410
....*....|....*....
gi 1093953565 1856 LASRLKENMEKLTEERDQR 1874
Cdd:PLN02939 384 SIKEFQDTLSKLKEESKKR 402
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1600-1815 |
5.45e-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: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1600 KEMESRDEEVEEARQSCQKKLKQMEVQLE---EEYEDKQKVLREKRE----LEGKLATLSDQVNRRDFESEKRLRkDLKR 1672
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEelnEEYNELQAELEALQAeidkLQAEIAEAEAEIEERREELGERAR-ALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1673 TKALLADAQLML------DHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1746
Cdd:COG3883 98 SGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1747 SRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1815
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
6.07e-05 |
|
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 42.52 E-value: 6.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1093953565 269 GLVPGDRLVEINGHNVESKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1536-1788 |
6.59e-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: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1536 QDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD---EQAGTIQMLEQAKLRLEmEMERMRQTHSkEMESRDEEVEEA 1612
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVDLSEEAKLLLQ-QLSELESQLA-EARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1613 RQSCQKKLKQMEVQLEEEYEDK--QKVLREKRELEGKLATLSdqvnrrdfeseKRLRKDLKRTKALladaqlmldhlkns 1690
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELS-----------ARYTPNHPDVIAL-------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1691 apsKREIAQLKNQLEEseftcaAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRL---QREKNEIQNRLEEDQEDM 1767
Cdd:COG3206 297 ---RAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY 367
|
250 260
....*....|....*....|.
gi 1093953565 1768 NELMKKHKAAVAQASRDLAQI 1788
Cdd:COG3206 368 ESLLQRLEEARLAEALTVGNV 388
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1769-1944 |
6.61e-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: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1769 ELMKKHKAAVAQA--------SRDLAQINDLQAQLEEANK--------------EKQELQEKLQALQSQVEFLEQSMV-- 1824
Cdd:pfam13851 1 ELMKNHEKAFNEIknyynditRNNLELIKSLKEEIAELKKkeerneklmseiqqENKRLTEPLQKAQEEVEELRKQLEny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1825 --DKSLVSRQEAKIRELEtrleferTQVKRLESLASRLKENMEKLTEERD---QRIAAENREKEQNKRLQRQLRDTK-EE 1898
Cdd:pfam13851 81 ekDKQSLKNLKARLKVLE-------KELKDLKWEHEVLEQRFEKVERERDelyDKFEAAIQDVQQKTGLKNLLLEKKlQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1899 MGE-LARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL 1944
Cdd:pfam13851 154 LGEtLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
7.28e-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: 7.28e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1093953565 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1585-1935 |
7.52e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.93 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1585 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKVLrekrELEGKLATLSDQVNRRDFESEK 1664
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1665 RLRkdlkrtkALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavkarkameveiedlhlQIDDIAKAKTALEE 1744
Cdd:PLN03229 505 MHP-------VLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1745 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDLAQINDLQAQLEEANKEKQ-ELQEKLQALQSQVEFL 1819
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMVDKSLVSRQE---AKIREL--ETRLEFERT-QVKRLESLASRLKENMEKLTEERDQriaaenREKEQNKRLQRQLR 1893
Cdd:PLN03229 632 TKKNKDTAEQTPPPnlqEKIESLneEINKKIERViRSSDLKSKIELLKLEVAKASKTPDV------TEKEKIEALEQQIK 705
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1093953565 1894 DTKEEmgelARKEAEASRKKHELEMDLESLEAANQSLQADLK 1935
Cdd:PLN03229 706 QKIAE----ALNSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1431-1645 |
8.31e-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: 45.81 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1431 EESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQaHEeaqreklqreklqREKDMLLAE 1506
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQ-HE-------------RMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1507 AFSLKQQLEEKDM-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGTIQMLEQAK 1584
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1585 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKVLREkRELE 1645
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
9.72e-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: 9.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1711-1908 |
1.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1711 CAAAVKARKAMEVEIEDLHLQIDDI-----AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1785
Cdd:PRK12704 19 VIGYFVRKKIAEAKIKEAEEEAKRIleeakKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 AQindlqaQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRlefertQVKRLESLASrlkenme 1865
Cdd:PRK12704 99 DR------KLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEE------QLQELERISG------- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1093953565 1866 kLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAE 1908
Cdd:PRK12704 150 -LTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
1265-1640 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1265 EEQIRNKDEEIQQLRSKLEKAEKERnelrlnSDRLESRISELTSELTDerntgesASQLLDAETAERLRAE-----KEMK 1339
Cdd:pfam14643 77 AQHSLLRKSWIKELDETLEKLEKER------ADKLKSVLKKYVEILED-------IAHLLPPDVYRLIDKEameinQALL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALKKQmevmemevmearlIRAAEINGEVDD----DDAGGEWR-LKYERAVRE--VDFTKKRLQQEFEDKLEVE 1412
Cdd:pfam14643 144 ENRRAYAKLFAN-------------LMEAELKQELSFrlrwQDRVDRWKaLKTEHLIQEfkEFIASEEIQNPPERKKELE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1413 QQNKRQ---LERRLGDLQADSEESQRALQqlKKKCQRLTAELQD-------------TKLHLEGQQVRNHELEKKQRRFD 1476
Cdd:pfam14643 211 EMLKEQkklQQKRLELLQKISDLLPPAYS--KSKVEEWWASLEAlneqldqyhdqcmTKLRAEYEEVWQECLARVQKLKQ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1477 S-ELSQAHEEAQREKLQRE-------KLQR--EKDMLLAEAF--SLKQQLEEKDMDIAGFTQKVVSLEAELQdissqesk 1544
Cdd:pfam14643 289 ElLDYKVCSEEEAEALVNEeflplvgKLQRdaEDELEKLDKFleELAKQTEAQSEDLFKFFREAAQLWDVHQ-------- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1545 deaslAKVKKQLRDLEAKVKDQEEELDEQagtIQMLEQAklrLEMEMERMRQthskemESRDEEVEEARQSCQKKLKQME 1624
Cdd:pfam14643 361 -----TELAKQELELEKKLEQCRQKHDQE---NQAKEAA---LDKKLDQLRQ------ASTEEKLKECLDKALKFLDDIE 423
|
410
....*....|....*.
gi 1093953565 1625 VQLEEEYEDKQKVLRE 1640
Cdd:pfam14643 424 KEYEDFHDKLTAIVKE 439
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1563-1900 |
1.08e-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: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1563 VKDQEEELDEQAGTIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1626
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1627 LEEEYED-KQKVlrekRELEGKLATLSDQVnrrdfESEKRLRKDLKRTKALLADAQLMldhlknsapskreIAQLKNQLE 1705
Cdd:pfam15742 81 LTAEWKHcQQKI----RELELEVLKQAQSI-----KSQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1706 ESEFTCAAAVKA--RKAMEVEIEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQ-----NRLEEDQEDMNELMKKHK 1775
Cdd:pfam15742 139 HAHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQqqvrsLQDKEAQLEMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1776 aaVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRL 1843
Cdd:pfam15742 216 --IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1844 EFERTQ----VKRLESLASRLKENMEKLTEERDQrIAAENREKEQNKR-LQRQLRDtKEEMG 1900
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 |
1.09e-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: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 220 ELELQRRPTGDFGFSLRRttmldrGPEGQACRrvVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSGIF--VKSISPG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKA 71
|
....*...
