|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
14-449 |
5.40e-175 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 519.31 E-value: 5.40e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 14 RRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL 93
Cdd:COG0514 3 DDALEVLKRVFGYDSFR-PGQEEIIEAVLAG-RDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 KVRVSSLNSKLSAQERKELLADLERekPQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRA--GELKLLYVAPERLLNPRFL----ELLRRLKISLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElISDPYGNLKDFcLKALGQE 253
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDP-RVFVGSFDRPNLRLEVVPKP-PDDKLAQLLDF-LKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 254 AdkglsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAH 333
Cdd:COG0514 232 S-------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 334 WNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKAsdkatimAFDALVTFCEELGCRH 413
Cdd:COG0514 305 YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERA-------KLDAMLAYAETTGCRR 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530413160 414 AAIAKYFGDALPACAKGCDHCQNPT-------AVRRRLEALER 449
Cdd:COG0514 378 QFLLRYFGEELAEPCGNCDNCLGPPetfdgteAAQKALSCVYR 420
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
17-221 |
1.23e-131 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 395.69 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 17 RSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCF 221
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFKTPCF 205
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
17-446 |
6.98e-128 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 400.60 E-value: 6.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 17 RSTLKKVFGFDSFKtPLQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:TIGR01389 2 QQVLKRTFGYDDFR-PGQEEIISHVLDGR-DVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNG--ELKLLYVAPERLEQDYFL----NMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElisdpygNLKDFCLKALGQEadK 256
Cdd:TIGR01389 154 GSLAERFPQVPRIALTATADAETRQDIRELLRLADA-NEFITSFDRPNLRFSVVKKN-------NKQKFLLDYLKKH--R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 336
Cdd:TIGR01389 224 GQSG--IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkEVAKLQEKRGNKASDKatimaFDALVTFCEELGCRHAAI 416
Cdd:TIGR01389 302 PGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDDYKQIEREK-----LRAMIAYCETQTCRRAYI 374
|
410 420 430
....*....|....*....|....*....|.
gi 530413160 417 AKYFGDALPACAKGCDHC-QNPTAVRRRLEA 446
Cdd:TIGR01389 375 LRYFGENEVEPCGNCDNClDPPKSYDATVEA 405
|
|
| RecQ5 |
pfam06959 |
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ... |
625-826 |
1.25e-121 |
|
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.
Pssm-ID: 399738 Cd Length: 202 Bit Score: 369.58 E-value: 1.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 625 KSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDED 704
Cdd:pfam06959 1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 705 GSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEA 784
Cdd:pfam06959 81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSSVAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530413160 785 EGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLR 826
Cdd:pfam06959 161 EGASPSCEGVQGPPMAPEKCTGEEDGAQGHLAAPPQTEECTR 202
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-448 |
9.08e-98 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 321.28 E-value: 9.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 6 TTFPFDPERRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PRK11057 3 QAEVLNLESLAKQVLQETFGYQQFR-PGQQEIIDAVLSG-RDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 86 QVDHLLTLKVRVSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFqptLNSLVSRHLlSYLVVDEAHCVSQW 165
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTG--QIKLLYIAPERLMMDNF---LEHLAHWNP-ALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 166 GHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP---VAIFKTPCFRANLFYdvQFKelisdPYGNL 242
Cdd:PRK11057 155 GHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPliqISSFDRPNIRYTLVE--KFK-----PLDQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 243 KDFCLKALGQeadkglsgCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMG 322
Cdd:PRK11057 228 MRYVQEQRGK--------SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 323 VDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KEVAKLQEKRGNKasdkatima 398
Cdd:PRK11057 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIERHK--------- 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 530413160 399 FDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTavrRRLEALE 448
