|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
634-860 |
3.34e-153 |
|
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: 469.27 E-value: 3.34e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITTPLSINLPPVLIIGPYGTGKTFTLAQAVKHILKQPESRVLICTHSNSAADLYIKDYLHPYVEAGNP 713
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 714 HARPLRVYFRNRWVKTVHPLVQQYCLISgAHFTFQMPTRQDVERHRVVVVTLSTSQYLCQLDLEPGIFTHILLDEAAQAM 793
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 794 ECETIMPLALAVKSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPSEYPCRILLCENYR 860
Cdd:cd18077 160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
756-1044 |
1.92e-48 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 187.64 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 756 ERHRVVVVTLSTSQYLcqLDLEPGIFTHILLDEAAQAMECETIMPLALAvksTRVVLAGDHMQLSPFV---YSEFARERN 832
Cdd:COG1112 533 ELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARA---KRVVLVGDPKQLPPVVfgeEAEEVAEEG 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 833 LHVSLLDRLYEHYPseyPCRILLCENYRSHEAIINYTSDLFYEGKLMA---SGKQPPHKDFYPLTFFTARGedVQEKNST 909
Cdd:COG1112 608 LDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGG 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 910 AYYNNAEVFEIVERVEEMRKKWPvswgklEEGSIGVVSPYADQVFRIRAELRKKRMSEVSVERVLNV---QGKQFRVLFL 986
Cdd:COG1112 683 SRTNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVIIF 756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 987 STVRTRhtckhkqtaikrkeqlveDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDP 1044
Cdd:COG1112 757 SLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR 797
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
861-1061 |
1.20e-45 |
|
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: 163.17 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 861 SHEAIINYTSDLFYEGKLMAS-------GKQPPHKDFYPLTFFTARGEDVQEKNSTAYYNNAEVFEIVERVEEMRKKWpv 933
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 934 swgkLEEGSIGVVSPYADQVFRIRAELRKKRM--SEVSVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtaikrkeqlved 1011
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGGllEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1012 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSVGRCRKFWETFI 1061
Cdd:cd18808 141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
833-1044 |
5.81e-44 |
|
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: 158.87 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 833 LHVSLLDRLYEHYPSeypCRILLCENYRSHEAIINYTSDLFYEGKLMA-------SGKQPPHKD--FYPLTFF-TARGED 902
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDgpsvaerPLPDDFHLPdpLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 903 VQEKNSTAYYNNAEVFEIVERVEEMRKKWPVswgklEEGSIGVVSPYADQVFRIRAELRKKRM--SEVSVERVLNVQGKQ 980
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPE-----EPSDIGVITPYRAQVRLIRKLLKRKLGgkLEIEVNTVDGFQGRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 981 FRVLFLSTVRtrhtckhkqtaikrkeqlvedSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1044
Cdd:pfam13087 153 KDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
639-826 |
6.05e-15 |
|
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: 76.61 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 639 QKEAIL-AITTPlsinlPPVLIIGPYGTGKTFTLAQAVKHILKQPE------SRVLICTHSNSAAD----LYIKDYLHPY 707
Cdd:pfam13086 2 QREAIRsALSSS-----HFTLIQGPPGTGKTTTIVELIRQLLSYPAtsaaagPRILVCAPSNAAVDnileRLLRKGQKYG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 708 V--------EAGNPHARPLRVYFRNRWVKTVHPLVQQYCLISG-----------------------AHFTFQMPTRQD-- 754
Cdd:pfam13086 77 PkivrighpAAISEAVLPVSLDYLVESKLNNEEDAQIVKDISKeleklakalrafekeiivekllkSRNKDKSKLEQErr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 755 ------------------------VERHRVVVVTLSTS--QYLCQLDLepgiFTHILLDEAAQAMECETIMPLALAVKst 808
Cdd:pfam13086 157 klrserkelrkelrrreqslereiLDEAQIVCSTLSGAgsRLLSSLAN----FDVVIIDEAAQALEPSTLIPLLRGPK-- 230
|
250
....*....|....*...
gi 1207168626 809 RVVLAGDHMQLSPFVYSE 826
Cdd:pfam13086 231 KVVLVGDPKQLPPTVISK 248
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
171-195 |
1.76e-05 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 42.95 E-value: 1.76e-05
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1337-1649 |
1.94e-05 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 49.62 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1337 MAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQtPMHPQASSFPPSfYSGPPMG--PRGLQSPVLEGGEDPmGAGMSEDLKG 1414
Cdd:pfam09606 149 MQPGGQAGGMMQPSSGQPGSGTPNQMGPNGG-PGQGQAGGMNGG-QQGPMGGqmPPQMGVPGMPGPADA-GAQMGQQAQA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1415 VVRGLPAQMHQQPLRLNSFGEESLDSLLGDTLDGQASSGMDALQHQQQArVGQWGEHTPFLPAGVAPFPLPQQLAHLAQP 1494
Cdd:pfam09606 226 NGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGG-AGQGGPGQPMGPPGQQPGAMPNVMSIGDQN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1495 ---GLRIPPQILRAGwGLGPAADEEpRPTMPRYPG-----LLREMLPQDQQYEQRDPAEMPPpqsrllqyrqqIQPRSPG 1566
Cdd:pfam09606 305 nyqQQQTRQQQQQQG-GNHPAAHQQ-QMNQSVGQGgqvvaLGGLNHLETWNPGNFGGLGANP-----------MQRGQPG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1567 DLPSPS--------SSAPNHNFPAPAQPSYPDtsrepPVGFSQAPfPPDHSAGPLPVKYLLQeAHWPHPGHMLGHglpfg 1638
Cdd:pfam09606 372 MMSSPSpvpgqqvrQVTPNQFMRQSPQPSVPS-----PQGPGSQP-PQSHPGGMIPSPALIP-SPSPQMSQQPAQ----- 439
|
330
....*....|.
gi 1207168626 1639 lQAMAQRQDPG 1649
Cdd:pfam09606 440 -QRTIGQDSPG 449
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1473-1835 |
2.15e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1473 PFLPAGVAPFPLPQqlahlAQPGLRIPPQILRAGWGLGPAADEEPRPTMPRYPGLLREMLPqDQQYEQRDPAEMPP-PQS 1551
Cdd:PHA03247 2509 PPAPSRLAPAILPD-----EPVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAP-DRSVPPPRPAPRPSePAV 2582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1552 RLLQYR-----QQIQPRSPGDlpsPSSSAPNhnfPAPAQPSYPDTSREPPVGFSQAPFPPDHSAG-PLPVKYLLQEAHWP 1625
Cdd:PHA03247 2583 TSRARRpdappQSARPRAPVD---DRGDPRG---PAPPSPLPPDTHAPDPPPPSPSPAANEPDPHpPPTVPPPERPRDDP 2656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1626 HPGHMLGHglpfgLQAMAQRQDPGPLQHqqqkqqlqapqsslhsldeyePRGPGRPLYQRRISSSSPQPYPDSLEPQDQP 1705
Cdd:PHA03247 2657 APGRVSRP-----RRARRLGRAAQASSP---------------------PQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1706 VPSYRYPSADLWLGGPGPVPGPAPIHNIPCNGASHIGP---------HREILVSKAMSEEQMKAECLQPPPPPPPHPASA 1776
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 1777 ASLQHHGQFPPLLPSKQTPPDPGGGGNTSPAGHPKPPTMSYASALRAPPKPRPMLPEQS 1835
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849
|
|
| KLF1_2_4_N-like |
cd22056 |
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ... |
1334-1380 |
4.72e-05 |
|
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.