gi 1093953565 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 ... |
1711-1965 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1711 CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQIND 1790
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1791 LQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFER------------TQV-KRLESLA 1857
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaahikavTQIeQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1858 SRLKENMEKLTEERDQR--IAAENREKEQNKRLQRQLRDTKEEMGELARKEA---EASRKKHELEMDLESLEAANQSLQA 1932
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRaaHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsirEISCQQHTLTQHIHTLQQQKTTLTQ 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 1093953565 1933 DLKLAFKRIGDL-----QAAIEDEMESDENEDLINSEG 1965
Cdd:TIGR00618 394 KLQSLCKELDILqreqaTIDTRTSAFRDLQGQLAHAKK 431
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1551-1706 |
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 1093953565 1551 KVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1630
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1631 YEDKQKVLREKRELEGKLATLSDQVNRRDFESEK---RLRKDLKRTKALLAD--AQLMLDHLKNSApsKREIAQLKNQLE 1705
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 1093953565 1706 E 1706
Cdd:PRK12704 180 E 180
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1567-1937 |
1.45e-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: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1567 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEE--ARQSCQKKLKQMEVQLEEEYEDKQKVLREKREL 1644
Cdd:pfam07111 22 ERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAEliSRQLQELRRLEEEVRLLRETSLQQKMRLEAQAM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1645 EGKLATLSDQVNRRDFESekrlrkdlkrTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVE 1724
Cdd:pfam07111 102 ELDALAVAEKAGQAEAEG----------LRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDLAQINDLQAQLEEANKE 1801
Cdd:pfam07111 171 AEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1802 KQELQEKLQALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEerdQRIAAE 1878
Cdd:pfam07111 251 MQHLQEDRADLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQD 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1879 NREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1937
Cdd:pfam07111 327 LEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1717-1927 |
1.45e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 45.37 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEE-DQEDMNELMKKHKAAVAQASRDLAQIND---- 1790
Cdd:pfam12795 31 KIDASKQRAAAYQKALDDAPAELRELRQELAALQaKAEAAPKEILASlSLEELEQRLLQTSAQLQELQNQLAQLNSqlie 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1791 LQAQLEEANKEKQELQEKLQALQSQvefLEQSMVDKSLVSrqEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEE 1870
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNR---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKAR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1871 RDQRiaaenreKEQNKRLQRQLRDTKEEMGELARKEAEASRKkhELEMDLESLEAAN 1927
Cdd:pfam12795 186 RDLL-------TLRIQRLEQQLQALQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1796-1911 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1796 EEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLESLASRLKENMEKltEERDQRi 1875
Cdd:COG2433 402 EHEERELTEEEEEIRRLEEQVERLE-------------AEVEELEAELEEKDERIERLERELSEARSEERR--EIRKDR- 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 1093953565 1876 AAENREKEqNKRLQRQLRDTKEEMGELARKEAEASR 1911
Cdd:COG2433 466 EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1740-1898 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1740 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1815
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1816 VEFLEQSMVdKSLVSRQEaKIRELETRLEFERTQV--KRLES-----LASRLKENMEKLTEERDQrIAAENREKE----Q 1884
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLtsKSQSSssqseLENRLHQLTETLIQKQTM-LEALSTEKNslvlQ 199
|
170
....*....|....
gi 1093953565 1885 NKRLQRQLRDTKEE 1898
Cdd:pfam09787 200 LERMEQQIKELQGE 213
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1694-1912 |
1.95e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1773
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1774 HKA--------AVAQASRDLA-----------QINDLQAQLEEANKEKQELQEKlqalQSQvefleqsmvDKSLVSRQEA 1834
Cdd:PRK11637 139 HTGlqlilsgeESQRGERILAyfgylnqarqeTIAELKQTREELAAQKAELEEK----QSQ---------QKTLLYEQQA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1835 KIRELE-TRLEFERTqvkrLESLASRLKENMEKLTEERDQRIAAENR----EKEQNKRLQRQLRdtkeEMGELARKEAEA 1909
Cdd:PRK11637 206 QQQKLEqARNERKKT----LTGLESSLQKDQQQLSELRANESRLRDSiaraEREAKARAEREAR----EAARVRDKQKQA 277
|
...
gi 1093953565 1910 SRK 1912
Cdd:PRK11637 278 KRK 280
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
2.03e-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: 2.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 260 GAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1270-1595 |
2.05e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1270 NKDEEIQQLRSKLEK-AEKERnELRLNSDRLESRISELTSELTDERN--------TGESASQLLDAETAERLRAEKEMKE 1340
Cdd:pfam00038 1 NEKEQLQELNDRLASyIDKVR-FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1341 LQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQEfedkleveqqnk 1416
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEE------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 rqlerrLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQA----HEEAQREKL 1491
Cdd:pfam00038 144 ------VRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQAaarnGDALRSAKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1492 QREKLQREKDMLLAEAFSLKQQLEekdmdiagftqkvvSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELD 1571
Cdd:pfam00038 218 EITELRRTIQSLEIELQSLKKQKA--------------SLERQLAET---EERYELQLADYQELISELEAELQETRQEMA 280
|
330 340
....*....|....*....|....
gi 1093953565 1572 EQAGTIQMLEQAKLRLEMEMERMR 1595
Cdd:pfam00038 281 RQLREYQELLNVKLALDIEIATYR 304
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1259-1578 |
2.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEM 1338
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1339 KELQTQYDALKKQMevmemevmearliraaeingevddddaggewrlkyeravrevdftkKRLQQEFEDKleveQQNKRQ 1418
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1419 LERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQR 1498
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1499 EKDMLLAEAfslKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ 1578
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1661-1960 |
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 1093953565 1661 ESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMeveiedlhlqiddiAKAKT 1740
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1741 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQS 1814
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1815 QVEFLEQSMVD-KSLVSRQEAKIRELetrlefertqvkrleslaSRLKENMEKLTEERDQriaAENREKEQNKRLQRQLR 1893
Cdd:pfam15905 206 KLVSTEKEKIEeKSETEKLLEYITEL------------------SCVSEQVEKYKLDIAQ---LEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1894 DTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1960
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
2.20e-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: 2.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1721-1959 |
2.26e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1721 MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKkhkaaVAQASRDLAQIND---LQAQLEE 1797
Cdd:PRK05771 77 KKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEP-----WGNFDLDLSLLLGfkyVSVFVGT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1798 ANKEKQElQEKLQALQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEerdq 1873
Cdd:PRK05771 152 VPEDKLE-ELKLESDVENVEYISTDKGYVYVVvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEE---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1874 riaaenrekeqnkrLQRQLRDTKEEMGELARKEAEASRKKHE-LEMDLESLEAANQSLQADLKLAF------KRIGDLQA 1946
Cdd:PRK05771 227 --------------IEKERESLLEELKELAKKYLEELLALYEyLEIELERAEALSKFLKTDKTFAIegwvpeDRVKKLKE 292
|
250 260
....*....|....*....|..
gi 1093953565 1947 AIED---------EMESDENED 1959
Cdd:PRK05771 293 LIDKatggsayveFVEPDEEEE 314
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1256-1350 |
2.69e-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: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1256 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgesasqlldAETAERLRAE 1335
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKD 464
|
90
....*....|....*
gi 1093953565 1336 KEMKELQTQYDALKK 1350
Cdd:COG2433 465 REISRLDREIERLER 479
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1832-1940 |
2.73e-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: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1832 QEAKIRELETRLEFERTQVKRLESLASRLKENMEklteERDQRIAaenREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1911
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1093953565 1912 KKHELE---MDLESLEAANQSLQADLKLAFKR 1940
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1777-1910 |
2.87e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1777 AVAQASRDLAQINDLQAQLEEANKEKQ-ELQEKL--QALQSQVEFLEQsmvdkslVSRQEAKIRELEtrlefertqvKRL 1853
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLlEAEDKLvqQDLEQTLALLDK-------IDRQKEETEQLK----------QQL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1854 ESLASRLKENMEKLT--EERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1910
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 |
3.02e-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: 3.02e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1093953565 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1266-1629 |
3.04e-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: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTG-----ESASQLLDAETAERLRAEKEMKE 1340
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAakaqlEVAKARHAAAVAELKSVKEELES 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1341 LQTQYDALKKQMEVMEMEVMEArLIRAAEINGEVDDddaggewrlkyerAVREVDFTKKRLQQEFEDKLEVE-------- 1412
Cdd:pfam05701 150 LRKEYASLVSERDIAIKRAEEA-VSASKEIEKTVEE-------------LTIELIATKESLESAHAAHLEAEehrigaal 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1413 --QQNKRQLERRLGDLQadsEESQRALQQ------LKKKCQRLTAELQDTKLHL----EGQQVRNHELEKKQRRFDSELS 1480
Cdd:pfam05701 216 arEQDKLNWEKELKQAE---EELQRLNQQllsakdLKSKLETASALLLDLKAELaaymESKLKEEADGEGNEKKTSTSIQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1481 QAHEEAQRE----KLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQK-------VVSLEAELQDISSQeskdeasL 1549
Cdd:pfam05701 293 AALASAKKEleevKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQRegmasiaVSSLEAELNRTKSE-------I 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1550 AKVKKQLRDLEAKVKDQEEELDEQAgtiQMLEQAKLRLEMEMERMRQTHskemesrdEEVEEARQSCQkklkQMEVQLEE 1629
Cdd:pfam05701 366 ALVQAKEKEAREKMVELPKQLQQAA---QEAEEAKSLAQAAREELRKAK--------EEAEQAKAAAS----TVESRLEA 430
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1437-1665 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1437 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEeaqreklqrEKLQREKDMLLaeafSLKQQLE 1515
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1516 EKDMDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGTIQMLEQAKLRLEMEM 1591
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1592 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEyedKQKVLREKRELEGKLATLSDQVNRRDFESEKR 1665
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATL---QQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPR 697
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
219-307 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRpTGDFGFSLRrttmldrgpeGQACRRVvHFAEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06712 2 RTVHLTKE-EGGFGFTLR----------GDSPVQV-ASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKS 67
|
90
....*....|
gi 1093953565 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 |
3.41e-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: 3.41e-04
10 20 30
....*....|....*....|....*....|.