Cdd:PRK11057 368 LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP---KQYDGLE 414
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-370 |
1.24e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 195.52 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 9 PFDPerrvrsTLKKVFGFDSFKTPLQESATMAVVKGNKD--VFVCMPTGAGKSLCYQLPALLAK---GITIVVSPLIALI 83
Cdd:NF041063 126 PGDP------FLAEALGFTHYRSPGQREAVRAALLAPPGstLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 84 QDQVDHLLTLKVRVSSLNSK-------LSAQERKELLADLEREkpQTKILYITPEmAASSSFQPTLNSLVSRHLLSYLVV 156
Cdd:NF041063 200 IDQERRARELLRRAGPDLGGplawhggLSAEERAAIRQRIRDG--TQRILFTSPE-SLTGSLRPALFDAAEAGLLRYLVV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 157 DEAHCVSQWGHDFRPDYLRLGALRSRL------GHAP-CVALTATATPQVQE------------DVFAALHLKKPVAIFK 217
Cdd:NF041063 277 DEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFrTLLLSATLTESTLDtletlfgppgpfIVVSAVQLRPEPAYWV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 218 TPCFRANlfydvqfkelisdpygNLKDFCLKALgQEADKGLsgcgIVYCRTREACEQLAIELSCRGVN-AKAYHAGLKAS 296
Cdd:NF041063 357 AKCDSEE----------------ERRERVLEAL-RHLPRPL----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDA 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413160 297 ERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 370
Cdd:NF041063 416 ERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
31-201 |
1.96e-30 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 118.11 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESAtMAVVKGNKDVFVCMPTGAGKSLCYQLPAL------LAKGITIVVSPLIALIQDQVDHLLTL-KVRVSSLNSK 103
Cdd:pfam00270 1 TPIQAEA-IPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 104 LSAQERKELLADLERekpqTKILYITPEMAASSsfqptLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPDYLR-LGALRSr 182
Cdd:pfam00270 80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDL-----LQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEiLRRLPK- 147
|
170
....*....|....*....
gi 530413160 183 lgHAPCVALTATATPQVQE 201
Cdd:pfam00270 148 --KRQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
22-229 |
2.61e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.27 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 22 KVFGFDSFkTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA-----KGITIVVSPLIALIQDQVDHLLTL--- 93
Cdd:smart00487 2 EKFGFEPL-RPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLgps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 -KVRVSSLNSKLSAQERKELLadlerEKPQTKILYITPEMAasssFQPTLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPD 172
Cdd:smart00487 81 lGLKVVGLYGGDSKREQLRKL-----ESGKTDILVTTPGRL----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530413160 173 YLRLgaLRSRLGHAPCVALTATATPQVQEdvFAALHLKKPvaIFKTPCFRANLFYDV 229
Cdd:smart00487 150 LEKL--LKLLPKNVQLLLLSATPPEEIEN--LLELFLNDP--VFIDVGFTPLEPIEQ 200
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
632-929 |
3.56e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 632 EPPEPNEYDIPPASHVYSLKPKRVGagfPKGSCPFQTATELmettriREQAPqPErggehepPSRPCGLLDEDGSEPLPG 711
Cdd:PHA03247 2550 DPPPPLPPAAPPAAPDRSVPPPRPA---PRPSEPAVTSRAR------RPDAP-PQ-------SARPRAPVDDRGDPRGPA 2612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 712 PRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSiarffcRRVESPAllasapEAEGACPSC 791
Cdd:PHA03247 2613 PPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP------RRARRLG------RAAQASSPP 2680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 792 EGVQgPPMAPEKYTGEEDGAggHSPAPPQTEEClRERPRPPGMREPPGPSAVMPALPStstcPPRDQGTPEVQPTPAKDT 871
Cdd:PHA03247 2681 QRPR-RRAARPTVGSLTSLA--DPPPPPPTPEP-APHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPG 2752
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530413160 872 WKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAP 929
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
681-898 |
3.09e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 47.84 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 681 QAPQPERGgEHEPPSRPcglldEDGSEPLPGPRGEVPggsahyggPSPEKKAKSssggsslakgraSKKQQLLATAAHKD 760
Cdd:NF033839 160 ETPQPENP-EHQKPTTP-----APDTKPSPQPEGKKP--------SVPDINQEK------------EKAKLAVATYMSKI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 761 SQSIARFFCRRVESPALLASAPEAE----GACPSCEGVQgPPMAPEKyTGEEDGAGGHSPAPPQTEECLRERPRPPGMRE 836
Cdd:NF033839 214 LDDIQKHHLQKEKHRQIVALIKELDelkkQALSEIDNVN-TKVEIEN-TVHKIFADMDAVVTKFKKGLTQDTPKEPGNKK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530413160 837 PPGPSAVM---PALPSTSTCPPRDQGTPEVQPTPAKDTWKGKrPRSQQENPESQPQ-KRPRPSAKP 898
Cdd:NF033839 292 PSAPKPGMqpsPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK-PQPEKPKPEVKPQlETPKPEVKP 356
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
772-937 |
