|
Name |
Accession |
Description |
Interval |
E-value |
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
19-641 |
0e+00 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 898.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 19 LERDAEVEERRSWQENISLKELQSRGVCLLKLQVSsQRTGLYGRLLVTFEpRRYGSAAALPSnsftsGDIVGLYDAaNEG 98
Cdd:TIGR00376 1 LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFG-RRKAIATEISV-----GDIVLVSRG-NPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 99 SQLATGILTRVTQKSVTVAFDEShDFQLSLDRensYRLLKLANDVTYRRLKKALIALKKYHSgpasSLIEVLFGRSAPSP 178
Cdd:TIGR00376 73 QSDLTGVVTRVGKRFITVALEES-VPQWSLKR---VRIDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 179 ASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALC 258
Cdd:TIGR00376 145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 259 KQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVK-NKKTQDKREKSNFRNEIKLLRKELKEReEAA 337
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEErNKKTKPSPQKRRGLSDIKILRKALKKR-EAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 338 MLESLTSANVVLATNTGASADGPLKLLPES---------------------------YFDVVVIDECAQALEASCWIPLL 390
Cdd:TIGR00376 304 GIESLKIASMAEWIETNKSIDRLLKLLPESeerimneilaesdatnsmagseilngqYFDVAVIDEASQAMEPSCLIPLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 391 KARKCILAGDHKQLPPTTVSHKAalAGLSLSLMERLAEEYGARvVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARH 470
Cdd:TIGR00376 384 KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKEYPER-SRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 471 LLRDLPGVAATEE-----TGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQV 545
Cdd:TIGR00376 461 LLRDLPKVEATESeddleTGIPLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQV 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 546 DLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKT 625
Cdd:TIGR00376 541 DLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKR 620
|
650
....*....|....*.
gi 119392094 626 LVEYFTQHGEVRTAFE 641
Cdd:TIGR00376 621 LIEWCKQHGEVREAFK 636
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
191-443 |
5.81e-111 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350802 [Multi-domain] Cd Length: 191 Bit Score: 340.74 E-value: 5.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18044 1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLArsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsANVVLA 350
Cdd:cd18044 81 LLESVLDHSLDALVA-----------------------------------------------------------AQVVLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADGplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18044 102 TNTGAGSRQ---LLPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLY 178
|
250
....*....|...
gi 119392094 431 GARVVRTLTVQYR 443
Cdd:cd18044 179 GESVVRMLTVQYR 191
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
418-615 |
6.38e-73 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 238.99 E-value: 6.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 418 LSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPgvaATEETGVPLLLVDTAGCg 497
Cdd:pfam13087 1 LDRSLFERLQELGPSAVV-MLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDF---HLPDPLGPLVFIDVDGS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 498 lFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPA-RDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKE 573
Cdd:pfam13087 76 -EEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggkLEIEVNTVDGFQGREKD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119392094 574 AVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSR 615
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
14-630 |
2.16e-69 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 248.12 E-value: 2.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 14 LDLLELERDAEVEERRSWQENISLKELQSRGVCLLKLQVSSQRTGLYGRLLVTFEPRRYGSAAALPSNSFTSGDIVGLYD 93
Cdd:COG1112 206 LLLLLLLLALLLLLALLLLLDALLLLLAALALLALALLLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 94 AANEGSQLATGILTRVTQKSVTVAFDESHDFQLSLDRENSYRLLKLANDVTYRRLKKALIALKKYHSGPASSLIEVLFGR 173
Cdd:COG1112 286 ALLAALALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 174 SAPSPASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG1112 366 ALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 254 RLALCKQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvkNKKTQDKREKSNFRNEIKLLRKELKER 333
Cdd:COG1112 446 AALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEEL--EKLIAELREAARLRRALRRELKKRREL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 334 EEAAMLESLTSANVVLATNTGASADGPLKllpESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVS--- 410
Cdd:COG1112 524 RKLLWDALLELAPVVGMTPASVARLLPLG---EGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGeea 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 411 HKAALAGLSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPGvaateetgvPLLL 490
Cdd:COG1112 601 EEVAEEGLDESLLDRLLARLPERGV-MLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS---------PLVF 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 491 VDTAGCGlfeleEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQVDLLRQSL----VHRHPELEIKSVDG 566
Cdd:COG1112 671 IDVDGVY-----ERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLrealGDGLEPVFVGTVDR 745
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 567 FQGREKEAVILSFVRSNRK---GEVGFLAED-RRINVAVTRARRHVAVICDSRTV---NNHAFLKTLVEYF 630
Cdd:COG1112 746 FQGDERDVIIFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYL 816
|
|
| R3H_Smubp-2_like |
cd02641 |
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ... |
726-784 |
1.38e-27 |
|
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.
Pssm-ID: 100070 Cd Length: 60 Bit Score: 105.90 E-value: 1.38e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMAS-KKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02641 1 VKHLKAMVKAFMKDpKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
706-785 |
1.19e-18 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 81.19 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 706 APSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSKR 785
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
733-784 |
1.17e-11 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 60.58 E-value: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119392094 733 IVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:pfam01424 10 LAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| ZnF_AN1 |
smart00154 |
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ... |
902-937 |
1.18e-08 |
|
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.