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
3.56e-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: 3.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1093953565 269 GLV-PGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1742-1989 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1742 LEEQLSRLQREKNeiQNRLEEDQEdMNELMKKHKAAVAQASRDLAQINDLQAQLEeaNKEKQElQEKLQALQSQVEFLEQ 1821
Cdd:pfam05557 7 SKARLSQLQNEKK--QMELEHKRA-RIELEKKASALKRQLDRESDRNQELQKRIR--LLEKRE-AEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1822 SMVDKSLVSRqeaKIRELETRLEFERTQVKRLESLASRLKENMEKlteeRDQRIAAENREKEqnkRLQRQLRdtkeemgE 1901
Cdd:pfam05557 81 KKKYLEALNK---KLNEKESQLADAREVISCLKNELSELRRQIQR----AELELQSTNSELE---ELQERLD-------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1902 LARKEAEASRKKHELEMDLESLEAANQ---------SLQADLKLAFKRIGDLQAAIEdEMES------DENEDLINSEGD 1966
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiQSQEQDSEIVKNSKSELARIP-ELEKelerlrEHNKHLNENIEN 222
|
250 260
....*....|....*....|...
gi 1093953565 1967 SDVdseLEDRVDGVKSWLSKNKG 1989
Cdd:pfam05557 223 KLL---LKEEVEDLKRKLEREEK 242
|
|
| Phage_HK97_TLTM |
pfam06120 |
Tail length tape measure protein; This family consists of the tail length tape measure protein ... |
1699-1914 |
3.99e-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: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1699 QLKNQLEESEFTCAAAVKARKAmEVEIEDLHLQIDDIAKAKTALEEQ--LSRLQREKNE--------IQNRLEEDQEDMN 1768
Cdd:pfam06120 41 QKQEQARQSALEYAATIDQVRA-NLNKMTLPETADNSGKTKESLAAQnkLVDEQRQKVEglksaiagYQQMLASPGPSIN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1769 ELMKKHKAAVAQASRDLAQINDL----QAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLvsRQEAKIRELETR 1842
Cdd:pfam06120 120 GYLINHLISQEDAVKSLAAAQDElsveQSRLNELSKKSEEIQSALKAVESQRDFLirQQSAAQNNM--RHSLLMVNAEHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1843 lEFERTQ-------VKRLESLASRLKENMEKLTEERDQRIAAENREKEQN-----KRLQRQLRDTKEEMGELARKEAEAS 1910
Cdd:pfam06120 198 -EFNRIMsagnqilTNRLALVNSPMRIPAAPLSEKQQDFIQKSERDKELSaltgeARVIRQAEFAADDIGLLNKPEFADN 276
|
....
gi 1093953565 1911 RKKH 1914
Cdd:pfam06120 277 RQKY 280
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
4.06e-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: 4.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 259 PGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1398-1645 |
4.08e-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: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1398 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEES--QRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHELEKKQRRF 1475
Cdd:pfam13868 50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEReqKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EEKLEKQRQL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1476 DSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMdiagftqkvvsleaelqdisSQESKDEASLAKVKKQ 1555
Cdd:pfam13868 129 REEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE--------------------AEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELDEQagtiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQMEVQLEEEY 1631
Cdd:pfam13868 189 LRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRLAEEAEREE 260
|
250
....*....|....
gi 1093953565 1632 EDKQKVLREKRELE 1645
Cdd:pfam13868 261 EEFERMLRKQAEDE 274
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1796-1918 |
4.08e-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: 42.21 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1796 EEANKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKL------TE 1869
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1093953565 1870 ERDQRIAAENREKEQNKRLQRQlrdtkeemgELARKEAEASRKKHELEM 1918
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEE---------EVERKEEEARRLQEELEE 115
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1742-1922 |
4.10e-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: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1742 LEEQLSRLQREKNEIQNRLEEDQE-DMNELMKKHKaavaqasRDLAQINDLQAQLEEANKEKQELQEKL-QALQSQVEFL 1819
Cdd:pfam09755 112 LSRKLTQLRQEKVELEQTLEQEQEyQVNKLMRKIE-------KLEAETLNKQTNLEQLRREKVELENTLeQEQEALVNRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1820 EQSMvdkslvSRQEAKIRELETRLEFERT--------------------QVKRLESLASRLKENMEKLTEERDQRIAA-- 1877
Cdd:pfam09755 185 WKRM------DKLEAEKRLLQEKLDQPVSappsprdstsegdtaqnltaHIQYLRKEVERLRRQLATAQQEHTEKMAQya 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1093953565 1878 --ENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrkKHELEMDLES 1922
Cdd:pfam09755 259 qeERHIREENLRLQRKLQLEMERREALCRHLSES---ESSLEMDEER 302
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1745-1934 |
4.46e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1745 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQALQSQvefleQ 1821
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1822 SMVDKSLVSRQEAKIRE-----LETRLEFERTQVK-RLESLASRL----KENMEKLTEERDQrIAAENREKEQNKRLQRQ 1891
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1093953565 1892 LRDTKEEMgELARKEAEASRKKhelemDLESLEAANQSLQADL 1934
Cdd:PRK11637 199 LLYEQQAQ-QQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1260-1576 |
4.58e-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: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRL----NSDRLESRISELTSELTDE-RNTGEsasQLLDAETAERLRA 1334
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNENANNLIKQfENTKE---KIAEYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1335 EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGE-WRLKYERAVREVDF----------------T 1397
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaIKEEIENIVGEVELsksseeldsfkdtiesT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1398 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDS 1477
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEAQREKLQR-----EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE---AELQDISSQESKDEASL 1549
Cdd:COG5185 460 ESQSRLEEAYDEINRSvrskkEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHIL 539
|
330 340
....*....|....*....|....*..
gi 1093953565 1550 AKVKKQlRDLEAKvKDQEEELDEQAGT 1576
Cdd:COG5185 540 ALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1657-1953 |
4.77e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1657 RRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----IEDLHLQ 1731
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1732 IDDIAKAKtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQE-KLQ 1810
Cdd:pfam13868 82 IEEREQKR---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1811 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQR 1890
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1891 QLRDtKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1953
Cdd:pfam13868 239 QARE-EQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1750-1929 |
4.85e-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: 44.94 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1750 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslv 1829
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA------------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1830 sRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENR--EKEQNKRLQRQLRdtKEEMGELARKEA 1907
Cdd:pfam15709 418 -QERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQ--KQEAEEKARLEA 494
|
170 180
....*....|....*....|..