3.03e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 772 VESPALLASAPEAEGACPScEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPRPPGMREP-PGPSAVMPALPST 850
Cdd:PRK12323 382 VAQPAPAAAAPAAAAPAPA-APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGaPAPAPAPAAAPAA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 851 STCPPrdqgTPEVQPTPAKDTwkgKRPRSQQENPESQPQKRPRPS--------AKPSVVAEVKGSVSASEQGTLNPTAQD 922
Cdd:PRK12323 461 AARPA----AAGPRPVAAAAA---AAPARAAPAAAPAPADDDPPPweelppefASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170
....*....|....*
gi 530413160 923 PfqlSAPGVSLKEAA 937
Cdd:PRK12323 534 P---DDAFETLAPAP 545
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
827-922 |
4.71e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.91 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 827 ERPRPPGMREPPGPSAVM---PALPSTSTCPPRDQGTPEVQPTPAKDTWKGKrPRSQQENPESQPQ-KRPRPSAKPSVVA 902
Cdd:NF033839 392 EKPKPEVKPQPEKPKPEVkpqPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVK-PQPEKPKPEVKPQpETPKPEVKPQPEK 470
|
90 100
....*....|....*....|...
gi 530413160 903 ---EVKGSVSASEQGTLNPTAQD 922
Cdd:NF033839 471 pkpEVKPQPEKPKPDNSKPQADD 493
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
14-449 |
5.40e-175 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 519.31 E-value: 5.40e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 14 RRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL 93
Cdd:COG0514 3 DDALEVLKRVFGYDSFR-PGQEEIIEAVLAG-RDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 KVRVSSLNSKLSAQERKELLADLERekPQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRA--GELKLLYVAPERLLNPRFL----ELLRRLKISLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElISDPYGNLKDFcLKALGQE 253
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDP-RVFVGSFDRPNLRLEVVPKP-PDDKLAQLLDF-LKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 254 AdkglsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAH 333
Cdd:COG0514 232 S-------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 334 WNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKAsdkatimAFDALVTFCEELGCRH 413
Cdd:COG0514 305 YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERA-------KLDAMLAYAETTGCRR 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530413160 414 AAIAKYFGDALPACAKGCDHCQNPT-------AVRRRLEALER 449
Cdd:COG0514 378 QFLLRYFGEELAEPCGNCDNCLGPPetfdgteAAQKALSCVYR 420
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
17-221 |
1.23e-131 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 395.69 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 17 RSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCF 221
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFKTPCF 205
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
17-446 |
6.98e-128 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 400.60 E-value: 6.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 17 RSTLKKVFGFDSFKtPLQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:TIGR01389 2 QQVLKRTFGYDDFR-PGQEEIISHVLDGR-DVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNG--ELKLLYVAPERLEQDYFL----NMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElisdpygNLKDFCLKALGQEadK 256
Cdd:TIGR01389 154 GSLAERFPQVPRIALTATADAETRQDIRELLRLADA-NEFITSFDRPNLRFSVVKKN-------NKQKFLLDYLKKH--R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 336
Cdd:TIGR01389 224 GQSG--IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkEVAKLQEKRGNKASDKatimaFDALVTFCEELGCRHAAI 416
Cdd:TIGR01389 302 PGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDDYKQIEREK-----LRAMIAYCETQTCRRAYI 374
|
410 420 430
....*....|....*....|....*....|.
gi 530413160 417 AKYFGDALPACAKGCDHC-QNPTAVRRRLEA 446
Cdd:TIGR01389 375 LRYFGENEVEPCGNCDNClDPPKSYDATVEA 405
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
18-434 |
6.69e-126 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 391.06 E-value: 6.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 18 STLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRV 97
Cdd:TIGR00614 1 KILKKYFGLSSFR-PVQLEVINAVLLG-RDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 98 SSLNSKLSAQERKELLADLEreKPQTKILYITPE-MAASSSFqptLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR00614 79 TFLNSAQTKEQQLNVLTDLK--DGKIKLLYVTPEkISASNRL---LQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKelisdpYGNLKDFCLKALgQEADK 256
Cdd:TIGR00614 154 GSLKQKFPNVPVMALTATASPSVREDILRQLNLLNP-QIFCTSFDRPNLYYEVRRK------TPKILEDLLRFI-RKEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 336
Cdd:TIGR00614 226 GKSG--IIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqvSFLIRKEVakLQEKRGNKASDKATIMafdALVTFCEELG-CRHAA 415
Cdd:TIGR00614 304 PKSMESYYQESGRAGRDGLPSECHLFYAPAD----MNRLRRLL--MEEPDGNFRTYKLKLY---EMMEYCLNSStCRRLI 374
|
410 420
....*....|....*....|....*.