Pssm-ID: 197545 Cd Length: 39 Bit Score: 51.62 E-value: 1.18e-08
10 20 30
....*....|....*....|....*....|....*.
gi 119392094 902 CTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERAR 937
Cdd:smart00154 4 CRKKVGLTGFKCRHCGNLFCGEHRLPEDHDCPGDYK 39
|
|
| zf-AN1 |
pfam01428 |
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ... |
897-934 |
2.02e-08 |
|
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.
Pssm-ID: 460208 Cd Length: 37 Bit Score: 50.77 E-value: 2.02e-08
10 20 30
....*....|....*....|....*....|....*...
gi 119392094 897 CGFAKCTAGVTTLGQfCQLCSRRYCLSHHLPEIHGCGE 934
Cdd:pfam01428 1 CSFKGCKKKDFLPFK-CRFCGKNFCLKHRLPEDHDCSG 37
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
196-256 |
1.93e-07 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 52.49 E-value: 1.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094 196 QKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL--KVLCCAPSNIAVDNLVERLA 256
Cdd:smart00487 13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELK 75
|
|
| PRK12438 |
PRK12438 |
hypothetical protein; Provisional |
786-845 |
1.05e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 171499 [Multi-domain] Cd Length: 991 Bit Score: 46.39 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 786 APRPRAALGPPAGTGGPAPLQPVPPtPAQTEQPPREQRGPDQPDLRTLHLER-LQRVRSAQ 845
Cdd:PRK12438 905 APGGDAASAPPPGAGPPAPPQAVPP-PRTTQPPAAPPRGPDVPPAAVAELREtLADLRSAQ 964
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
662-878 |
2.29e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 662 AATKPQGPATSTRTGSQRQEGGQEAAAPARQgrkKPAGKSLASEAPSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKK 741
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 742 MQLEFPPSLNSHDRLRVH-QIAEEHGLRHDSSGEGKRRFITVSKRAPRPRAALGPPAGTGGPAPLQPVPPTPAQTE---Q 817
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfaL 2900
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 818 PPREQRGPDQPDLRTLHLERLQRVRSAQGQPAsKEQQASGQQKLPEKKKKKAKGHPATDLP 878
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP-PPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
204-275 |
3.26e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 40.15 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQRilrlGHPARLLESI 275
Cdd:NF038214 87 IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRF-----TTAADLVEQLAQARAD----GRLGRLLRRL 149
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
19-641 |
0e+00 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 898.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 19 LERDAEVEERRSWQENISLKELQSRGVCLLKLQVSsQRTGLYGRLLVTFEpRRYGSAAALPSnsftsGDIVGLYDAaNEG 98
Cdd:TIGR00376 1 LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFG-RRKAIATEISV-----GDIVLVSRG-NPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 99 SQLATGILTRVTQKSVTVAFDEShDFQLSLDRensYRLLKLANDVTYRRLKKALIALKKYHSgpasSLIEVLFGRSAPSP 178
Cdd:TIGR00376 73 QSDLTGVVTRVGKRFITVALEES-VPQWSLKR---VRIDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 179 ASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALC 258
Cdd:TIGR00376 145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 259 KQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVK-NKKTQDKREKSNFRNEIKLLRKELKEReEAA 337
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEErNKKTKPSPQKRRGLSDIKILRKALKKR-EAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 338 MLESLTSANVVLATNTGASADGPLKLLPES---------------------------YFDVVVIDECAQALEASCWIPLL 390
Cdd:TIGR00376 304 GIESLKIASMAEWIETNKSIDRLLKLLPESeerimneilaesdatnsmagseilngqYFDVAVIDEASQAMEPSCLIPLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 391 KARKCILAGDHKQLPPTTVSHKAalAGLSLSLMERLAEEYGARvVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARH 470
Cdd:TIGR00376 384 KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKEYPER-SRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 471 LLRDLPGVAATEE-----TGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQV 545
Cdd:TIGR00376 461 LLRDLPKVEATESeddleTGIPLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQV 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 546 DLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKT 625
Cdd:TIGR00376 541 DLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKR 620
|
650
....*....|....*.
gi 119392094 626 LVEYFTQHGEVRTAFE 641
Cdd:TIGR00376 621 LIEWCKQHGEVREAFK 636
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
191-443 |
5.81e-111 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350802 [Multi-domain] Cd Length: 191 Bit Score: 340.74 E-value: 5.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18044 1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLArsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsANVVLA 350
Cdd:cd18044 81 LLESVLDHSLDALVA-----------------------------------------------------------AQVVLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADGplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18044 102 TNTGAGSRQ---LLPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLY 178
|
250
....*....|...