gi 1093953565 1908 EASRKKHELEMDLESLEAANQS 1929
Cdd:pfam15709 495 EERRQKEEEAARLALEEAMKQA 516
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1521-1765 |
4.93e-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: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1521 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQaklrlememermrqthsk 1600
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1601 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKlaTLSDQVNRRDF-----ESEKRLRKDLKRTKA 1675
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSE--SFSDFLDRLSAlskiaDADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1676 LLADAQLMLDHLKNsapskrEIAQLKNQLEEseftcaaavkARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNE 1755
Cdd:COG3883 144 ELEAKKAELEAKLA------ELEALKAELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250
....*....|
gi 1093953565 1756 IQNRLEEDQE 1765
Cdd:COG3883 208 AEAAAAAAAA 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1272-1451 |
5.05e-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: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1272 DEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQT--QYDALK 1349
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1350 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQAD 1429
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1093953565 1430 SEESQRALQQLKKKCQRLTAEL 1451
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1588-1914 |
5.17e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1588 EMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEyeDKQKVLREKRELEGKLAtLSDQVNRRDFESEKRLR 1667
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEE--DSELKPSGQGGLDEEEA-FLDRTAKREERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1668 KDLKRTKALLADAqlmldhlknsAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLS 1747
Cdd:pfam02029 81 EALERQKEFDPTI----------ADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1748 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEA---NKEKQELQEKLQALQSQVEFLEQSMV 1824
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1825 DKSLVSRQEAKIR-ELETRLE-------------FERTQVKR------LESLASRLKENMEKLTEERDQRiaaENREKEQ 1884
Cdd:pfam02029 231 SQSQEREEEAEVFlEAEQKLEelrrrrqekeseeFEKLRQKQqeaeleLEELKKKREERRKLLEEEEQRR---KQEEAER 307
|
330 340 350
....*....|....*....|....*....|
gi 1093953565 1885 NKRLQRQLRDTKEEMgELARKEAEASRKKH 1914
Cdd:pfam02029 308 KLREEEEKRRMKEEI-ERRRAEAAEKRQKL 336
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1532-1936 |
5.24e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1532 EAELQDISSQESKDEASLAKVKKQLR----DLEAKVKD----QEEELDEQAGTIQMLEQAKLRLEMEMERMRQthskEME 1603
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEaefnQKRAKFKElylaKEEDLKRQNAVLQEAQVELDALQNQLALARA----EME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1604 SRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREkrelegklatlsdqvNRRDFESEKRLRKDLKRTKalladaqlm 1683
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKE---------------TVREYEVQFHRRLEQERAQ--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1684 LDHLKNSApsKREIAQLKNQLEESEFTCAAAVKARKAMEvEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQnrlEED 1763
Cdd:pfam03528 135 WNQYRESA--EREIADLRRRLSEGQEEENLEDEMKKAQE-DAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELE---ASK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1764 QEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE-ANKEKQELQEKLQALQsqvefLEQSMVDKSLVSRQEAKIRELETR 1842
Cdd:pfam03528 209 MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEdAEKLRKELHEVCHLLE-----QERQQHNQLKHTWQKANDQFLESQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1843 LEFERtQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLES 1922
Cdd:pfam03528 284 RLLMR-DMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINS 362
|
410
....*....|....
gi 1093953565 1923 LEAANQSLQADLKL 1936
Cdd:pfam03528 363 AHGSVHSLDTDVVL 376
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1772-1915 |
5.61e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1772 KKHKAAVAQASRDLAQIndlqaqLEEANKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFERTQV 1850
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1851 -KRLESLASR------LKENMEKLTEERDQRIA-AENREKEQNKRLQRQLRDTKEEMGELARKEAEaSRKKHE 1915
Cdd:PRK12704 99 dRKLELLEKReeelekKEKELEQKQQELEKKEEeLEELIEEQLQELERISGLTAEEAKEILLEKVE-EEARHE 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1416-1633 |
5.79e-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: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1416 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEEAQREK 1490
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1491 LQREKLQREKDMLLAEAFSLKQqleekDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1566
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1567 ----EEELDEQAGTIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1633
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1468-1680 |
6.04e-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: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1468 LEKKQRRFDSELSQAheEAQREKLQREK----LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQ--DISSQ 1541
Cdd:COG3206 180 LEEQLPELRKELEEA--EAALEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1542 ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLK 1621
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093953565 1622 QMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfesEKRLRKDLKRTKALLADA 1680
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLE---EARLAEALTVGNVRVIDP 393
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1787-1961 |
6.12e-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: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1787 QINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslvsrqeakIRELETrlEFERTQvKRLESLASRLKEnMEK 1866
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRR-------------IQLLEE--ELERTE-ERLAEALEKLEE-AEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1867 LTEERDQ-RIAAENREKEQNKR---LQRQLRDTKEEMGELARKEAEASRKKHELEMDLE-------SLEAANQSLQADLK 1935
Cdd:pfam00261 72 AADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEELK 151
|
170 180
....*....|....*....|....*..
gi 1093953565 1936 LAFKRIGDLQAAIEDEMES-DENEDLI 1961
Cdd:pfam00261 152 VVGNNLKSLEASEEKASEReDKYEEQI 178
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1753-1935 |
6.33e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1753 KNEIQNRLEE--DQEDMNELMKKHKAAVAQASRDLAQI-------NDLQAQLEEANKEKQELQEKLQALQSQveflEQSM 1823
Cdd:PRK11281 38 EADVQAQLDAlnKQKLLEAEDKLVQQDLEQTLALLDKIdrqkeetEQLKQQLAQAPAKLRQAQAELEALKDD----NDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1824 VDKSLVSRQeakIRELETRLEfertqvKRLESLASRLKEnmekLTEERDQRIAAENR-EKEQN------KRLQ---RQLR 1893
Cdd:PRK11281 114 TRETLSTLS---LRQLESRLA------QTLDQLQNAQND----LAEYNSQLVSLQTQpERAQAalyansQRLQqirNLLK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1093953565 1894 DTKEEmgelaRKEAEASRKKhELEMDLESLEAANQSLQADLK 1935
Cdd:PRK11281 181 GGKVG-----GKALRPSQRV-LLQAEQALLNAQNDLQRKSLE 216
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1547-1874 |
6.64e-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: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1547 ASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAklrLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQ 1626
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRG---LSVQLANLEK-VREGLEKVLNELKKDFKQLLKDLDAALER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1627 LEEEYE--DKQKVLREKRELEGKLATLSDQVNRRDFES---------------EKRLRKDLKRTKALLADAQLMLDHLKN 1689
Cdd:pfam04108 79 LEETLDklRNTPVEPALPPGEEKQKTLLDFIDEDSVEIlrdalkelidelqaaQESLDSDLKRFDDDLRDLQKELESLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1690 SAPSKREIAQLKNQLEESEftcaaavkarKAMEVEIEDLHLQIDDIAKAKTALE--------------EQLSRLQREKNE 1755
Cdd:pfam04108 159 PSESISLIPTLLKELESLE----------EEMASLLESLTNHYDQCVTAVKLTEggraemlevlendaRELDDVVPELQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1756 IQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQL-----------EEANKEKQELQEKLQALQSQVEFLEQ--S 1822
Cdd:pfam04108 229 RLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLpeylaalkefeERWEEEKETIEDYLSELEDLREFYEGfpS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1093953565 1823 MVDKSLVsrqeakirELETRLEFErtqvKRLESLASRLKENMEKLTEERDQR 1874
Cdd:pfam04108 309 AYGSLLL--------EVERRREWA----EKMKKILRKLAEELDRLQEEERKR 348
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
6.77e-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: 6.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1626-1932 |
6.96e-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: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLE 1705
Cdd:TIGR00618 180 QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1706 ESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKnEIQNRLEEDQEDMNELMKKhkaavaqasrdL 1785
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQSKMRSRAKL-----------L 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1786 AQINDLQAQleeaNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1865
Cdd:TIGR00618 328 MKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1866 KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1932
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
7.33e-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: 7.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1324-1590 |
7.82e-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: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1324 LDAETAERLRAEKEMKELQTQYDALKK----------------------QMEVMEMEVMEARLIRAAEINGEVDDDDAGG 1381
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKekerliierdtlretneelrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1382 EWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQ 1461
Cdd:pfam05622 279 EIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDS 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1462 QVRNHELEKKQRrfdsELSQAHEEAQREKLQREKLQREKDMLLAE-AFSLKQQLEEKDMDIAGFTQK-----------VV 1529
Cdd:pfam05622 359 SLLKQKLEEHLE----KLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksvIK 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1530 SLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagtiqmLEQAKLRLEME 1590
Cdd:pfam05622 435 TLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1264-1482 |
8.28e-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: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1264 SEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDerntgesasqlldaetaerlrAEKEMKELQT 1343
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1344 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQEFEDKLEVEQQ 1414
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 1415 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1482
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1695-1924 |
8.72e-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: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1695 REIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1774
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1775 KAAVAQASRDLAQINDLQAQL-------EEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFER 1847
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953565 1848 TQVKRLESLAsrlkenmekltEERDQRiaaENREKEQNKRLQRQLRDTKeemgelARKEaEASRKKHELEMDLESLE 1924
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAE------TRAE-FAERSVQKLEKEVDRLE 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1272-1506 |
9.92e-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: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1272 DEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERL----------RAEKEMKE- 1340
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfaaalgdAVERELREn 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1341 LQTQYDALKKQMEVMEMevmeaRLIRA---------AEINGEVDDDDAGGEWRLKYERaVREVDFtkKRLQQEFEDKLev 1411
Cdd:COG4913 771 LEERIDALRARLNRAEE-----ELERAmrafnrewpAETADLDADLESLPEYLALLDR-LEEDGL--PEYEERFKELL-- 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1412 eqqnKRQLERRLGDLQAD-SEESQRALQQLKkkcqRLTAELQ------DTKLHLEGQQVRNHELEKKQRRFD--SELSQA 1482
Cdd:COG4913 841 ----NENSIEFVADLLSKlRRAIREIKERID----PLNDSLKripfgpGRYLRLEARPRPDPEVREFRQELRavTSGASL 912
|
250 260
....*....|....*....|....