gi 530413160 416 IAKYFGD-------ALPACAKGCDHC 434
Cdd:TIGR00614 375 LLSYFGEkgfnksfCIMGTEKCCDNC 400
|
|
| RecQ5 |
pfam06959 |
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ... |
625-826 |
1.25e-121 |
|
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.
Pssm-ID: 399738 Cd Length: 202 Bit Score: 369.58 E-value: 1.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 625 KSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDED 704
Cdd:pfam06959 1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 705 GSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEA 784
Cdd:pfam06959 81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSSVAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530413160 785 EGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLR 826
Cdd:pfam06959 161 EGASPSCEGVQGPPMAPEKCTGEEDGAQGHLAAPPQTEECTR 202
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
17-220 |
1.10e-99 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 311.39 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 17 RSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:cd17920 1 EQILKEVFGYDEFR-PGQLEAINAVLAG-RDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSLNSKLSAQERKEllADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd17920 79 AAALNSTLSPEEKRE--VLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPC 220
Cdd:cd17920 157 GRLRRALPGVPILALTATATPEVREDILKRLGLRNPV-IFRASF 199
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-448 |
9.08e-98 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 321.28 E-value: 9.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 6 TTFPFDPERRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PRK11057 3 QAEVLNLESLAKQVLQETFGYQQFR-PGQQEIIDAVLSG-RDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 86 QVDHLLTLKVRVSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFqptLNSLVSRHLlSYLVVDEAHCVSQW 165
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTG--QIKLLYIAPERLMMDNF---LEHLAHWNP-ALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 166 GHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP---VAIFKTPCFRANLFYdvQFKelisdPYGNL 242
Cdd:PRK11057 155 GHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPliqISSFDRPNIRYTLVE--KFK-----PLDQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 243 KDFCLKALGQeadkglsgCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMG 322
Cdd:PRK11057 228 MRYVQEQRGK--------SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 323 VDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KEVAKLQEKRGNKasdkatima 398
Cdd:PRK11057 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIERHK--------- 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 530413160 399 FDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTavrRRLEALE 448
Cdd:PRK11057 368 LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP---KQYDGLE 414
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
6-434 |
1.35e-97 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 334.56 E-value: 1.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 6 TTFPFdpERRVRSTLKKVFGFDSFKtPLQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PLN03137 440 RNFPW--TKKLEVNNKKVFGNHSFR-PNQREIINATMSGY-DVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 86 QVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQ 164
Cdd:PLN03137 516 QIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEkVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 165 WGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPCFRANLFYDVQFKelisdpygnlKD 244
Cdd:PLN03137 596 WGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCV-VFRQSFNRPNLWYSVVPK----------TK 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 245 FCLkalgQEADKGL-----SGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISF 319
Cdd:PLN03137 665 KCL----EDIDKFIkenhfDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAF 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 320 GMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRK-EVAKLQEKRG-NKASDKATIM 397
Cdd:PLN03137 741 GMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQgGVEQSPMAMGyNRMASSGRIL 820
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 530413160 398 AFDA-----LVTFCE-ELGCRHAAIAKYFGDALPA--CAKGCDHC 434
Cdd:PLN03137 821 ETNTenllrMVSYCEnEVDCRRFLQLVHFGEKFDStnCKKTCDNC 865
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
15-219 |
6.11e-68 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 226.09 E-value: 6.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 15 RVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLK 94
Cdd:cd18015 5 KVKDTLKNVFKLEKFR-PLQLETINATMAG-RDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 95 VRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:cd18015 83 ISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEkIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530413160 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTP 219