gi 119392094 431 GARVVRTLTVQYR 443
Cdd:cd18044 179 GESVVRMLTVQYR 191
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
418-615 |
6.38e-73 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 238.99 E-value: 6.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 418 LSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPgvaATEETGVPLLLVDTAGCg 497
Cdd:pfam13087 1 LDRSLFERLQELGPSAVV-MLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDF---HLPDPLGPLVFIDVDGS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 498 lFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPA-RDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKE 573
Cdd:pfam13087 76 -EEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggkLEIEVNTVDGFQGREKD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119392094 574 AVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSR 615
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
14-630 |
2.16e-69 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 248.12 E-value: 2.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 14 LDLLELERDAEVEERRSWQENISLKELQSRGVCLLKLQVSSQRTGLYGRLLVTFEPRRYGSAAALPSNSFTSGDIVGLYD 93
Cdd:COG1112 206 LLLLLLLLALLLLLALLLLLDALLLLLAALALLALALLLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 94 AANEGSQLATGILTRVTQKSVTVAFDESHDFQLSLDRENSYRLLKLANDVTYRRLKKALIALKKYHSGPASSLIEVLFGR 173
Cdd:COG1112 286 ALLAALALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 174 SAPSPASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG1112 366 ALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 254 RLALCKQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvkNKKTQDKREKSNFRNEIKLLRKELKER 333
Cdd:COG1112 446 AALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEEL--EKLIAELREAARLRRALRRELKKRREL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 334 EEAAMLESLTSANVVLATNTGASADGPLKllpESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVS--- 410
Cdd:COG1112 524 RKLLWDALLELAPVVGMTPASVARLLPLG---EGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGeea 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 411 HKAALAGLSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPGvaateetgvPLLL 490
Cdd:COG1112 601 EEVAEEGLDESLLDRLLARLPERGV-MLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS---------PLVF 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 491 VDTAGCGlfeleEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQVDLLRQSL----VHRHPELEIKSVDG 566
Cdd:COG1112 671 IDVDGVY-----ERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLrealGDGLEPVFVGTVDR 745
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 567 FQGREKEAVILSFVRSNRK---GEVGFLAED-RRINVAVTRARRHVAVICDSRTV---NNHAFLKTLVEYF 630
Cdd:COG1112 746 FQGDERDVIIFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYL 816
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
195-410 |
2.24e-68 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 228.77 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 195 SQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL-------KVLCCAPSNIAVDNLVERLALCKQ----RIL 263
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPAtsaaagpRILVCAPSNAAVDNILERLLRKGQkygpKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 264 RLGHPARLLESIQQHSLDAVLAR----SDSAQIVADIRK------------------DIDQVFVKNKKTQDKREKSNFRN 321
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESklnnEEDAQIVKDISKeleklakalrafekeiivEKLLKSRNKDKSKLEQERRKLRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 322 EIKLLRKELKEREEAAMLESLTSANVVLATNTGASADgplKLLPESYFDVVVIDECAQALEASCWIPLLKA-RKCILAGD 400
Cdd:pfam13086 161 ERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSR---LLSSLANFDVVIIDEAAQALEPSTLIPLLRGpKKVVLVGD 237
|
250
....*....|
gi 119392094 401 HKQLPPTTVS 410
Cdd:pfam13086 238 PKQLPPTVIS 247
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
444-630 |
3.24e-59 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350195 [Multi-domain] Cd Length: 184 Bit Score: 200.54 E-value: 3.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 444 MHQAIMRWASDTMYLGQLTAHSSVARHLLRDlpgvaATEETGVPLLLVDTAGCglfELEEEDEQSKGNPGEVRLVSLHIQ 523
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-----PLPGPSKPLVFVDVSGG---EEREESGTSKSNEAEAELVVELVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 524 ALVDAGVPARDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKEAVILSFVRSNRKGE-VGFLAEDRRINV 599
Cdd:cd18808 73 YLLKSGVKPSSIGVITPYRAQVALIRELLRKRGgllEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|.
gi 119392094 600 AVTRARRHVAVICDSRTVNNHAFLKTLVEYF 630
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
191-443 |
6.27e-45 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350799 [Multi-domain] Cd Length: 203 Bit Score: 160.86 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLARSDSAQivadirkdidqvfvknkktqdkreksnfrneikllrkELKereeaamlESLTSANVVLA 350
Cdd:cd18041 81 IHPDVQEFTLEAILKSCKSVE-------------------------------------ELE--------SKYESVSVVAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADgplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18041 116 TCLGINHP----IFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAH 191
|
250
....*....|...
gi 119392094 431 GARVVrTLTVQYR 443
Cdd:cd18041 192 PDAVV-QLTIQYR 203
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
192-443 |
6.96e-45 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350797 [Multi-domain] Cd Length: 234 Bit Score: 162.03 E-value: 6.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALsQKELAIIHGPPGTGKTTTVVEIILQAVKQGL-KVLCCAPSNIAVDNLVERLALCKQRILRLghPAR 270
Cdd:cd18039 2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVYHLVKQGNgPVLVCAPSNVAVDQLTEKIHQTGLKVVRL--CAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLARsdsaqivaDIRK-DIDQVFVKNKKTQDKREKSNFRNEIKLlrKELKEREEAAMLESltsANVVL 349
Cdd:cd18039 79 SREAVESPVSFLALHN--------QVRNlDSAEKLELLKLLKLETGELSSADEKRY--RKLKRKAERELLRN---ADVIC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 350 ATNTGAsADgplKLLPESYFDVVVIDECAQALEASCWIPLLK-ARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAe 428
Cdd:cd18039 146 CTCVGA-GD---PRLSKMKFRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLV- 220
|
250
....*....|....*
gi 119392094 429 EYGARVVRtLTVQYR 443
Cdd:cd18039 221 QLGIRPIR-LQVQYR 234
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
192-443 |
1.29e-37 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438712 [Multi-domain] Cd Length: 218 Bit Score: 140.43 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALS-QKELAIIHGPPGTGKTTTVVEII-------------------------LQAVKQGLKVLCCAPSN 245
Cdd:cd18042 1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILsvllagkyrkyyekvkkklrklqrnLNNKKKKNRILVCAPSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 246 IAVDNLVERLalckqrilrlghparllesiqqhsldavlarsdsaqivadirkdidqvfvKNKKTQDKREKSNFRNEIKL 325
Cdd:cd18042 81 AAVDEIVLRL--------------------------------------------------LSEGFLDGDGRSYKPNVVRV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 326 LRKELKEreeaamlESLTSANVVLATNTGASADgPLKLLPESyFDVVVIDECAQALEASCWIPL-LKARKCILAGDHKQL 404
Cdd:cd18042 111 GRQELRA-------SILNEADIVCTTLSSSGSD-LLESLPRG-FDTVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQL 181
|
250 260 270
....*....|....*....|....*....|....*....