gi 1093953565 1483 HEEAQREKlQREKLQREKDMLLAE 1506
Cdd:COG4913 913 FDEELSEA-RFAALKRLIERLRSE 935
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1701-1878 |
1.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1701 KNQLEESEFTCAAAVK-ARKAMEVEIEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1778
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1779 AQASRDLAQINDLQAQLEEANKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFERtqvkrles 1855
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180 190
....*....|....*....|....*....|....
gi 1093953565 1856 lASRLKENMEKLTEERD-----------QRIAAE 1878
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADkkakeilaqaiQRCAAD 204
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1417-1596 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfdSELSQAHEEAQREKLQREKL 1496
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR--EQLQELEEQLATERSARREA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1497 QREKDMLLAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQ-ESKDEASLAKvkkqlRDLEAKVKDQEEELDEQAG 1575
Cdd:pfam09787 113 EAELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRNQlTSKSQSSSSQ-----SELENRLHQLTETLIQKQT 184
|
170 180
....*....|....*....|.
gi 1093953565 1576 TIQMLEQAKLRLEMEMERMRQ 1596
Cdd:pfam09787 185 MLEALSTEKNSLVLQLERMEQ 205
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1737-1862 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1737 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQV 1816
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1817 EFLEQSMVDKslvsrqEAKIRELETRLEFERTQVKRLESLASRLKE 1862
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 |
1.35e-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: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1093953565 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 ... |
1694-1815 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAK----TALEEQLSRLQREKNEIQNRLEEDQEDMNE 1769
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDptelDRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1770 LMKKHKAAVAQASRDLAQINDLQAQLEEAN----KEKQELQEKLQALQSQ 1815
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 |
1.51e-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: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 258 EPGAGTKDLALGLvpGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1403-1538 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1403 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQdtklhlEGQQVrnheLEKKQRRFDSELSQA 1482
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQK------EEEQM----MEAQERSYQEHVKQL 248
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1483 HEEAQREklqREKLQREKDMLLAeafslKQQLEEKDMDIAGFTQKVVSLEAELQDI 1538
Cdd:pfam02841 249 IEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1266-1883 |
1.75e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1266 EQIRNKDEEIQQLRSKLEKAEKER------NELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAeRLRAEKEMK 1339
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQEFEDKLEVEQQNKRQ 1418
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1419 LERRLGDLQADSEesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EEA 1486
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1487 QREKLQREKLQREKDML------LAEAFSLKQQLEEKDMDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1558
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1559 LEAKVKDQEEELDEQAGTIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1632
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1633 DKQK---VLREKRELEGKLATLSDQVNRRDFES-EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEES- 1707
Cdd:PTZ00440 1553 IKDEietILNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1708 --------EFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1772
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1773 KhkaavaqASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFERTQVKR 1852
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670
....*....|....*....|....*....|....
gi 1093953565 1853 LESLASRLKENMEKLTEER---DQRIAAENREKE 1883
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 |
1.97e-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: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 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 ... |
1489-1640 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1489 EKLQREKLQREKDMLLAEAFSLKQQLEEKdmdIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1568
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1569 ELDeqagtiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKVLRE 1640
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
2.34e-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: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1093953565 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 ... |
1726-1819 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1726 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKekqEL 1805
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 1093953565 1806 QEKLQALQSQVEFL 1819
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1610-1775 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1610 EEARQSCQKKLKQMEVQLEEEYEDKQKvLREKRELegklatLSDQVNR--RDFESEKRLRKDL-KRTKALLADAQlmlDH 1686
Cdd:pfam10168 553 DLAREEIQKRVKLLKLQKEQQLQELQS-LEEERKS------LSERAEKlaEKYEEIKDKQEKLmRRCKKVLQRLN---SQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1687 LKNSAPSKREIAQLKNQLEESEFTCAAAVK-ARKAMEVeiedlhlQIDDIAKAKTALEE---QLSRLQREKneIQNRLEE 1762
Cdd:pfam10168 623 LPVLSDAEREMKKELETINEQLKHLANAIKqAKKKMNY-------QRYQIAKSQSIRKKsslSLSEKQRKT--IKEILKQ 693
|
170
....*....|...
gi 1093953565 1763 DQEDMNELMKKHK 1775
Cdd:pfam10168 694 LGSEIDELIKQVK 706
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1424-1568 |
2.58e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1424 GDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDML 1503
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953565 1504 LAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1568
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| 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 |
2.76e-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: 2.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQS--GDSVRLKVQ 308
Cdd:cd06732 39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKECpkGSEVTLLVQ 80
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1694-1839 |
2.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1694 KREIAQLKNQLEEsefTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqEDMNELMKK 1773
Cdd:PRK00409 508 KKLIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE---KEAQQAIKE 581
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1774 HKAAVAQASRDLAQindLQAQLEEANKEkQELQEKLQALQSQVEFLE-----QSMVDKSLVSRQEAKIREL 1839
Cdd:PRK00409 582 AKKEADEIIKELRQ---LQKGGYASVKA-HELIEARKRLNKANEKKEkkkkkQKEKQEELKVGDEVKYLSL 648
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1468-1630 |
3.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1468 LEKKQRRFDSELSQAHEEAQREKlqREKLQREKDmllaEAFSLKQQLEekdmdiagftQKVVSLEAELQDISSQESKDEA 1547
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIK--KEALLEAKE----EIHKLRNEFE----------KELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 SLakvKKQLRDLEAKvkdqEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEME-----SRDE-------EVE-EARQ 1614
Cdd:PRK12704 97 NL---DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEakeilleKVEeEARH 169
|
170
....*....|....*.