Cdd:cd18015 163 KKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCL-TFTAS 207
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
14-212 |
1.22e-66 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 222.39 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 14 RRVRSTLKKVFGFDSFKTPlQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL 93
Cdd:cd18016 3 KEMMKIFHKKFGLHQFRTN-QLEAINAALLGE-DCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 KVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPD 172
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEkISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530413160 173 YLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP 212
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRP 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
222-363 |
1.95e-66 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 219.00 E-value: 1.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 222 RANLFYDVQFKELISDPYGNLKdfclkalgQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLV 301
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLK--------RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDV 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530413160 302 QNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 363
Cdd:cd18794 73 QRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
19-219 |
2.09e-63 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 213.27 E-value: 2.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 19 TLKKVFGFDSFKtPLQESATMAVVKGNKDVFVcMPTGAGKSLCYQLPALL----AKGITIVVSPLIALIQDQVDHLLTLk 94
Cdd:cd18018 3 LLRRVFGHPSFR-PGQEEAIARLLSGRSTLVV-LPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 95 VRVSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFQPTLNSLVSrhlLSYLVVDEAHCVSQWGHDFRPDYL 174
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAG--EVKILYVSPERLVNESFRELLRQTPP---ISLLVVDEAHCISEWSHNFRPDYL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530413160 175 RLG-ALRSRLGHAPCVALTATATPQVQEDVfaALHLKKP-VAIFKTP 219
Cdd:cd18018 155 RLCrVLRELLGAPPVLALTATATKRVVEDI--ASHLGIPeSGVVRGP 199
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
18-213 |
2.06e-52 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 181.90 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 18 STLKKVFGFDSFKtPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVdhlLTLKVR- 96
Cdd:cd18017 2 NALNEYFGHSSFR-PVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQV---LQLVMSn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 97 VSSlnSKLSAQERKELLADLEREKpqTKILYITPEMAASSsfqPTLNSLVSRHLlSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18017 78 IPA--CFLGSAQSQNVLDDIKMGK--IRVIYVTPEFVSKG---LELLQQLRNGI-TLIAIDEAHCVSQWGHDFRSSYRHL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 530413160 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPV 213
Cdd:cd18017 150 GSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQ 186
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-370 |
1.24e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 195.52 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 9 PFDPerrvrsTLKKVFGFDSFKTPLQESATMAVVKGNKD--VFVCMPTGAGKSLCYQLPALLAK---GITIVVSPLIALI 83
Cdd:NF041063 126 PGDP------FLAEALGFTHYRSPGQREAVRAALLAPPGstLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 84 QDQVDHLLTLKVRVSSLNSK-------LSAQERKELLADLEREkpQTKILYITPEmAASSSFQPTLNSLVSRHLLSYLVV 156
Cdd:NF041063 200 IDQERRARELLRRAGPDLGGplawhggLSAEERAAIRQRIRDG--TQRILFTSPE-SLTGSLRPALFDAAEAGLLRYLVV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 157 DEAHCVSQWGHDFRPDYLRLGALRSRL------GHAP-CVALTATATPQVQE------------DVFAALHLKKPVAIFK 217
Cdd:NF041063 277 DEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFrTLLLSATLTESTLDtletlfgppgpfIVVSAVQLRPEPAYWV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 218 TPCFRANlfydvqfkelisdpygNLKDFCLKALgQEADKGLsgcgIVYCRTREACEQLAIELSCRGVN-AKAYHAGLKAS 296
Cdd:NF041063 357 AKCDSEE----------------ERRERVLEAL-RHLPRPL----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDA 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413160 297 ERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 370
Cdd:NF041063 416 ERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
31-201 |
1.96e-30 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 118.11 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESAtMAVVKGNKDVFVCMPTGAGKSLCYQLPAL------LAKGITIVVSPLIALIQDQVDHLLTL-KVRVSSLNSK 103
Cdd:pfam00270 1 TPIQAEA-IPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 104 LSAQERKELLADLERekpqTKILYITPEMAASSsfqptLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPDYLR-LGALRSr 182
Cdd:pfam00270 80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDL-----LQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEiLRRLPK- 147
|
170
....*....|....*....