gi 119392094 405 PPTTVSHKAALAGLSLSLMERLaEEYGARVVrTLTVQYR 443
Cdd:cd18042 182 PATVFSKVAQKLGYDRSLFERL-QLAGYPVL-MLTTQYR 218
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
196-443 |
1.89e-37 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 140.45 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 196 QKEAVLFALSQKELA---IIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLVERLA---LCKQRILRLGH 267
Cdd:cd18038 6 QKLAVRNIVTGTSRPppyIIFGPPGTGKTVTLVEAILQVLRQppEARILVCAPSNSAADLLAERLLnalVTKREILRLNA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 268 PARllesiqqhsldavlarsdsaqivadIRKDIDQVFVKnkktqdkreksnFRNEIKLLRKELKEREEaamlesLTSANV 347
Cdd:cd18038 86 PSR-------------------------DRASVPPELLP------------YCNSKAEGTFRLPSLEE------LKKYRI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 348 VLATNTGASadgplKL----LPESYFDVVVIDECAQALEASCWIPL----LKARKCILAGDHKQLPPTTVSHKAALAGLS 419
Cdd:cd18038 123 VVCTLMTAG-----RLvqagVPNGHFTHIFIDEAGQATEPEALIPLselaSKNTQIVLAGDPKQLGPVVRSPLARKYGLG 197
|
250 260 270
....*....|....*....|....*....|..
gi 119392094 420 LSLMERLAE--------EYGARVVRTLTVQYR 443
Cdd:cd18038 198 KSLLERLMErplyykdgEYNPSYITKLLKNYR 229
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
209-443 |
3.56e-30 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438708 [Multi-domain] Cd Length: 121 Bit Score: 115.41 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 209 LAIIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLverlalckqrilrlghparllesiqqhsldavlar 286
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQLLKGlrGKRVLVTAQSNVAVDNV----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 287 sdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsanvvlatntgasadgplkllpe 366
Cdd:cd17934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119392094 367 syfDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLS--LSLMERLAEEYGARVVRTLTVQYR 443
Cdd:cd17934 46 ---DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAALLGLSfiLSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| R3H_Smubp-2_like |
cd02641 |
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ... |
726-784 |
1.38e-27 |
|
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.
Pssm-ID: 100070 Cd Length: 60 Bit Score: 105.90 E-value: 1.38e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMAS-KKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02641 1 VKHLKAMVKAFMKDpKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
191-443 |
1.40e-25 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350836 [Multi-domain] Cd Length: 230 Bit Score: 106.30 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAV---LFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLVERLALCKqrILRL 265
Cdd:cd18078 1 DLNELQKEAVkriLGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNlpRSRILVCAPSNSAADLVTSRLHESK--VLKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 266 GHPARllesiqqhsLDAVLARSDsaqIVADIRKDIDqvfvknKKTQDKREKSNFRneikllrkelkereeaamlesltsa 345
Cdd:cd18078 79 GDMVR---------LNAVNRFES---TVIDARKLYC------RLGEDLSKASRHR------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 nVVLATNTGASADGPLKlLPESYFDVVVIDECAQALEASCWIPL----LKARKCILAGDHKQLPPTTVSHKAALAGLSLS 421
Cdd:cd18078 116 -IVISTCSTAGLLYQMG-LPVGHFTHVFVDEAGQATEPESLIPLglisSRDGQIILAGDPMQLGPVIKSRLASAYGLGVS 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 119392094 422 LMERLAEE---------------YGARVVRTLTVQYR 443
Cdd:cd18078 194 FLERLMNRplylrdpnrfgesggYNPLLVTKLVDNYR 230
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
192-443 |
6.16e-20 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350798 [Multi-domain] Cd Length: 271 Bit Score: 91.05 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSqKELAIIHGPPGTGKTTTVVEIILQAVKQ-------------GLKVLCCAPSNIAVDNLVERL-AL 257
Cdd:cd18040 2 LNPSQNHAVRTALT-KPFTLIQGPPGTGKTVTGVHIAYWFAKQnreiqsvsgegdgGPCVLYCGPSNKSVDVVAELLlKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 258 CKQRILRL-GHPARLLE----SIQQHSLDAVLARSDSAQIVADI--RKDIDQVfvKNKKTQDKREksnFRNEIKLLRKEL 330
Cdd:cd18040 81 PGLKILRVySEQIETTEypipNEPRHPNKKSERESKPNSELSSItlHHRIRQP--SNPHSQQIKA---FEARFERTQEKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 331 KEREE--------AAMLESLTSANVVLATNTGASADgplKLLPESYFDVVVIDECAQALEASCWIPLLKARKC---ILAG 399