gi 1093953565 1615 SCQKKLKQMEVQLEEE 1630
Cdd:PRK12704 170 EAAVLIKEIEEEAKEE 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1713-1917 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1713 AAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQLSRlqreKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLA-----Q 1787
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQ---SELVKARQALAQTIAR----QKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArealaE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1788 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQVKRLESLAS-RLKENMEK 1866
Cdd:pfam04012 92 KKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL------KAKKNLLKARLKAAKAQEAVQTSLGSlSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093953565 1867 LtEERDQRIAaenrEKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE 1917
Cdd:pfam04012 166 F-ERIEEKIE----EREARADAAAELASAVDLDAKLEQAGIQMEVSEDVLA 211
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1834-1959 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1834 AKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAEnrekEQNKRLQRQLRDTKEEMGELARKEAEASRKK 1913
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1093953565 1914 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1959
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| PDZ_RGS12-like |
cd06710 |
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ... |
219-308 |
3.67e-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: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 219 RELELQRRPTGdFGFSLRrttmldrgpeGQA-CrrVVHFAEPGAGTKDLalGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06710 1 RTVEIARGRAG-YGFTIS----------GQApC--VLSCVVRGSPADVA--GLKAGDQILAVNGINVSKASHEDVVKLIG 65
|
90
....*....|.
gi 1093953565 298 QSGDSVRLKVQ 308
Cdd:cd06710 66 KCTGVLRLVIA 76
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1259-1498 |
3.70e-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: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1259 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSD-------RLESRISELTSELTDERNTGESASQLLDAETAER 1331
Cdd:pfam19220 146 EEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEeqaaelaELTRRLAELETQLDATRARLRALEGQLAAEQAER 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1332 LRAEKEMKELQTQYdALKKQMEVMEMEVMEARLIRAAEINGEVDDddaggewrlkyerAVREvdftKKRLQQEFEDKLEV 1411
Cdd:pfam19220 226 ERAEAQLEEAVEAH-RAERASLRMKLEALTARAAATEQLLAEARN-------------QLRD----RDEAIRAAERRLKE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1412 EQQNKRQLERRLGDLQADSE-------ESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK----QRRFDSELS 1480
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLErrtqqfqEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRiaelTKRFEVERA 367
|
250 260
....*....|....*....|
gi 1093953565 1481 QAHEEAQR--EKLQREKLQR 1498
Cdd:pfam19220 368 ALEQANRRlkEELQRERAER 387
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
3.74e-03 |
|
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467170 [Multi-domain] Cd Length: 85 Bit Score: 38.48 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1093953565 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1260-1489 |
3.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1260 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgesasqlldAETAERLRAEKEMK 1339
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-----------EELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1340 ELQTQYDALkkqmevmEMEVMEARLIRAAEINGEVDDDDAggewrlkyeRAVREVDFTKKRL---QQEFEDKLEVEQQNK 1416
Cdd:COG3883 100 GSVSYLDVL-------LGSESFSDFLDRLSALSKIADADA---------DLLEELKADKAELeakKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQRE 1489
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
4.05e-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: 4.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093953565 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1717-1821 |
4.25e-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: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1796
Cdd:pfam13863 11 VQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|....*
gi 1093953565 1797 EANKEKQELQEKLQALQSQVEFLEQ 1821
Cdd:pfam13863 91 ELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1561-1811 |
4.35e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1561 AKVKDQEEElDEQAgtiqmlEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKvlRE 1640
Cdd:PRK05035 436 AEIRAIEQE-KKKA------EEAKARFEARQARLE----REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKA--AA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1641 KRELEGKLATLSDQvnrRDFESEKRLRKDLKRTKALLADAQlmldhlKNSAPSKREIAqlknqleeseftcaAAV---KA 1717
Cdd:PRK05035 503 TQPIVIKAGARPDN---SAVIAAREARKAQARARQAEKQAA------AAADPKKAAVA--------------AAIaraKA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1718 RKAMEVEIEDLHLQIDDIAKAKTALEeqLSRLQREKNEiQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1797
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVAAA--IARAKAKKAA-QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE 636
|
250
....*....|....
gi 1093953565 1798 ANKEKQELQEKLQA 1811
Cdd:PRK05035 637 PEEPVDPRKAAVAA 650
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1796-1935 |
4.49e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1796 EEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLefertqvKRLESLASRLKENMEKLTEERDQRI 1875
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELER---------ELEQKAEEAEALL-------KEAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1876 AaenrekEQNKRLQRQLRDTKEEMGELAR------KEAEASRKKHELEMDLESLEAANQSLQADLK 1935
Cdd:PRK00409 569 E------EAEKEAQQAIKEAKKEADEIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
4.52e-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: 4.52e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1093953565 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1273-1884 |
4.69e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1273 EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQ-TQYDALKKQ 1351
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASrRQQALQQAL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1352 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQ---- 1427
Cdd:PRK10246 271 AAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslnt 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1428 -------------------ADSEESQRALQQLKKKCQRLTAELQ------DTKLHLEGQQVRNH-ELEKKQRRFDSELSQ 1481
Cdd:PRK10246 351 wlaehdrfrqwnnelagwrAQFSQQTSDREQLRQWQQQLTHAEQklnalpAITLTLTADEVAAAlAQHAEQRPLRQRLVA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1482 AHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSL------EAELQDISSQESKDEA-------- 1547
Cdd:PRK10246 431 LHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVkticeqEARIKDLEAQRAQLQAgqpcplcg 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1548 -----------SLAKVKKQLR--DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMR---QTHSKEMESRDEEVEE 1611
Cdd:PRK10246 511 stshpaveayqALEPGVNQSRldALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRqeeQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1612 ARQSCQKKLKQMEVQleEEYEDKQKVLREKRELEGKLATLSDQVnrrdfeseKRLRKDLKRTKALLADAqlmLDHLKNSA 1691
Cdd:PRK10246 591 TLQPQDDIQPWLDAQ--EEHERQLRLLSQRHELQGQIAAHNQQI--------IQYQQQIEQRQQQLLTA---LAGYALTL 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1692 P---------SKREIAQLKNQLEESEFT--------CAAAVKARKAM-EVEIEDLHLQIDDIAKAKT---ALEEQLSRLQ 1750
Cdd:PRK10246 658 PqedeeaswlATRQQEAQSWQQRQNELTalqnriqqLTPLLETLPQSdDLPHSEETVALDNWRQVHEqclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1751 REKNEIQNRLEEDQEdmnelmkkHKAAVAQASRDLAQINDLQAQLEEAN-----KEKQELQEKLQALQSQVEFLEQsmvd 1825
Cdd:PRK10246 738 QQDVLEAQRLQKAQA--------QFDTALQASVFDDQQAFLAALLDEETltqleQLKQNLENQRQQAQTLVTQTAQ---- 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1826 kSLVSRQEAKIRELETRLEFERTQVkRLESLASRLKENMEKLTEERDQ-RIAAENREKEQ 1884
Cdd:PRK10246 806 -ALAQHQQHRPDGLDLTVTVEQIQQ-ELAQLAQQLRENTTRQGEIRQQlKQDADNRQQQQ 863
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1700-1845 |
4.78e-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: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1700 LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIakaKTALEEQLSRLQREKNEIQNRleeDQEDMNELMKKHKAAVA 1779
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDC---DPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1780 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEakIRELETRLEF 1845
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKE--IEKLKEQLKL 282
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1401-1562 |
4.99e-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: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1401 LQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1477
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1478 ELSQAHEEaqreKLQR-EKLQREKDmllaeafSLKQQLEEKDMDI---AGF-----TQKVVSL-------EAELQDISSQ 1541
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERD-------ELYDKFEAAIQDVqqkTGLknlllEKKLQALgetlekkEAQLNEVLAA 171
|
170 180
....*....|....*....|..