Pssm-ID: 409231 [Multi-domain] Cd Length: 339 Bit Score: 47.73 E-value: 4.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1207168626 1334 NFHMAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQTPMHPQASSFPPS 1380
Cdd:cd22056 260 YQYMNAPYPPHYAHQGAPQFHGQYSVFREPMRVHHQGHPGSMLTPPS 306
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1486-1844 |
5.21e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 48.22 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1486 QQLAHLAQPGLRIPPQIlrAGWGLGPAADEEPRPTMPRYPgllremlpqdqqyEQRDPAEMPPPQSRL-----LQYRQQI 1560
Cdd:pfam03154 170 QPPVLQAQSGAASPPSP--PPPGTTQAATAGPTPSAPSVP-------------PQGSPATSQPPNQTQstaapHTLIQQT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1561 QPRSPGDLPSPSSSAPNHNFPAPAQPSYPDTSREPPVGFSQAPFPPDHSAGPlpvkyllqeAHWPHPGHMLGHGLPfglQ 1640
Cdd:pfam03154 235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGP---------SHMQHPVPPQPFPLT---P 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1641 AMAQRQDPgPLQHQQQKQQLQAPQSSLHSLDEYEPRGPGR--PLyqrrisSSSPQPYPDSLEPQDQPVPSYRYPSADLWL 1718
Cdd:pfam03154 303 QSSQSQVP-PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqPL------PPAPLSMPHIKPPPTTPIPQLPNPQSHKHP 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1719 GGPGPVPGPAPIHNIPCNGA--------SHIGPHREILVSKAMSEEQmkaeclqppppppphpasaaSLQHHGQFPPLLP 1790
Cdd:pfam03154 376 PHLSGPSPFQMNSNLPPPPAlkplsslsTHHPPSAHPPPLQLMPQSQ--------------------QLPPPPAQPPVLT 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 1791 SKQTPPDPGGGGNTSPAGHPKPPTMSYASALRAPPKPRPMLPEQSKKNSDPISL 1844
Cdd:pfam03154 436 QSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAM 489
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
634-696 |
6.57e-05 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 48.01 E-value: 6.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 634 RLNAKQKEAILAITTPLsinlppvLII-GPyGTGKTFTLAQAVKHILKQ---PESRVLICTHSNSAA 696
Cdd:COG0210 6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEggvDPEQILAVTFTNKAA 64
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1336-1713 |
3.99e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1336 HMAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQTPMHPQASSFP--------PSFYSGPPMGPR--GLQSPV--LEGGEDP 1403
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgrAAQASSPPQRPRrrAARPTVgsLTSLADP 2701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1404 MGAGMSEDLK--GVVRGLPAQMHQQPLRlNSFGEESLDSLLGDTLDGQASSGMDALQHQQQARVGQWGEHTPFLPAGVAP 1481
Cdd:PHA03247 2702 PPPPPTPEPAphALVSATPLPPGPAAAR-QASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1482 FPLPQQLAHLAQPGLRIPPqilragwgLGPAADEEPRPTMPRYPGLLREMLPQdqqyeqrdpAEMPPPQSRLLQYRQQIQ 1561
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLP--------SPWDPADPPAAVLAPAAALPPAASPA---------GPLPPPTSAQPTAPPPPP 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1562 PRSPGDLPSPSSSAPNHNF----PAPAQPSYPDTSREPPVG-FSQAPFPPDHSAGPLPVkylLQEAHWPHPGhmlghglp 1636
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPAAPARPPVRrLARPAVSRSTESFALPP---DQPERPPQPQ-------- 2912
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 1637 fgLQAMAQRQDPGPLQHQQQKQQLQAPQSSLHSLDEYEPRGPGRPlyqrriSSSSPQPYPDSLEPQDQPVPSYRYPS 1713
Cdd:PHA03247 2913 --APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP------SGAVPQPWLGALVPGRVAVPRFRVPQ 2981
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
656-734 |
1.47e-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: 41.20 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 656 PVLIIGPYGTGKTfTLAQAVKHILKQPESRVLICTHSNSAADLYIKDYLHPYVEAGNPHARPLRVYFRNRWVKTVHPLV 734
Cdd:smart00382 4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
634-860 |
3.34e-153 |
|
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: 469.27 E-value: 3.34e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITTPLSINLPPVLIIGPYGTGKTFTLAQAVKHILKQPESRVLICTHSNSAADLYIKDYLHPYVEAGNP 713
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 714 HARPLRVYFRNRWVKTVHPLVQQYCLISgAHFTFQMPTRQDVERHRVVVVTLSTSQYLCQLDLEPGIFTHILLDEAAQAM 793
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 794 ECETIMPLALAVKSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPSEYPCRILLCENYR 860
Cdd:cd18077 160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
634-860 |
4.23e-86 |
|
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: 281.04 E-value: 4.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITTPLSiNLPPVLIIGPYGTGKTFTLAQAVKHILKQ-PESRVLICTHSNSAADLYIKDYLHPYVEAgn 712
Cdd:cd18038 1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLRQpPEARILVCAPSNSAADLLAERLLNALVTK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 713 phARPLRVYFRNRWVKTVHPLVQQYCLISgAHFTFQMPTRQDVERHRVVVVTLSTSQYLCQLDLEPGIFTHILLDEAAQA 792
Cdd:cd18038 78 --REILRLNAPSRDRASVPPELLPYCNSK-AEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168626 793 MECETIMPLA-LAVKSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPSEY------PCRILLCENYR 860
Cdd:cd18038 155 TEPEALIPLSeLASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKdgeynpSYITKLLKNYR 229
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
634-860 |
2.36e-69 |
|
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: 232.86 E-value: 2.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAIT--TPLSINLPPVLIIGPYGTGKTFTLAQAVKHILKQPESRVLICTHSNSAADLYIKDYLHPYVEAG 711
Cdd:cd18076 1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 712 NPHARPLRVYFRNRWVKTVHPLVQQYCLISGAHFTFQMPTRQDVERHRVVVVTLSTSQylcQLDLEPGIFTHILLDEAAQ 791
Cdd:cd18076 81 HPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAAQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 792 AMECETIMPLALAVKSTRVVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPSE-----YPCRILLCENYR 860
Cdd:cd18076 158 MLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
756-1044 |
1.92e-48 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 187.64 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 756 ERHRVVVVTLSTSQYLcqLDLEPGIFTHILLDEAAQAMECETIMPLALAvksTRVVLAGDHMQLSPFV---YSEFARERN 832
Cdd:COG1112 533 ELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARA---KRVVLVGDPKQLPPVVfgeEAEEVAEEG 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 833 LHVSLLDRLYEHYPseyPCRILLCENYRSHEAIINYTSDLFYEGKLMA---SGKQPPHKDFYPLTFFTARGedVQEKNST 909