Cdd:cd18040 156 TEEDIktykiliwEARFEELETVDVILCTCSEAASQ---KMRTHANVKQCIVDECGMCTEPESLIPIVSAPRAeqvVLIG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 119392094 400 DHKQLPPTTVSHKAALAGLSLSLMERLAEEygarvVRTLTVQYR 443
Cdd:cd18040 233 DHKQLRPVVQNKEAQKLGLGRSLFERYAEK-----ACMLDTQYR 271
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
192-442 |
9.07e-20 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350694 [Multi-domain] Cd Length: 178 Bit Score: 87.60 E-value: 9.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQkELAIIHGPPGTGKTTT---VVEIILQAVKQGLK--VLCCAPSNIAVDNLVER-LALCKQRILRL 265
Cdd:cd17936 2 LDPSQLEALKHALTS-ELALIQGPPGTGKTFLgvkLVRALLQNQDLSITgpILVVCYTNHALDQFLEGlLDFGPTKIVRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 266 GhparllesiqqhsldavlarsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsA 345
Cdd:cd17936 81 G------------------------------------------------------------------------------A 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 NVVLATNTGASADgpLKLLPESYFDVVVIDECAQALEA---SCWIPllKARKCILAGDHKQLPPTTVSHKAALAG--LSL 420
Cdd:cd17936 83 RVIGMTTTGAAKY--RELLQALGPKVVIVEEAAEVLEAhilAALTP--STEHLILIGDHKQLRPKVNVYELTAKKynLDV 158
|
250 260
....*....|....*....|..
gi 119392094 421 SLMERLAEEyGARVVrTLTVQY 442
Cdd:cd17936 159 SLFERLVKN-GLPFV-TLNVQR 178
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
706-785 |
1.19e-18 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 81.19 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 706 APSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSKR 785
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
192-430 |
4.17e-13 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350835 [Multi-domain] Cd Length: 226 Bit Score: 69.82 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQKELAI----IHGPPGTGKTTTVVEIILQAVKQ-GLKVLCCAPSNIAVDNLVERLAlckqrilrlg 266
Cdd:cd18077 2 LNAKQKEAVLAITTPLSIQLppvlLIGPFGTGKTFTLAQAVKHILQQpETRILICTHSNSAADLYIKEYL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 267 HPARLLESIQQHSLdAVLARSDSaqiVADIRKDIDQVFVKNkktqdkrEKSNFRNEIKllrkelkereeaamlESLTSAN 346
Cdd:cd18077 72 HPYVETGNPRARPL-RVYYRNRW---VKTVHPVVQKYCLID-------EHGTFRMPTR---------------EDVMRHR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 347 VVLATNTGASADGPLKLLPeSYFDVVVIDECAQALEASCWIPLLKARK---CILAGDHKQLPPTTVSHKAALAGLSLSLM 423
Cdd:cd18077 126 VVVVTLSTSQYLCQLDLEP-GFFTHILLDEAAQAMECEAIMPLALATKstrIVLAGDHMQLSPEVYSEFARERNLHISLL 204
|
....*..
gi 119392094 424 ERLAEEY 430
Cdd:cd18077 205 ERLYEHY 211
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
192-253 |
6.24e-12 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 69.24 E-value: 6.24e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 192 LDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG0507 125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSE 186
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
726-784 |
8.81e-12 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 61.09 E-value: 8.81e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMASK-KMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02325 1 REEREEELEAFAKDAaGKSLELPP-MNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
733-784 |
1.17e-11 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 60.58 E-value: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119392094 733 IVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:pfam01424 10 LAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
195-450 |
1.38e-11 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 64.76 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 195 SQKEAVLFAlSQKELAIIHGPPGTGKTTTVVEII--LQAVKQGLKVLCCAPSNIAVDNLVERL--ALCKQR-ILRLGHPA 269
Cdd:cd17935 9 TQIEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIIsnLYHNFPNQRTLIVTHSNQALNQLFEKImaLDIDERhLLRLGHGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 270 RLLESIQQHsldAVLARSDsaqivadirkdidqvFVknkktqdkreKSNFRneikllrkelkereeaamlesltsanvvl 349
Cdd:cd17935 88 KIIAMTCTH---AALKRGE---------------LV----------ELGFK----------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 350 atntgasadgplkllpesyFDVVVIDECAQALEASCWIPLL---------KARKCILAGDHKQLPPttVSHKAALAGLS- 419
Cdd:cd17935 111 -------------------YDNILMEEAAQILEIETFIPLLlqnpedgpnRLKRLIMIGDHHQLPP--VIKNMAFQKYSn 169
|
250 260 270
....*....|....*....|....*....|...