gi 1093953565 1542 ESKDEASLAKVKKQLRD-LEAK 1562
Cdd:pfam13851 172 ANLDPDALQAVTEKLEDvLESK 193
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1725-1963 |
4.99e-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: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQA-SRDLAQ-----INDLQAQLEEA 1798
Cdd:pfam13949 19 IERLEKSLDDLPKLKQRNREIL-------DEAEKLLDEEESEDEQLRAKYGTRWTRPpSSELTAtlraeIRKYREILEQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1799 NKEKQELQEKLQALQSQVEFLEQSMVD--KSLVSRQEAKIRELETRlefertQVKRLESLASRLkenmEKLTEERDQRIa 1876
Cdd:pfam13949 92 SESDSQVRSKFREHEEDLELLSGPDEDleAFLPSSRRAKNSPSVEE------QVAKLRELLNKL----NELKREREQLL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1877 AENREKEQNKRLQRQLRDTKEEMGELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIgdLQAAIEDEME 1953
Cdd:pfam13949 161 KDLKEKARNDDISPKLLLEKARLIAPNQEEQlfeEELEKYDPLQNRLEQNLHKQEELLKEITEANNEF--LQDKRVDSEK 238
|
250
....*....|
gi 1093953565 1954 SDENEDLINS 1963
Cdd:pfam13949 239 QRQREEALQK 248
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1417-1657 |
5.10e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1417 RQLERRLGDLQADSEESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheeaqrEKLqREK 1495
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL-REA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1496 LQREKDML----------LAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK---Q 1555
Cdd:COG0497 228 LQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEErlaL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1556 LRDLEAKVKDQEEELdeqagtIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDKQ 1635
Cdd:COG0497 308 LRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELLEAA 361
|
250 260
....*....|....*....|...
gi 1093953565 1636 KVLREKRElegKLA-TLSDQVNR 1657
Cdd:COG0497 362 EKLSAARK---KAAkKLEKAVTA 381
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1555-1809 |
5.15e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1555 QLRDLeaKVKDQEEELDEQAGTIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1632
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1633 DKQKVLR----EKRELEGKLATLSdqvNRRDFESEKRLRKDLKRTKALLADAQlmldhlKNSAPSKREIAQLKNQLEESE 1708
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1709 F----TCAAAVKARKAMEV--EIEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1782
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260
....*....|....*....|....*....
gi 1093953565 1783 rdlaqiNDLQAQLE--EANKEKQELQEKL 1809
Cdd:PRK05771 247 ------EELLALYEylEIELERAEALSKF 269
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1717-1816 |
5.21e-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: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEV-----EIEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEiqnrLEEDQEDMNELMKKHKAAVAQASR 1783
Cdd:COG0542 400 ARVRMEIdskpeELDELERRLEQLEIEKEALKkeqdeasfERLAELRDELAE----LEEELEALKARWEAEKELIEEIQE 475
|
90 100 110
....*....|....*....|....*....|...
gi 1093953565 1784 DLAQINDLQAQLEEANKEKQELQEKLQALQSQV 1816
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1695-1885 |
5.30e-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: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1695 REIAQLKNQLEESEFTCAAAVKARKAMEVEI-----EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1769
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTDYGDDLESVEAllkkhEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1770 LMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQvefleQSMVDKSLVSRQEAKIRELETRLEFERTQ 1849
Cdd:cd00176 87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE-----DLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1093953565 1850 VKRLESLASRLKENMEKLTEERDQRIAAENREKEQN 1885
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1766-1870 |
5.55e-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: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1766 DMNELMKKHKAAVAQASRDLAQINDLQAQLEeanKEKQELQEKLQALQSQVEFLEQSMVDKslvsrQEAKIRELETrlEF 1845
Cdd:COG2825 30 DVQRILQESPEGKAAQKKLEKEFKKRQAELQ---KLEKELQALQEKLQKEAATLSEEERQK-----KERELQKKQQ--EL 99
|
90 100
....*....|....*....|....*
gi 1093953565 1846 ERTQVKRLESLASRLKENMEKLTEE 1870
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 |
5.96e-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: 5.96e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1093953565 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 49 IKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATLLIE 87
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1737-2030 |
6.12e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1737 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDLAQINDLQAQLEEANKEKQELQEKLqaLQS 1814
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1815 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFERTQVKR--LESLAsRLKENMEKLTEERDQRIAAENREKEQNKRLQRQL 1892
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKL 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1893 RDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSE 1972
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNN 1249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1093953565 1973 LEDRVDGVKSWLSKNKGPSKAASDDgsLKSSSPTSYWKSLAPDRSDDEHDPLDNTSRP 2030
Cdd:PTZ00108 1250 SSKSSEDNDEFSSDDLSKEGKPKNA--PKRVSAVQYSPPPPSKRPDGESNGGSKPSSP 1305
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1395-1618 |
6.63e-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: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1395 DFTKKRLQ------QEFEDKLEVEQQN----KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqvr 1464
Cdd:pfam15905 148 DGTQKKMSslsmelMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE----- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1465 nhelekKQRRFDSELSQAHEEAQREKLqreklqrekdmllaEAFSLKQQLEEKDMDIagftqkvVSLEAELQdissqESK 1544
Cdd:pfam15905 223 ------KLLEYITELSCVSEQVEKYKL--------------DIAQLEELLKEKNDEI-------ESLKQSLE-----EKE 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093953565 1545 DEaslakvkkqlrdLEAKVKDQEEELdeqagtiQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK 1618
Cdd:pfam15905 271 QE------------LSKQIKDLNEKC-------KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQK 325
|
|
| PDZ_ARHGEF11-12-like |
cd23069 |
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
253-308 |
6.67e-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: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 253 VVHFAEPGAGTKdlaLGLVPGDRLVEINGHNVESKSRDEIVEMIRqSGDSVRLKVQ 308
Cdd:cd23069 25 VQSVKEGGAAYR---AGVQEGDRIIKVNGTLVTHSNHLEVVKLIK-SGSYVALTLL 76
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1626-1941 |
6.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1626 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQL 1704
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLE-EELEQARSELEQLEEELEELNEQLQAAQAElAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1705 EESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQE-DMNELMKKHKAAVA 1779
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQleslQEELAALEQELQAlSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1780 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQ--SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLA 1857
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKdsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1858 SRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1937
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
....
gi 1093953565 1938 FKRI 1941
Cdd:COG4372 351 LDND 354
|
|
| PDZ_MAST1 |
cd23073 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ... |
225-314 |
6.75e-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: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 225 RRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLalGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVR 304
Cdd:cd23073 8 QRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEA--GLCAGDLITHVNGEPVHGMVHPEVVELILKSGNKVA 85
|
90
....*....|
gi 1093953565 305 LKVQPIPELS 314
Cdd:cd23073 86 VTTTPFENTS 95
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1406-1773 |
6.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLT-------------------------AELQDTKLHLEG 1460
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlnlladetladrveeireqlDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1461 QQVRNHELEKKQRRFDSELSQaHEEAQREKLQREKLQREKDM---LLAE--------AFSLKQQLEEKDMDIA-GFTQKV 1528
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDAKQqafALTEvvqrrahfSYEDAAEMLAKNSDLNeKLRQRL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1529 VSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ---------MLEQAKLRLEMEMERMRQThs 1599
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgAEERARARRDELHARLSAN-- 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1600 kemESRDEEVEEARQSC--------------QKKLKQMEVQLEEEYEDKQKVLR-------EKRELEGKLATLSDQvnrr 1658
Cdd:PRK04863 1073 ---RSRRNQLEKQLTFCeaemdnltkklrklERDYHEMREQVVNAKAGWCAVLRlvkdngvERRLHRRELAYLSAD---- 1145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1659 dfESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKReiAQLKNQleeseFTCAAAVKARKAMEVEIedlhLQIDDIAKA 1738
Cdd:PRK04863 1146 --ELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKR--PERKVQ-----FYIAVYQHLRERIRQDI----IRTDDPVEA 1212
|
410 420 430
....*....|....*....|....*....|....*
gi 1093953565 1739 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1773
Cdd:PRK04863 1213 IEQMEIELSRLTEELTSREQKLAISSESVANIIRK 1247
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1727-1816 |
7.25e-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: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1727 DLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLaqiNDLQAQLEEANKEKQELQ 1806
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNL---ATAQAALANAEARLAKAK 338
|
90
....*....|
gi 1093953565 1807 EKLQALQSQV 1816
Cdd:TIGR04320 339 EALANLNADL 348
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1470-1622 |
7.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1470 KKQRRFDSELSQAHEEAQRE--KLQREKLQREKDMLLAEAFSLKQQL----EEKDMDIAGFTQKVVSLEAELQDISSQES 1543
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEaeEKLEAALLEAKELLLRERNQQRQEArrerEELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1544 KDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAK----LRLEMEMERMRQTHSKEMESRDEevEEARQSCQKK 1619
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRVAGLTP--EQARklllKLLDAELEEEKAQRVKKIEEEAD--LEAERKAQNI 181
|
...