gi 530413160 183 lgHAPCVALTATATPQVQE 201
Cdd:pfam00270 148 --KRQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
22-229 |
2.61e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.27 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 22 KVFGFDSFkTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA-----KGITIVVSPLIALIQDQVDHLLTL--- 93
Cdd:smart00487 2 EKFGFEPL-RPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLgps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 -KVRVSSLNSKLSAQERKELLadlerEKPQTKILYITPEMAasssFQPTLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPD 172
Cdd:smart00487 81 lGLKVVGLYGGDSKREQLRKL-----ESGKTDILVTTPGRL----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530413160 173 YLRLgaLRSRLGHAPCVALTATATPQVQEdvFAALHLKKPvaIFKTPCFRANLFYDV 229
Cdd:smart00487 150 LEKL--LKLLPKNVQLLLLSATPPEEIEN--LLELFLNDP--VFIDVGFTPLEPIEQ 200
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
5-357 |
7.17e-19 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 92.21 E-value: 7.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 5 HTTFPFDPERRVRSTLKKvFGFD---SFktplQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVV 76
Cdd:COG1205 34 YAPWPDWLPPELRAALKK-RGIErlySH----QAEAIEAARAG-KNVVIATPTASGKSLAYLLPVLEAlledPGATaLYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 77 SPLIALIQDQVDHLLTL------KVRVSSLNSKLSAQERKELladleREKPQtkILYITPEMaasssfqptLN-SLVSRH 149
Cdd:COG1205 108 YPTKALARDQLRRLRELaealglGVRVATYDGDTPPEERRWI-----REHPD--IVLTNPDM---------LHyGLLPHH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 150 L--------LSYLVVDEAHC---V--SQWGHDFRpdylRLGALRSRLGHAP-CVALTAT-ATPQvqedVFAalhlkkpva 214
Cdd:COG1205 172 TrwarffrnLRYVVIDEAHTyrgVfgSHVANVLR----RLRRICRHYGSDPqFILASATiGNPA----EHA--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 215 ifktpcfrANLFyDVQFkELISD---PYGNlKDFCL-----------KALGQEA--------DKGLSgcGIVYCRTREAC 272
Cdd:COG1205 235 --------ERLT-GRPV-TVVDEdgsPRGE-RTFVLwnpplvddgirRSALAEAarlladlvREGLR--TLVFTRSRRGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 273 EQLAIEL------SCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFV--AHWniAKSMAGYY 344
Cdd:COG1205 302 ELLARYArralrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVvlAGY--PGTRASFW 379
|
410
....*....|...
gi 530413160 345 QESGRAGRDGKPS 357
Cdd:COG1205 380 QQAGRAGRRGQDS 392
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
273-354 |
3.30e-18 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 79.95 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 273 EQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGR 352
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 530413160 353 DG 354
Cdd:smart00490 81 AG 82
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
45-194 |
2.54e-17 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 79.75 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 45 NKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIQDQ---VDHLLTLKVRVSSLNSKLSAQERKELLADLE 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413160 118 rekpqtKILYITPEMAASSSFQptlNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLgaLRSRLGHAPCVALTAT 194
Cdd:cd00046 81 ------DIIIATPDMLLNLLLR---EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
247-354 |
3.22e-16 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 75.32 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 247 LKALGQEADKGLSGCGIVYCRTREACEqLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 530413160 327 NVRFVAHWNIAKSMAGYYQESGRAGRDG 354
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
45-160 |
1.83e-13 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 69.15 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 45 NKDVFVCMPTGAGKSLCYQLPALL------AKGITIV-VSPLIALIQDQVDHL------LTLKVRVSSLNSKLSAQERKE 111
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLeepldeIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530413160 112 LLadlerEKPQTkILYITPEmaassSFQPTLNSLVSRHLLS---YLVVDEAH 160
Cdd:cd17922 81 QL-----KNPPG-ILITTPE-----SLELLLVNKKLRELFAglrYVVVDEIH 121
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-355 |
4.02e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.01 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 12 PERRVRSTLKKvFGFDSFkTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGITIV-VSPLIALIQDQVD 88
Cdd:COG1204 7 PLEKVIEFLKE-RGIEEL-YPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 89 HL------LTLKVRVSSLNsklsAQERKELLADlerekpqTKILYITPEMAAS-SSFQPtlnSLVSRhlLSYLVVDEAHC 161
Cdd:COG1204 85 EFkrdfeeLGIKVGVSTGD----YDSDDEWLGR-------YDILVATPEKLDSlLRNGP---SWLRD--VDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 162 VsqwGHDFR-PDY------LRLGALRSRLghapcVALTATAT-PQVQEDVFAALHLK---KPVAIfktpcfRANLFYD-- 228
Cdd:COG1204 149 I---DDESRgPTLevllarLRRLNPEAQI-----VALSATIGnAEEIAEWLDAELVKsdwRPVPL------NEGVLYDgv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 229 VQFKELISDPYGNLKDFCLKALGQEadkglsGCGIVYCRTREACEQLAIELS---------------------------- 280
Cdd:COG1204 215 LRFDDGSRRSKDPTLALALDLLEEG------GQVLVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 281 ---------C--RGVnakAYH-AGLKASERTLVQnDWMEE-KVPVIVATISFGMGVdkaN--VRFV----AHWNIAKSMA 341
Cdd:COG1204 289 thtnekladCleKGV---AFHhAGLPSELRRLVE-DAFREgLIKVLVATPTLAAGV---NlpARRViirdTKRGGMVPIP 361
|
410
....*....|....*.