gi 119392094 420 --LSLMERLAeEYGARVVRtLTVQYRMHQAIMR 450
Cdd:cd17935 170 meQSLFTRLV-RLGVPTVD-LDAQGRARASISS 200
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
193-406 |
2.76e-11 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350801 [Multi-domain] Cd Length: 127 Bit Score: 61.83 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 193 DTSQKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDnlverlalckqrilrlghparll 272
Cdd:cd18043 1 DSSQEAAIISARNGK-NVVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALD----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 273 esiqqhsldaVLARSdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaAMLESLTSANVVLATN 352
Cdd:cd18043 57 ----------VVRFP-------------------------------------------------CWIMSPLSVSQYLPLN 77
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 119392094 353 TGasadgplkllpesYFDVVVIDECAQALEASCwIPLL-KARKCILAGDHKQLPP 406
Cdd:cd18043 78 RN-------------LFDLVIFDEASQIPIEEA-LPALfRGKQVVVVGDDKQLPP 118
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
196-253 |
3.50e-10 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 59.49 E-value: 3.50e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119392094 196 QKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:cd17933 2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSE 58
|
|
| R3H_G-patch |
cd02646 |
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a ... |
726-784 |
4.81e-09 |
|
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100075 Cd Length: 58 Bit Score: 53.34 E-value: 4.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119392094 726 VDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02646 1 IEDIKDEIEAFLLDSRDSLSFPP-MDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVTK 58
|
|
| ZnF_AN1 |
smart00154 |
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ... |
902-937 |
1.18e-08 |
|
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.
Pssm-ID: 197545 Cd Length: 39 Bit Score: 51.62 E-value: 1.18e-08
10 20 30
....*....|....*....|....*....|....*.
gi 119392094 902 CTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERAR 937
Cdd:smart00154 4 CRKKVGLTGFKCRHCGNLFCGEHRLPEDHDCPGDYK 39
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
533-608 |
1.45e-08 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350173 [Multi-domain] Cd Length: 89 Bit Score: 52.82 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 533 RDIAVVSPYNLQVDLLRQSLVHRH------PELEIKSVDGFQGREKEAVILSFVRSNrkgevgfLAEDRRINVAVTRARR 606
Cdd:cd18786 11 YKGVVLTPYHRDRAYLNQYLQGLSldefdlQLVGAITIDSSQGLTFDVVTLYLPTAN-------SLTPRRLYVALTRARK 83
|
..
gi 119392094 607 HV 608
Cdd:cd18786 84 RL 85
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
196-265 |
1.55e-08 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 54.15 E-value: 1.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094 196 QKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQG---LKVLCCAPSNIAVDNLVERLALCKQRILRL 265
Cdd:pfam13245 1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKRLSERTGLPASTIHRL 72
|
|
| zf-AN1 |
pfam01428 |
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ... |
897-934 |
2.02e-08 |
|
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.
Pssm-ID: 460208 Cd Length: 37 Bit Score: 50.77 E-value: 2.02e-08
10 20 30
....*....|....*....|....*....|....*...
gi 119392094 897 CGFAKCTAGVTTLGQfCQLCSRRYCLSHHLPEIHGCGE 934
Cdd:pfam01428 1 CSFKGCKKKDFLPFK-CRFCGKNFCLKHRLPEDHDCSG 37
|
|
| R3H_DEXH_helicase |
cd06007 |
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ... |
732-784 |
2.61e-08 |
|
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100077 Cd Length: 59 Bit Score: 51.16 E-value: 2.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 119392094 732 MIVEFMASKKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd06007 7 ALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
196-256 |
1.93e-07 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 52.49 E-value: 1.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094 196 QKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL--KVLCCAPSNIAVDNLVERLA 256
Cdd:smart00487 13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELK 75
|
|
| R3H_NRF |
cd02640 |
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ... |
730-784 |
2.05e-07 |
|
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100069 Cd Length: 60 Bit Score: 48.55 E-value: 2.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 119392094 730 RAMIVEFMASKKMQ-LEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02640 5 RQIIQNYAHSDDIRdMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
192-280 |
3.33e-07 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 51.80 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAV-LFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:pfam13604 2 LNAEQAAAVrALLTSGDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAKVLGEELGIPADTIAKLLHRLG 81
|
90
....*....|
gi 119392094 271 LLESIQQHSL 280
Cdd:pfam13604 82 GRAGLDPGTL 91
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
346-442 |
7.82e-07 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 49.02 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 NVVLATNTGASADgplkllpesYFDVVVIDECAQALEASCWIP---LLKARKCILAGDHKQLPPTTVSHKAALAGLSLSL 422
Cdd:cd17914 33 RILLVTPTNKAAA---------QLDNILVDEAAQILEPETSRLidlALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSL 103
|
90 100
....*....|....*....|
gi 119392094 423 MERLAeEYGARVVRtLTVQY 442
Cdd:cd17914 104 FTRLV-RLGVSLIR-LQVQY 121
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
192-406 |