Cdd:COG1112 608 LDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGG 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 910 AYYNNAEVFEIVERVEEMRKKWPvswgklEEGSIGVVSPYADQVFRIRAELRKKRMSEVSVERVLNV---QGKQFRVLFL 986
Cdd:COG1112 683 SRTNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVIIF 756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 987 STVRTRhtckhkqtaikrkeqlveDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDP 1044
Cdd:COG1112 757 SLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR 797
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
861-1061 |
1.20e-45 |
|
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: 163.17 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 861 SHEAIINYTSDLFYEGKLMAS-------GKQPPHKDFYPLTFFTARGEDVQEKNSTAYYNNAEVFEIVERVEEMRKKWpv 933
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 934 swgkLEEGSIGVVSPYADQVFRIRAELRKKRM--SEVSVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtaikrkeqlved 1011
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGGllEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1012 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSVGRCRKFWETFI 1061
Cdd:cd18808 141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
833-1044 |
5.81e-44 |
|
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: 158.87 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 833 LHVSLLDRLYEHYPSeypCRILLCENYRSHEAIINYTSDLFYEGKLMA-------SGKQPPHKD--FYPLTFF-TARGED 902
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDgpsvaerPLPDDFHLPdpLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 903 VQEKNSTAYYNNAEVFEIVERVEEMRKKWPVswgklEEGSIGVVSPYADQVFRIRAELRKKRM--SEVSVERVLNVQGKQ 980
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPE-----EPSDIGVITPYRAQVRLIRKLLKRKLGgkLEIEVNTVDGFQGRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 981 FRVLFLSTVRtrhtckhkqtaikrkeqlvedSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1044
Cdd:pfam13087 153 KDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
635-860 |
6.47e-37 |
|
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: 139.81 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 635 LNAKQKEAILAITTPLSINLPPVlIIGPYGTGKTFTLAQAVKHILKQ-PESRVLICTHSNSAADLYIKDyLHPYVEAGNP 713
Cdd:cd18078 2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEAILQVVYNlPRSRILVCAPSNSAADLVTSR-LHESKVLKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 714 HARPLRVYfrNRWVKTVHPLVQQYCLISgahftfqmPTRQDVERHRVVVVTLSTSQYLCQLDLEPGIFTHILLDEAAQAM 793
Cdd:cd18078 80 DMVRLNAV--NRFESTVIDARKLYCRLG--------EDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 794 ECETIMPLAL-AVKSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPSEYP-CRIL-------LCENY 859
Cdd:cd18078 150 EPESLIPLGLiSSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLVDNY 229
|
.
gi 1207168626 860 R 860
Cdd:cd18078 230 R 230
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
634-847 |
4.29e-27 |
|
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: 110.40 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITTPLSInlppVLIIGPYGTGKTFTLAQAVKHILKQPESrVLICTHSNSAAD---LYIKDYLHPYVEA 710
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVRILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 711 GNPHarplrvyfrnrwvkTVHPLVQQYCLISGAHFTFQMPTRQDV-ERHRVVVVT-LSTSQYLcqldLEPGIFTHILLDE 788
Cdd:cd18041 76 GRLK--------------KIHPDVQEFTLEAILKSCKSVEELESKyESVSVVATTcLGINHPI----FRRRTFDYCIVDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 789 AAQAMECETIMPLALAvksTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPS 847
Cdd:cd18041 138 ASQITLPICLGPLRLA---KKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPD 193
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
634-860 |
2.83e-26 |
|
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: 107.70 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILaittpLSINLPPVLII-GPYGTGKTFTLAQAVKHILKQpESRVLICTHSNSAADLYIKDYLH---PYVE 709
Cdd:cd18044 1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAVKR-GEKVLACAPSNIAVDNLVERLVAlkvKVVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 710 AGNPhARplrvyfrnrwvktVHPLVQQYCLisGAHFtfqmptrqdveRHRVVVVTLSTSqylCQLDLEPGI-FTHILLDE 788
Cdd:cd18044 75 IGHP-AR-------------LLESVLDHSL--DALV-----------AAQVVLATNTGA---GSRQLLPNElFDVVVIDE 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168626 789 AAQAMECETIMPLalaVKSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPSEypCRILLCENYR 860
Cdd:cd18044 125 AAQALEASCWIPL---LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
635-841 |
5.37e-24 |
|
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: 102.71 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 635 LNAKQKEAI-LAITTPLSinlppvLIIGPYGTGKTFTLAQAVKHILKQPESRVLICTHSNSAADlYIKDYLHpyveagNP 713
Cdd:cd18039 2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH------QT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 714 HARPLRVYFRNRW-----VK--TVHPLVQQYCLISGAHFTFQMP------TRQDVERHR---------------VVVVTL 765
Cdd:cd18039 69 GLKVVRLCAKSREavespVSflALHNQVRNLDSAEKLELLKLLKletgelSSADEKRYRklkrkaerellrnadVICCTC 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168626 766 STSqylcqLD--LEPGIFTHILLDEAAQAMECETIMPLALAVKstRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 841
Cdd:cd18039 149 VGA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
635-860 |
2.55e-19 |
|
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: 88.42 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 635 LNAKQKEAILAIttpLSINLPPVLIIGPYGTGKTFTLAQAVKHIL------------------------KQPESRVLICT 690
Cdd:cd18042 1 LNESQLEAIASA---LQNSPGITLIQGPPGTGKTKTIVGILSVLLagkyrkyyekvkkklrklqrnlnnKKKKNRILVCA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 691 HSNSAAD---LYIKDylhpyveaGNPHARPLRVYFRNrwvktvhplvqqyCLISGahftfqmptRQDVERH-----RVVV 762
Cdd:cd18042 78 PSNAAVDeivLRLLS--------EGFLDGDGRSYKPN-------------VVRVG---------RQELRASilneaDIVC 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 763 VTLSTSQYLcQLDLEPGIFTHILLDEAAQAMECETIMPLALAVKstRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLY 842
Cdd:cd18042 128 TTLSSSGSD-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQ 204
|
250
....*....|....*...