gi 1093953565 1620 LKQ 1622
Cdd:PRK12705 182 LAQ 184
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1742-1931 |
7.85e-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: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1742 LEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQIND----LQAQLEEANKEKQELQEKLQAlqsQVE 1817
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEeeqrLQEEAEQLQKELEALAGQLQA---QVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1818 FLEQSmvdKSLVSRQEAKIRELETRLEFERTQVKRLEslasRLKENME--KLTeerDQRIAAENRE-KEQNKRLQRQ-LR 1893
Cdd:pfam15070 111 DNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGfVK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1093953565 1894 DTKEEM-------------GELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1931
Cdd:pfam15070 181 LTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1638-1972 |
8.07e-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: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1638 LREKRELEGKLATLSDQVNRRDFESEKRLRKD-LKRTKALLADaqlmLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVK 1716
Cdd:COG5185 66 VLDGLNYQNDVKKSESSVKARKFLKEKKLDTKiLQEYVNSLIK----LPNYEWSADILISLLYLYKSEIVALKDELIKVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1717 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkHKAAVAQASRDLAQINDLQAQLE 1796
Cdd:COG5185 142 KLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1797 EANKEKQElqeklqalqsqvefleqsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIA 1876
Cdd:COG5185 219 STLLEKAK---------------------------EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1877 AEN----REKEQNKRLQRQLRDTKEEMGELArKEAEASRKKHELEMDLESLEaANQSLQADLKLAFKRIGDLQAAIEDEM 1952
Cdd:COG5185 272 ENAesskRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQ 349
|
330 340
....*....|....*....|.
gi 1093953565 1953 ES-DENEDLINSEGDSDVDSE 1972
Cdd:COG5185 350 ESlTENLEAIKEEIENIVGEV 370
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1669-1925 |
8.17e-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: 41.04 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1669 DLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLS 1747
Cdd:pfam15964 348 NFEKTKALIQCEQLKSELERQKERLEKELAsQQEKRAQEKE-------ALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1748 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLA-QINDLQAQLEEANKEKQELQEKlqaLQSQVEFLEQsmvdk 1826
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1827 slvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqriaaenrEKEQNKRLQRQLRDTKEE-MGELARK 1905
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 1093953565 1906 EA-EASRKKHELEMDLESLEA 1925
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1570-1814 |
8.39e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1570 LDEQAGTIQMLEQAklrlemeMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKVLREKRElegKLA 1649
Cdd:pfam04012 17 LDKAEDPEKMLEQA-------IRDMQSELVKARQALAQTIARQKQL-ERRLEQQTEQAKKLEEKAQAALTKGNE---ELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1650 tlsdqvnRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQLEeseftcaaAVKARKAMeveiedl 1728
Cdd:pfam04012 86 -------REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQlAALETKIQQLKAKKN--------LLKARLKA------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1729 hlqiddiAKAKTALEEQLSRLQREKNEIQ-NRLEEDQEDMnelmkkhkAAVAQASRDLAQINDLQAQLEEANKEKQELQE 1807
Cdd:pfam04012 144 -------AKAQEAVQTSLGSLSTSSATDSfERIEEKIEER--------EARADAAAELASAVDLDAKLEQAGIQMEVSED 208
|
....*..
gi 1093953565 1808 KLQALQS 1814
Cdd:pfam04012 209 VLARLKA 215
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1800-1913 |
8.54e-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: 40.25 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1800 KEKQELQEKLQALQSQVEFLEQSmvDKSLvSRQEAKIRELETRLEFERTQVKRLESLASRL-----------KENMEKLT 1868
Cdd:cd16269 167 KAEEVLQEFLQSKEAEAEAILQA--DQAL-TEKEKEIEAERAKAEAAEQERKLLEEQQRELeqkledqersyEEHLRQLK 243
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1093953565 1869 EERDQRIaaENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKK 1913
Cdd:cd16269 244 EKMEEER--ENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1725-1892 |
8.64e-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: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1725 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR----------LEEDQEDMNELMKKHKAAVaqasRDLA-QINDLQA 1793
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKeskflenlasLKHENDNLSSMLNRKERRL----KDLEdQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1794 QLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEAK------IRELETRLE-FERTQVKRLESLASRL 1860
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSASETTLEAELerlqiqYDALVDSQNEYKdhyqqeINTLQESLEdLKLENEKQLENYQQRI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1093953565 1861 KENM----EKLTEERDQRIAAENREKEQNKRLQRQL 1892
Cdd:pfam17078 161 SSNDkdidTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1420-1575 |
8.76e-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: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1420 ERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSElsqaheeaQREKLQREklqRE 1499
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE--------ERREIRKD---RE 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093953565 1500 KDMLLAEAFSLKQQLEEKDMDIAGFTQKVvsleAELQDISSQESKDEASLAKVKKQLRdleakvKDQEEELDEQAG 1575
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKL----ERLKELWKLEHSGELVPVKVVEKFT------KEAIRRLEEEYG 532
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1268-1622 |
8.88e-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: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1268 IRNKDEEIQQLRSKLEKAE--KERNELRLNSDRLESRISELTSELTDERNTgesasQLLDAETAERLRAEKEMKELQTQY 1345
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEMMEE-----ERERALEEEEEKEEERKEERKRYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1346 DALKKQMEVMEMEVMEARLIRAAEingevddddagGEWRLKYERAVREVDFTKKRLQQEFEDKL--EVEQQNKRQLERRL 1423
Cdd:pfam13868 76 QELEEQIEEREQKRQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1424 GDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSElsQAHEEAQREKLQREKLQREKDML 1503
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE--KAERDELRAKLYQEEQERKERQK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1504 LAEAfsLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ--AGTIQMLE 1581
Cdd:pfam13868 223 EREE--AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIE 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1093953565 1582 QAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQ 1622
Cdd:pfam13868 301 EREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1406-1611 |
9.62e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1406 EDKLEVEqqnkrqlerrlgDLQADSEESQRALQQLKKKCQRLTAELQdtKLHLEGQQvrnhELEKKQRRFDSELSQAHEE 1485
Cdd:PRK00409 513 EDKEKLN------------ELIASLEELERELEQKAEEAEALLKEAE--KLKEELEE----KKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1486 AQrEKLqrEKLQREKDMLLAEafsLKQQLEEKDMDIAgftqkvvslEAELQDIssqeskdeasLAKVKKQLRDLEAKVKD 1565
Cdd:PRK00409 575 AQ-QAI--KEAKKEADEIIKE---LRQLQKGGYASVK---------AHELIEA----------RKRLNKANEKKEKKKKK 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1566 QEEELDE-------------QAGTI-QMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEE 1611
Cdd:PRK00409 630 QKEKQEElkvgdevkylslgQKGEVlSIPDDKEAIVQAGIMKMK-VPLSDLEKIQKPKKK 688
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
1785-1870 |
9.75e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 37.95 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953565 1785 LAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQ----SMVDKS----LVSRQEAK-IRELETRLEFERTQVKRLES 1855
Cdd:COG1382 13 LAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKlpddAEVYKSvgnlLVKTDKEEvIKELEEKKETLELRLKTLEK 92
|
90
....*....|....*
gi 1093953565 1856 LASRLKENMEKLTEE 1870
Cdd:COG1382 93 QEERLQKQLEELQEK 107
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
1199-1221 |
9.89e-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: 9.89e-03
|
| |