8.12e-07 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350834 [Multi-domain] Cd Length: 230 Bit Score: 51.04 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQKELA------IIHGPPGTGKTTTVVEIILQAVKQ-GLKVLCCAPSNIAVDNLVERLAlckQRILR 264
Cdd:cd18076 2 GNNKQQLAFNFIAGKPSEArfvpplLIYGPFGTGKTFTLAMAALEVIREpGTKVLICTHTNSAADIYIREYF---HPYVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 265 LGHPArlLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvknkktqdkreksnfrneikllrkELKEREEaamlesLTS 344
Cdd:cd18076 79 KGHPE--ARPLRIKATDRPNAITDPDTITYCCLTKDRQCF------------------------RLPTRDE------LDF 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119392094 345 ANVVLATNTGASAdgpLKLLPeSYFDVVVIDECAQALEASCWIPLLKA---RKCILAGDHKQLPP 406
Cdd:cd18076 127 HNIVITTTAMAFN---LHVLS-GFFTHIFIDEAAQMLECEALIPLSYAgpkTRVVLAGDHMQMTP 187
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
192-555 |
5.06e-06 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 50.32 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQkeLAIIHGPpGTGKTTTVVEIILQAVKQGL----KVLCCAPSNIAVDNLVERL------------ 255
Cdd:COG0210 7 LNPEQRAAVEHPEGP--LLVLAGA-GSGKTRVLTHRIAYLIAEGGvdpeQILAVTFTNKAAREMRERIeallgrlarglw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 256 -----ALCkQRILRLgHPARL-LESIQQhsldaVLARSDSAQIVADIRKDIDQvfvknkkTQDKREKSNFRNEIKLLRKE 329
Cdd:COG0210 84 vgtfhSLA-LRILRR-HAELLgLPPNFT-----ILDGDDQLRLIKELLKELGL-------DEKRFPPRELLSLISRAKNE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 330 LKEREEAAMLESLTSANVVLAT----------NTGAsAD------GPLKLL---PE------SYFDVVVIDEC-----AQ 379
Cdd:COG0210 150 GLTPEELAELLAADPEWRAAAElyeayqerlrANNA-LDfddlllLAVRLLeenPEvlekyqNRFRYILVDEYqdtnpAQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 380 ALeascwipLLKArkciLAGDHKQLpptTV---------SHKAAlaglSLSLMERLAEEYGARVVRTLTVQYRMHQAImr 450
Cdd:COG0210 229 YE-------LLRL----LAGDGRNL---CVvgdddqsiyGFRGA----DPENILRFEKDFPDAKVIKLEQNYRSTQNI-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 451 wasdtmylgqLTAHSSVARHLLRDLPGVAATE-ETGVPLLLVdtagcglfELEEEDEqskgnpgEVRLVSLHIQALVDAG 529
Cdd:COG0210 289 ----------LDAANAVIANNPGRLGKNLWTDnGEGEKVRLY--------VAPDEEE-------EARFVADEIRELHEEG 343
|
410 420
....*....|....*....|....*.
gi 119392094 530 VPARDIAVVSPYNLQVDLLRQSLVHR 555
Cdd:COG0210 344 VPLSDIAVLYRTNAQSRALEEALRRA 369
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
209-251 |
6.20e-06 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 46.33 E-value: 6.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 119392094 209 LAIIHGPPGTGKTTTVVEIIL----QAVKQGLKVLCCAPSNIAVDNL 251
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAalmqNKNGEPGRILLVTPTNKAAAQL 47
|
|
| R3H_encore_like |
cd02642 |
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ... |
733-785 |
5.49e-05 |
|
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100071 Cd Length: 63 Bit Score: 41.82 E-value: 5.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 119392094 733 IVEFMASKK-MQLEFPPSlNSHDRLRVHQIAEEHGLRHDSSGEGKRRfITVSKR 785
Cdd:cd02642 12 LLAFIKDSTrQSLELPPM-NSYYRLLAHRVAQYYGLDHNVDNSGGKC-VIVNKT 63
|
|
| PRK12438 |
PRK12438 |
hypothetical protein; Provisional |
786-845 |
1.05e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 171499 [Multi-domain] Cd Length: 991 Bit Score: 46.39 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 786 APRPRAALGPPAGTGGPAPLQPVPPtPAQTEQPPREQRGPDQPDLRTLHLER-LQRVRSAQ 845
Cdd:PRK12438 905 APGGDAASAPPPGAGPPAPPQAVPP-PRTTQPPAAPPRGPDVPPAAVAELREtLADLRSAQ 964
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
173-275 |
1.19e-04 |
|
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273631 [Multi-domain] Cd Length: 582 Bit Score: 45.91 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 173 RSAPSPASE-IHPLTFFNTcldtSQKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIIL----QAVKQG-LKVLCCAPSNI 246
Cdd:TIGR01447 129 RTAPSAILEnLFPLLNEQN----WRKTAVALALKSN-FSLITGGPGTGKTTTVARLLLalvkQSPKQGkLRIALAAPTGK 203
|
90 100
....*....|....*....|....*....
gi 119392094 247 AVDNLVERLalcKQRILRLGHPARLLESI 275
Cdd:TIGR01447 204 AAARLAESL---RKAVKNLAAAEALIAAL 229
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
501-612 |
1.52e-04 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350194 [Multi-domain] Cd Length: 150 Bit Score: 42.99 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 501 LEEEDEQSkgnpgEVRLVSLHIQALVDAG-VPARDIAVVSPYNLQVDLLRQSLvhrhpELEIKSVDGFQGREKEAVILSF 579
Cdd:cd18807 37 LLAKDEAD-----EAKAIADEIKRLIESGpVQYSDIAILVRTNRQARVIEEAL-----RVTLMTIHASKGLEFPVVFIVG 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 119392094 580 VRSNRKGEVGF----------LAEDRRI-NVAVTRARRHVAVIC 612
Cdd:cd18807 107 LGEGFIPSDASyhaakedeerLEEERRLlYVALTRAKKELYLVG 150
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
207-255 |
2.31e-04 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 42.54 E-value: 2.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 119392094 207 KELAIIHGPPGTGKTTTVV-EIILQAVKQGLKVLCCAPSNIAVDNLVERL 255
Cdd:cd17931 1 GQLTVLDLHPGAGKTTRVLpQIIREAIKKRLRTLVLAPTRVVAAEMYEAL 50
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
211-359 |
2.31e-04 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 43.75 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 211 IIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLalcKQRILRLGHP-ARLLES--IQQHSLDAVLARS 287
Cdd:COG0467 24 LLSGPPGTGKTTLALQFLAEGLRRGEKGLY-----VSFEESPEQL---LRRAESLGLDlEEYIESglLRIIDLSPEELGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 288 DSAQIVADIRKDIDqvfvknkKTQDKR--------------EKSNFRNEIKLLRKELKEREEAAMLESLTSANVVLATNT 353
Cdd:COG0467 96 DLEELLARLREAVE-------EFGAKRvvidslsglllalpDPERLREFLHRLLRYLKKRGVTTLLTSETGGLEDEATEG 168
|
....*...