gi 1207168626 843 EHypsEYPCrILLCENYR 860
Cdd:cd18042 205 LA---GYPV-LMLTTQYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
639-826 |
6.05e-15 |
|
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: 76.61 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 639 QKEAIL-AITTPlsinlPPVLIIGPYGTGKTFTLAQAVKHILKQPE------SRVLICTHSNSAAD----LYIKDYLHPY 707
Cdd:pfam13086 2 QREAIRsALSSS-----HFTLIQGPPGTGKTTTIVELIRQLLSYPAtsaaagPRILVCAPSNAAVDnileRLLRKGQKYG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 708 V--------EAGNPHARPLRVYFRNRWVKTVHPLVQQYCLISG-----------------------AHFTFQMPTRQD-- 754
Cdd:pfam13086 77 PkivrighpAAISEAVLPVSLDYLVESKLNNEEDAQIVKDISKeleklakalrafekeiivekllkSRNKDKSKLEQErr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 755 ------------------------VERHRVVVVTLSTS--QYLCQLDLepgiFTHILLDEAAQAMECETIMPLALAVKst 808
Cdd:pfam13086 157 klrserkelrkelrrreqslereiLDEAQIVCSTLSGAgsRLLSSLAN----FDVVIIDEAAQALEPSTLIPLLRGPK-- 230
|
250
....*....|....*...
gi 1207168626 809 RVVLAGDHMQLSPFVYSE 826
Cdd:pfam13086 231 KVVLVGDPKQLPPTVISK 248
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
634-841 |
2.30e-14 |
|
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: 72.96 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAI-LAITTPLSInlppvlIIGPYGTGKTFTLAQAVKHIL----KQPESRVLICTHSNSAADLYIKDYLhpyv 708
Cdd:cd17936 1 TLDPSQLEALkHALTSELAL------IQGPPGTGKTFLGVKLVRALLqnqdLSITGPILVVCYTNHALDQFLEGLL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 709 EAGNPHArpLRVyfrnrwvktvhplvqqyclisGAhftfqmptrqdverhRVVVVTLSTSQYLCQL--DLEPGIfthILL 786
Cdd:cd17936 71 DFGPTKI--VRL---------------------GA---------------RVIGMTTTGAAKYRELlqALGPKV---VIV 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 787 DEAAQAMECETIMplALAVKSTRVVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 841
Cdd:cd17936 110 EEAAEVLEAHILA--ALTPSTEHLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERL 164
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
657-860 |
9.73e-14 |
|
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: 69.57 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 657 VLIIGPYGTGKTFTLAQAVKHILKQ-PESRVLICTHSNSAADlyikdylhpyveagnpharplrvyfrnrwvktvhplvq 735
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGlRGKRVLVTAQSNVAVD-------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 736 qyclisgahftfqmptrqdverhrvvvvtlstsqylcQLDlepgiftHILLDEAAQAMECETIMPLALAvksTRVVLAGD 815
Cdd:cd17934 44 -------------------------------------NVD-------VVIIDEASQITEPELLIALIRA---KKVVLVGD 76
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207168626 816 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPsEYPcRILLCENYR 860
Cdd:cd17934 77 PKQLPPVVQEDHAALlgLSFILSLLLLFRLLLP-GSP-KVMLDTQYR 121
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
634-841 |
4.38e-12 |
|
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: 67.07 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITTP-LSinlppvLIIGPYGTGKTFTLAQAVKHILKQ-PESRVLICTHSNSAA-DLYIKdylhpyVEA 710
Cdd:cd17935 5 KFTPTQIEAIRSGMQPgLT------MVVGPPGTGKTDVAVQIISNLYHNfPNQRTLIVTHSNQALnQLFEK------IMA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 711 gnpharpLRVYFRnrwvktvHPLVqqycLISGAHFTFQMPTRQDVERHRvvvvtlstsqyLCQLDLEpgiFTHILLDEAA 790
Cdd:cd17935 73 -------LDIDER-------HLLR----LGHGAKIIAMTCTHAALKRGE-----------LVELGFK---YDNILMEEAA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168626 791 QAMECETIMPLALAV------KSTRVVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 841
Cdd:cd17935 121 QILEIETFIPLLLQNpedgpnRLKRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
635-843 |
4.38e-12 |
|
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: 68.71 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 635 LNAKQKEAIL-AITTPLSinlppvLIIGPYGTGKTFTLAQAVKHILKQPESR------------VLICTHSNSAAD---- 697
Cdd:cd18040 2 LNPSQNHAVRtALTKPFT------LIQGPPGTGKTVTGVHIAYWFAKQNREIqsvsgegdggpcVLYCGPSNKSVDvvae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 698 ------------LYIK-----DY---------------------------LHPYV-EAGNPHARPLRVyFRNRWVKTVHP 732
Cdd:cd18040 76 lllkvpglkilrVYSEqiettEYpipneprhpnkksereskpnselssitLHHRIrQPSNPHSQQIKA-FEARFERTQEK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 733 L----VQQYC-LISGAHFtfqmptrQDVERHRVVVVTLS--TSQYLCqldlEPGIFTHILLDEAAQAMECETIMPLALAV 805
Cdd:cd18040 155 IteedIKTYKiLIWEARF-------EELETVDVILCTCSeaASQKMR----THANVKQCIVDECGMCTEPESLIPIVSAP 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 1207168626 806 KSTRVVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYE 843
Cdd:cd18040 224 RAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
574-1044 |
2.39e-09 |
|
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: 61.92 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 574 LVADQELQVELQFQLNRLPLCEMHYALDRVRDNSILFPDISLTPTIPWspnrqWDEQLDPRLNAKQKEAILAITTPLSIn 653
Cdd:COG0507 69 LVESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAA-----LEPRAGITLSDEQREAVALALTTRRV- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 654 lppVLIIGPYGTGKTFTLAQAVKHILKQPEsRVLICTHSNSAAD-LYikdylhpyvEAGNPHARplrvyfrnrwvkTVHP 732
Cdd:COG0507 143 ---SVLTGGAGTGKTTTLRALLAALEALGL-RVALAAPTGKAAKrLS---------ESTGIEAR------------TIHR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 733 LVQqyclISGAHFTFQMPTRQDVERHRVVVVtlstsqylcqldlepgifthillDEA--------AQAMEcetimplALA 804
Cdd:COG0507 198 LLG----LRPDSGRFRHNRDNPLTPADLLVV-----------------------DEAsmvdtrlmAALLE-------ALP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 805 VKSTRVVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypseypcrillcENYRSHEAI-INYTSDLFYEGKlM 879
Cdd:COG0507 244 RAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT-----------------EVYRQADDSrIIELAHAIREGD-A 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 880 ASGKQPPHKDFYplTFFTARGEDVQEKNSTAYYN--------------NAEVFEIVERVEEMRKKWPVSWGKLEE----- 940
Cdd:COG0507 306 PEALNARYADVV--FVEAEDAEEAAEAIVELYADrpaggediqvlaptNAGVDALNQAIREALNPAGELERELAEdgele 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 941 --------------------GSIGVVSPYADQVFRIRAELRKKRMSEVSVERVLNV-----------QGKQF-RVLFLST 988
Cdd:COG0507 384 lyvgdrvmftrndydlgvfnGDIGTVLSIDEDEGRLTVRFDGREIVTYDPSELDQLelayaitvhksQGSTFdRVILVLP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207168626 989 vrtrhtckhkqtaikrkeqlvedsteDLDYGFLSNyKLLNTAITRAQSLVAVVGDP 1044
Cdd:COG0507 464 --------------------------SEHSPLLSR-ELLYTALTRARELLTLVGDR 492
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
636-824 |
5.60e-08 |
|
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: 53.36 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 636 NAKQKEAILAIttplsINLPPVLIIGPYGTGKTFTLAQAVKHILKQPEsRVLICTHSNSAadlyikdylhpyveagnpha 715
Cdd:cd18043 1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAA-------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 716 rpLRVYFRNRWVktvhplvqqyclisgahftfqMPTrqdverhrvvvvtLSTSQYLcqlDLEPGIFTHILLDEAAQAMEC 795
Cdd:cd18043 55 --LDVVRFPCWI---------------------MSP-------------LSVSQYL---PLNRNLFDLVIFDEASQIPIE 95
|
170 180
....*....|....*....|....*....
gi 1207168626 796 ETImPLALAVKstRVVLAGDHMQLSPFVY 824
Cdd:cd18043 96 EAL-PALFRGK--QVVVVGDDKQLPPSIL 121
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
636-859 |
3.92e-07 |
|
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: 52.13 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 636 NAKQKEAILAITTPLsinlppvLII-GPyGTGKTFTLAQAVKHILKQ---PESRVLICTHSNSAADlYIKDYLHPYVeaG 711
Cdd:cd17932 1 NPEQREAVTHPDGPL-------LVLaGA-GSGKTRVLTHRIAYLILEggvPPERILAVTFTNKAAK-EMRERLRKLL--G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 712 NPHARPLrvyfrnrWVKTVHPLvqqyCL-ISGAHFTFqmptrQDVERHrvVVVTLSTSQYLCQLDLEPgiFTHILLDEA- 789
Cdd:cd17932 70 EQLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLLLY--ALELLEENPDVREKLQSR--FRYILVDEYq 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 790 ----AQamecETIMpLALAVKSTRVVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPSeyPCRILLCENY 859
Cdd:cd17932 130 dtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
656-697 |
3.41e-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: 47.87 E-value: 3.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207168626 656 PVLIIGPYGTGKTFTLAQAVKHILKQ---PESRVLICTHSNSAAD 697
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
171-195 |
1.76e-05 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 42.95 E-value: 1.76e-05
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1337-1649 |
1.94e-05 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 49.62 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1337 MAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQtPMHPQASSFPPSfYSGPPMG--PRGLQSPVLEGGEDPmGAGMSEDLKG 1414
Cdd:pfam09606 149 MQPGGQAGGMMQPSSGQPGSGTPNQMGPNGG-PGQGQAGGMNGG-QQGPMGGqmPPQMGVPGMPGPADA-GAQMGQQAQA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1415 VVRGLPAQMHQQPLRLNSFGEESLDSLLGDTLDGQASSGMDALQHQQQArVGQWGEHTPFLPAGVAPFPLPQQLAHLAQP 1494
Cdd:pfam09606 226 NGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGG-AGQGGPGQPMGPPGQQPGAMPNVMSIGDQN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1495 ---GLRIPPQILRAGwGLGPAADEEpRPTMPRYPG-----LLREMLPQDQQYEQRDPAEMPPpqsrllqyrqqIQPRSPG 1566
Cdd:pfam09606 305 nyqQQQTRQQQQQQG-GNHPAAHQQ-QMNQSVGQGgqvvaLGGLNHLETWNPGNFGGLGANP-----------MQRGQPG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1567 DLPSPS--------SSAPNHNFPAPAQPSYPDtsrepPVGFSQAPfPPDHSAGPLPVKYLLQeAHWPHPGHMLGHglpfg 1638
Cdd:pfam09606 372 MMSSPSpvpgqqvrQVTPNQFMRQSPQPSVPS-----PQGPGSQP-PQSHPGGMIPSPALIP-SPSPQMSQQPAQ----- 439
|
330
....*....|.
gi 1207168626 1639 lQAMAQRQDPG 1649
Cdd:pfam09606 440 -QRTIGQDSPG 449
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1473-1835 |
2.15e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1473 PFLPAGVAPFPLPQqlahlAQPGLRIPPQILRAGWGLGPAADEEPRPTMPRYPGLLREMLPqDQQYEQRDPAEMPP-PQS 1551
Cdd:PHA03247 2509 PPAPSRLAPAILPD-----EPVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAP-DRSVPPPRPAPRPSePAV 2582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1552 RLLQYR-----QQIQPRSPGDlpsPSSSAPNhnfPAPAQPSYPDTSREPPVGFSQAPFPPDHSAG-PLPVKYLLQEAHWP 1625
Cdd:PHA03247 2583 TSRARRpdappQSARPRAPVD---DRGDPRG---PAPPSPLPPDTHAPDPPPPSPSPAANEPDPHpPPTVPPPERPRDDP 2656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1626 HPGHMLGHglpfgLQAMAQRQDPGPLQHqqqkqqlqapqsslhsldeyePRGPGRPLYQRRISSSSPQPYPDSLEPQDQP 1705
Cdd:PHA03247 2657 APGRVSRP-----RRARRLGRAAQASSP---------------------PQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1706 VPSYRYPSADLWLGGPGPVPGPAPIHNIPCNGASHIGP---------HREILVSKAMSEEQMKAECLQPPPPPPPHPASA 1776
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 1777 ASLQHHGQFPPLLPSKQTPPDPGGGGNTSPAGHPKPPTMSYASALRAPPKPRPMLPEQS 1835
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
638-821 |
2.67e-05 |
|
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: 46.01 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 638 KQKEAILAITT-PLSInlppvlIIGPYGTGKTFTLAQAVKhILKQPESRVLICTHSNSAADLyikdyLHpyvEAGNPHAR 716
Cdd:cd17933 1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAKR-----LS---ESTGIEAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 717 plrvyfrnrwvkTVHPLvqqycLISGAHFTFQMPTRQDVERHRVVVVtlstsqylcqldlepgifthillDEAAqamece 796
Cdd:cd17933 66 ------------TIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEAS------ 99
|
170 180 190
....*....|....*....|....*....|...