gi 119392094 354 GAS--ADG 359
Cdd:COG0467 169 GLSylADG 176
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
662-878 |
2.29e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 662 AATKPQGPATSTRTGSQRQEGGQEAAAPARQgrkKPAGKSLASEAPSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKK 741
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 742 MQLEFPPSLNSHDRLRVH-QIAEEHGLRHDSSGEGKRRFITVSKRAPRPRAALGPPAGTGGPAPLQPVPPTPAQTE---Q 817
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfaL 2900
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 818 PPREQRGPDQPDLRTLHLERLQRVRSAQGQPAsKEQQASGQQKLPEKKKKKAKGHPATDLP 878
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP-PPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
211-268 |
2.30e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 39.75 E-value: 2.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 211 IIHGPPGTGKTTTVVEIILQA---VKQGLKVLCCAPSNIAVDNLVERLAlcKQRILRLGHP 268
Cdd:cd17917 5 VIVGETGSGKTTQVPQFLLEDglaKGGKGRIVCTQPRRIAAISVAERVA--EERGEKLGEE 63
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
211-293 |
2.36e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 211 IIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPARLLESIQQhsldavLARSDSA 290
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA------LARKLKP 79
|
...
gi 119392094 291 QIV 293
Cdd:smart00382 80 DVL 82
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
194-266 |
3.08e-03 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350746 [Multi-domain] Cd Length: 180 Bit Score: 39.79 E-value: 3.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119392094 194 TSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIIL-QAVKQGL--KVLCCAPSNIAVDNLVERlaLCKQRILRLG 266
Cdd:cd17988 4 YAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILdHYYKRGKycNIVVTQPRRIAAISIARR--VSQEREWTLG 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
657-863 |
3.20e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 657 QGSSHAATKPQGPATSTRTGSQRQEGGQEAAAPARQGRKKP-------AGKSLASEAP--SQPSLNGGSPEGVESQDG-- 725
Cdd:PHA03247 255 PAPPPVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPDgvwgaalAGAPLALPAPpdPPPPAPAGDAEEEDDEDGam 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 -----VDHFRAMIVEFMASKKMQLEFPPS----LNS---HDRLRVHQIAEEHGLRHDSS--GEGKRRFITVSKRAPRPrA 791
Cdd:PHA03247 335 evvspLPRPRQHYPLGFPKRRRPTWTPPSsledLSAgrhHPKRASLPTRKRRSARHAATpfARGPGGDDQTRPAAPVP-A 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 792 ALGPPAGTGGPAPLQPVPPTPAQTEQPPrEQRGPDQPDLRTLHLERLQRVRSAQGQPASKEQQASGQQKLPE 863
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAEPG-SDDGPAPPPERQPPAPATEPAPDDPDDATRKALDALRERRPPE 484
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
204-275 |
3.26e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 40.15 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQRilrlGHPARLLESI 275
Cdd:NF038214 87 IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRF-----TTAADLVEQLAQARAD----GRLGRLLRRL 149
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
195-256 |
4.12e-03 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350690 [Multi-domain] Cd Length: 189 Bit Score: 39.42 E-value: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 195 SQKEAVLfaLSQKELAIIHGPpGTGKTTTVVEIILQAVKQGlkvlCCAPSNI--------AVDNLVERLA 256
Cdd:cd17932 3 EQREAVT--HPDGPLLVLAGA-GSGKTRVLTHRIAYLILEG----GVPPERIlavtftnkAAKEMRERLR 65
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
196-239 |
7.79e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.90 E-value: 7.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 119392094 196 QKEAVLFALSQKELA--IIHGPPGTGKTTTVVEIILQAVKQGLKVL 239
Cdd:cd00009 6 AIEALREALELPPPKnlLLYGPPGTGKTTLARAIANELFRPGAPFL 51
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
197-267 |
8.61e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350732 [Multi-domain] Cd Length: 174 Bit Score: 38.25 E-value: 8.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094 197 KEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQA--VKQGLKVLCCAPSNIAVDNLVERLAlcKQRILRLGH 267
Cdd:cd17974 7 RDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgyTKGGGKIGCTQPRRVAAMSVAARVA--EEMGVKLGN 77
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
204-260 |
9.33e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 38.99 E-value: 9.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQ 260
Cdd:COG1484 96 IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRF-----TTAPDLVNELKEARA 147
|
|
|