gi 1207168626 797 tiM---PLALAV-----KSTRVVLAGDHMQLSP 821
Cdd:cd17933 100 --MvdtRLMAALlsaipAGARLILVGDPDQLPS 130
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
635-697 |
3.78e-05 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 47.63 E-value: 3.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 635 LNAKQKEAILAITTPLsinlppvLIIGPYGTGKTFTLAQAVKHILKQ----PESrVLICTHSNSAAD 697
Cdd:pfam00580 1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEggidPEE-ILAVTFTNKAAR 59
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
634-821 |
4.68e-05 |
|
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: 46.02 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 634 RLNAKQKEAILAITT-PLSInlppVLIIGPYGTGKTFTLAQAVKHILKQPEsRVLICTHSNSAADLYIKDYLHPyveagn 712
Cdd:pfam13604 1 TLNAEQAAAVRALLTsGDRV----AVLVGPAGTGKTTALKALREAWEAAGY-RVIGLAPTGRAAKVLGEELGIP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 713 phARplrvyfrnrwvkTVHplvqqyclisgaHFTFQMPTRQDVERHRVVVV----TLSTSQylcqldlepgifTHILLDE 788
Cdd:pfam13604 70 --AD------------TIA------------KLLHRLGGRAGLDPGTLLIVdeagMVGTRQ------------MARLLKL 111
|
170 180 190
....*....|....*....|....*....|...
gi 1207168626 789 AAQAmecetimplalavkSTRVVLAGDHMQLSP 821
Cdd:pfam13604 112 AEDA--------------GARVILVGDPRQLPS 130
|
|
| KLF1_2_4_N-like |
cd22056 |
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ... |
1334-1380 |
4.72e-05 |
|
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.
Pssm-ID: 409231 [Multi-domain] Cd Length: 339 Bit Score: 47.73 E-value: 4.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1207168626 1334 NFHMAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQTPMHPQASSFPPS 1380
Cdd:cd22056 260 YQYMNAPYPPHYAHQGAPQFHGQYSVFREPMRVHHQGHPGSMLTPPS 306
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1486-1844 |
5.21e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 48.22 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1486 QQLAHLAQPGLRIPPQIlrAGWGLGPAADEEPRPTMPRYPgllremlpqdqqyEQRDPAEMPPPQSRL-----LQYRQQI 1560
Cdd:pfam03154 170 QPPVLQAQSGAASPPSP--PPPGTTQAATAGPTPSAPSVP-------------PQGSPATSQPPNQTQstaapHTLIQQT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1561 QPRSPGDLPSPSSSAPNHNFPAPAQPSYPDTSREPPVGFSQAPFPPDHSAGPlpvkyllqeAHWPHPGHMLGHGLPfglQ 1640
Cdd:pfam03154 235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGP---------SHMQHPVPPQPFPLT---P 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1641 AMAQRQDPgPLQHQQQKQQLQAPQSSLHSLDEYEPRGPGR--PLyqrrisSSSPQPYPDSLEPQDQPVPSYRYPSADLWL 1718
Cdd:pfam03154 303 QSSQSQVP-PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqPL------PPAPLSMPHIKPPPTTPIPQLPNPQSHKHP 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1719 GGPGPVPGPAPIHNIPCNGA--------SHIGPHREILVSKAMSEEQmkaeclqppppppphpasaaSLQHHGQFPPLLP 1790
Cdd:pfam03154 376 PHLSGPSPFQMNSNLPPPPAlkplsslsTHHPPSAHPPPLQLMPQSQ--------------------QLPPPPAQPPVLT 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 1791 SKQTPPDPGGGGNTSPAGHPKPPTMSYASALRAPPKPRPMLPEQSKKNSDPISL 1844
Cdd:pfam03154 436 QSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAM 489
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
634-696 |
6.57e-05 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 48.01 E-value: 6.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 634 RLNAKQKEAILAITTPLsinlppvLII-GPyGTGKTFTLAQAVKHILKQ---PESRVLICTHSNSAA 696
Cdd:COG0210 6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEggvDPEQILAVTFTNKAA 64
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
635-711 |
1.18e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 635 LNAKQKEAILAITTPLSINLPPVLIIGPYGTGKTFTLAQAVKHILKQ-PESRVLICTHSNsaaDLY------IKDYLHPY 707
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKgPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
|
....
gi 1207168626 708 VEAG 711
Cdd:pfam04851 81 VEIG 84
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
588-722 |
1.70e-04 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 46.56 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 588 LNRLPLCEMHYALDRVRDNSILFPDISLTPTIPWSPNRQWDE-----QLDPRLNAKQKEAILAITTPLSINLPPVLIIGP 662
Cdd:COG1061 29 SLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAgdeasGTSFELRPYQQEALEALLAALERGGGRGLVVAP 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168626 663 YGTGKTFTLAQAVKHILKQPesRVLICTHS----NSAADLyIKDYLHPYVEAGNPHARPLRVYF 722
Cdd:COG1061 109 TGTGKTVLALALAAELLRGK--RVLVLVPRrellEQWAEE-LRRFLGDPLAGGGKKDSDAPITV 169
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1469-1841 |
2.14e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1469 GEHTPFLPAgVAPFPLPQQLAHLAQPGLRiPPqilragwglGPAA-------DEEPRPTMPRYPGLLREMLPQDQQYEQR 1541
Cdd:PHA03247 2549 GDPPPPLPP-AAPPAAPDRSVPPPRPAPR-PS---------EPAVtsrarrpDAPPQSARPRAPVDDRGDPRGPAPPSPL 2617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1542 DPAEMPPPQSRLLQYRQQIQPRSPGDLPSPSSSAPNhNFPAPAQPSYPDTSREP--PVGFSQAPFPPDHSAGPLPVKYLL 1619
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRLgrAAQASSPPQRPRRRAARPTVGSLT 2696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1620 QEAHWPHPG-------HMLGHGLPFGLQAMAQRQDPGPLQHQQQKQQLQAPQSSLHSldeyePRGPGRPLYQRRISSSSP 1692
Cdd:PHA03247 2697 SLADPPPPPptpepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----PARPARPPTTAGPPAPAP 2771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1693 QPYPDSLEPQDQPVPSYRYPSADLwlggpgpvpgpapihnipcngASHIGPHREILVSKAMSEEQMKAECLQPPPPPPPH 1772
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESR---------------------ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 1773 PASAAslqhhgQFPPLLPSKQTPPDPGGGGNTSPAG--HPKPPTMSYASALRAPPKP------RPMLPEQSKKNSDP 1841
Cdd:PHA03247 2831 PTSAQ------PTAPPPPPGPPPPSLPLGGSVAPGGdvRRRPPSRSPAAKPAAPARPpvrrlaRPAVSRSTESFALP 2901
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1336-1713 |
3.99e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1336 HMAPPHPAFPSHHGTSQFPQQYGLSRPPLRMQTPMHPQASSFP--------PSFYSGPPMGPR--GLQSPV--LEGGEDP 1403
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgrAAQASSPPQRPRrrAARPTVgsLTSLADP 2701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1404 MGAGMSEDLK--GVVRGLPAQMHQQPLRlNSFGEESLDSLLGDTLDGQASSGMDALQHQQQARVGQWGEHTPFLPAGVAP 1481
Cdd:PHA03247 2702 PPPPPTPEPAphALVSATPLPPGPAAAR-QASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1482 FPLPQQLAHLAQPGLRIPPqilragwgLGPAADEEPRPTMPRYPGLLREMLPQdqqyeqrdpAEMPPPQSRLLQYRQQIQ 1561
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLP--------SPWDPADPPAAVLAPAAALPPAASPA---------GPLPPPTSAQPTAPPPPP 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1562 PRSPGDLPSPSSSAPNHNF----PAPAQPSYPDTSREPPVG-FSQAPFPPDHSAGPLPVkylLQEAHWPHPGhmlghglp 1636
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPAAPARPPVRrLARPAVSRSTESFALPP---DQPERPPQPQ-------- 2912
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 1637 fgLQAMAQRQDPGPLQHQQQKQQLQAPQSSLHSLDEYEPRGPGRPlyqrriSSSSPQPYPDSLEPQDQPVPSYRYPS 1713
Cdd:PHA03247 2913 --APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP------SGAVPQPWLGALVPGRVAVPRFRVPQ 2981
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1357-1636 |
6.93e-04 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 44.66 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1357 YGLSRPPLRMQTPMHPQASSFPPSfySGPPMGPRglQSPVLEGGEDPMgagmsEDLKGVVRGLPAQMHQQPLRlnsfgee 1436
Cdd:PHA03379 413 YGTPRPPVEKPRPEVPQSLETATS--HGSAQVPE--PPPVHDLEPGPL-----HDQHSMAPCPVAQLPPGPLQ------- 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1437 slDSLLGDTLDGQASSGMDA---LQHQQQARVGQWgEHTPFLPAGVAPFP-LPQQLA---------HLAQPGLRIPPQIL 1503
Cdd:PHA03379 477 --DLEPGDQLPGVVQDGRPAcapVPAPAGPIVRPW-EASLSQVPGVAFAPvMPQPMPvepvpvptvALERPVCPAPPLIA 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1504 RAG-------------WGLGPAADEEPRPT--MPRYPGLLReMLPQDQQYEQrdPAEMPPPQ----------SRLLQYRQ 1558
Cdd:PHA03379 554 MQGpgetsgivrvrerWRPAPWTPNPPRSPsqMSVRDRLAR-LRAEAQPYQA--SVEVQPPQltqvspqqpmEYPLEPEQ 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1559 QIQPRSPGDLPSPSSSAPnhNFPApAQPSYPDTSREPPVGFSQAPFPPDHSAGPLPVKYLLQEAHWPHP-------GHML 1631
Cdd:PHA03379 631 QMFPGSPFSQVADVMRAG--GVPA-MQPQYFDLPLQQPISQGAPLAPLRASMGPVPPVPATQPQYFDIPltepinqGASA 707
|
....*
gi 1207168626 1632 GHGLP 1636
Cdd:PHA03379 708 AHFLP 712
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1471-1839 |
9.54e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1471 HTPFLPAGVAPFPLPQQLAHLAQPGLRIPPQILRAGWGLGPAADEEPRPTMPrypgllremLPQDQQYEQrdpAEMPPPQ 1550
Cdd:pfam03154 246 HPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP---------FPLTPQSSQ---SQVPPGP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1551 SRLLQYRQQIQPRSPGDLPSPSSSAPNHNFPAPAQP-SYPDTSREPPVGFSQAPFPPDHSagplpvkyllqeahwpHPGH 1629
Cdd:pfam03154 314 SPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPlSMPHIKPPPTTPIPQLPNPQSHK----------------HPPH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1630 MLGHGlPFglqAMAQRQDPGPlqhqqqkqqlqaPQSSLHSLDEYEPrgpgrplyqrrissSSPQPYPDSLEPQDQPVPSY 1709
Cdd:pfam03154 378 LSGPS-PF---QMNSNLPPPP------------ALKPLSSLSTHHP--------------PSAHPPPLQLMPQSQQLPPP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1710 ryPSADLWLGGPGPVPGPAPIHniPCNGASHIGPHREilvskAMSEEQMKAECLQPPPPPPPHPASAASLQHHGQFPPLL 1789
Cdd:pfam03154 428 --PAQPPVLTQSQSLPPPAASH--PPTSGLHQVPSQS-----PFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1207168626 1790 PSKQTPPDPGGGGNTSPAGHPKPPTMSYASALRAPPKP-RPMLPEQSKKNS 1839
Cdd:pfam03154 499 SVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPpRSPSPEPTVVNT 549
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1477-1628 |
1.35e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 43.66 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1477 AGVAPFPLPQQLAHlAQPGLRIPPQILRAGWGlGPAADEEPrPTMPRYPGL--LREMLPQDQQyeQRDPAEMPPPQSRLL 1554
Cdd:PRK14086 92 AGEPAPPPPHARRT-SEPELPRPGRRPYEGYG-GPRADDRP-PGLPRQDQLptARPAYPAYQQ--RPEPGAWPRAADDYG 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 1555 QYRQQIQPRSPGDLPSPSSSAPNHNF---PAPAQPSYPDTSREPPVGFSQAPFPPDHSAGPLPvkyllqeahWPHPG 1628
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERdrePYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRP---------EPPPG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
656-734 |
1.47e-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: 41.20 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168626 656 PVLIIGPYGTGKTfTLAQAVKHILKQPESRVLICTHSNSAADLYIKDYLHPYVEAGNPHARPLRVYFRNRWVKTVHPLV 734
Cdd:smart00382 4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
749-1041 |
1.64e-03 |
|
helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409652 [Multi-domain] Cd Length: 341 Bit Score: 42.90 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 749 MPTRQDVERHRVVVVTLSTSQYL-CQLDLEPGIFTHILL-DEAAQAMECEtIMPLALAVKSTRVVLAGDHMQL-SPFVYS 825
Cdd:cd21718 84 VPQRARVECFDGFKVNNTNAQYIfSTINALPECSADIVVvDEVSMCTNYD-LSVVNARLKYKHIVYVGDPAQLpAPRTLL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 826 EFARERNLHVSLLDRLYEHYPseyPCrILLCENYRSHEAIINYTSDLFYEGKLMAsgkqppHKDFYPLTFFTARGEDVQE 905
Cdd:cd21718 163 TEGSLEPKDYNVVTRLMVGSG---PD-VFLSKCYRCPKEIVDTVSKLVYDNKLKA------IKPKSRQCFKTFGKGDVRH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 906 KNSTAYynNAEVFEIVERVEEMRKKWpvswgkleeGSIGVVSPYADQvfriraELRKKRMSEVSVERVLNVQGKQF-RVL 984
Cdd:cd21718 233 DNGSAI--NRPQLEFVKRFLDRNPRW---------RKAVFISPYNAM------NNRASRLLGLSTQTVDSSQGSEYdYVI 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168626 985 FLSTVRTRHTCkhkqtaikrkeqlvedstedldygflsNYKLLNTAITRAQSLVAVV 1041
Cdd:cd21718 296 FCQTTDTAHAL---------------------------NINRFNVAITRAKHGILVI 325
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
639-697 |
1.67e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 40.66 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207168626 639 QKEAILAITTPlsinlPPVLIIGPYGTGKTFTLAQAVKHI--LKQPESRVLICTHSNSAAD 697
Cdd:pfam13245 1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLvaLGGVSFPILLAAPTGRAAK 56
|
|
| SMN |
pfam06003 |
Survival motor neuron protein (SMN); This family consists of several eukaryotic survival motor ... |
1286-1389 |
3.46e-03 |
|
Survival motor neuron protein (SMN); This family consists of several eukaryotic survival motor neuron (SMN) proteins. The Survival of Motor Neurons (SMN) protein, the product of the spinal muscular atrophy-determining gene, is part of a large macromolecular complex (SMN complex) that functions in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). The SMN complex functions as a specificity factor essential for the efficient assembly of Sm proteins on U snRNAs and likely protects cells from illicit, and potentially deleterious, non-specific binding of Sm proteins to RNAs.
Pssm-ID: 428716 [Multi-domain] Cd Length: 264 Bit Score: 41.53 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1286 LLTPERKAPELKEKQGDLESVQNKSPEPQSNMGFPANrlirKDPQralNFHMAPPHPAFPSHH-GTSQFPQQYGLSRPPL 1364
Cdd:pfam06003 118 LLTPPPDMDEDALKTANVNETESSTDESDRSSGSAKH----KSKS---NFPMGPPSPWNPSFPpGPPPPPPGFGRHGEKP 190
|
90 100
....*....|....*....|....*
gi 1207168626 1365 RMqtpMHPQASSFPPSFYSGPPMGP 1389
Cdd:pfam06003 191 RT---LGPFLSGWPPPFPLGPPMIP 212
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
655-700 |
6.69e-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: 39.05 E-value: 6.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1207168626 655 PPVLIIGPYGTGKTfTLAQAVKHILKQPESRVLICTHSNSAADLYI 700
Cdd:cd00009 20 KNLLLYGPPGTGKT-TLARAIANELFRPGAPFLYLNASDLLEGLVV 64
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1447-1621 |
6.90e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1447 DGQASSGMDALQHQQQARVGQwGEHTPFLPAGVAPFPLPQQLAHLAQPGLRIPPQIL---RAGWGLGPAADEEPRPTMPR 1523
Cdd:PRK12323 423 PARRSPAPEALAAARQASARG-PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAapaRAAPAAAPAPADDDPPPWEE 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1524 YPGLLREMLP--QDQQYEQRDPAEMPPPQSRLLQYRQQIQPRSPGDLPSPSSSAPNHNFPAPAQPSYPDtSREPPVGFSQ 1601
Cdd:PRK12323 502 LPPEFASPAPaqPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASA-SGLPDMFDGD 580
|
170 180
....*....|....*....|
gi 1207168626 1602 APfppdHSAGPLPVKYLLQE 1621
Cdd:PRK12323 581 WP----ALAARLPVRGLAQQ 596
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1514-1833 |
9.34e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1514 DEEPRPTMPRYPGllremlPQDQQYEQRDPAempppQSRLLQyRQQIQPRSPGDLPSPSSSAPNHNFPAPAQPSYPDTSR 1593
Cdd:pfam03154 138 DQDNRSTSPSIPS------PQDNESDSDSSA-----QQQILQ-TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1594 EPPVGFSQAPFPPDHSAGPLPVKYLLQEAHWPHPGHmlghgLPFGLQAMAQRQDPGPlqhqqqkqqlqAPQSSLHSLDEY 1673
Cdd:pfam03154 206 VPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR-----LPSPHPPLQPMTQPPP-----------PSQVSPQPLPQP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1674 EPRGPGRPLYQRRISSSS-------PQPYPDSLEPQDQPVPSYRYPSAdlwlggpgPVPGPAPIHNIPCNGASHIG--PH 1744
Cdd:pfam03154 270 SLHGQMPPMPHSLQTGPShmqhpvpPQPFPLTPQSSQSQVPPGPSPAA--------PGQSQQRIHTPPSQSQLQSQqpPR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168626 1745 REILVSKAMSEEQMKAECLQPPPPPPPHPASAASLQHHGQFPPLLPSKQTPP---DPGGGGNT--SPAGHPKP-PTMSYA 1818
Cdd:pfam03154 342 EQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPpalKPLSSLSThhPPSAHPPPlQLMPQS 421
|
330
....*....|....*
gi 1207168626 1819 SALRAPPKPRPMLPE 1833
Cdd:pfam03154 422 QQLPPPPAQPPVLTQ 436
|
|
| |