gi 530413160 342 G--YYQESGRAGRDGK 355
Cdd:COG1204 362 VleFKQMAGRAGRPGY 377
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
263-357 |
1.92e-12 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 65.74 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 263 IVYCRTREACEQLAIELSCRGVNAK-------AYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWN 335
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 530413160 336 IAKSMAGYYQESGRAGRDGKPS 357
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
46-160 |
2.68e-12 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 66.45 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 46 KDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVVSPLIALIQDQVDHL------LTLKVRVSSLNSKLSAQERKELLa 114
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAllrdPGSRaLYLYPTKALAQDQLRSLrelleqLGLGIRVATYDGDTPREERRAII- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530413160 115 dleREKPQtkILYITPEMaasssfqptLNSLVSRH---------LLSYLVVDEAH 160
Cdd:cd17923 95 ---RNPPR--ILLTNPDM---------LHYALLPHhdrwarflrNLRYVVLDEAH 135
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
263-354 |
1.08e-09 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 57.95 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 263 IVYCRTREACEQLAIELSCrgvnAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVD--------KANVRFVAHW 334
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|
gi 530413160 335 NIAKSMAGYYQESGRAGRDG 354
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPG 142
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
247-355 |
1.26e-09 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 57.13 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 247 LKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:cd18787 15 LLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIP 94
|
90 100
....*....|....*....|....*....
gi 530413160 327 NVRFVAHWNIAKSMAGYYQESGRAGRDGK 355
Cdd:cd18787 95 GVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
43-352 |
6.02e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 59.65 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 43 KGNKDVFVCMPTGAGKSL----CYQlpALLAKGITIVVSPLIALIQDQVDHLLTLkvrvssLNSKLSAQERKELLADler 118
Cdd:COG1061 98 RGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------LGDPLAGGGKKDSDAP--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 119 ekpqtkILYITPEMAASssfQPTLNSLVSRhlLSYLVVDEAHcvsqwghdfrpdylRLGA-----LRSRLGHAPCVALta 193
Cdd:COG1061 167 ------ITVATYQSLAR---RAHLDELGDR--FGLVIIDEAH--------------HAGApsyrrILEAFPAAYRLGL-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 194 TATPqVQEDvfaalhlKKPVAIFktpcFRANLFYDVQFKELISD--------------------PYGNLKDFCLKALGQE 253
Cdd:COG1061 220 TATP-FRSD-------GREILLF----LFDGIVYEYSLKEAIEDgylappeyygirvdltderaEYDALSERLREALAAD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 254 AD------------KGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGM 321
Cdd:COG1061 288 AErkdkilrellreHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
330 340 350
....*....|....*....|....*....|.
gi 530413160 322 GVDKANVRFVAHWNIAKSMAGYYQesgRAGR 352
Cdd:COG1061 368 GVDVPRLDVAILLRPTGSPREFIQ---RLGR 395
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
365-434 |
1.44e-08 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 52.29 E-value: 1.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530413160 365 RNDRDQVSFLIRKEVAKLQEKRGNKASdkatimaFDALVTFCEELG-CRHAAIAKYFGDALPA--CaKGCDHC 434
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQK-------LQAMVAYCENTTdCRRKQLLRYFGEEFDSepC-GNCDNC 65
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-195 |
3.61e-08 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 54.19 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIqDQVDHLLTLKVRVSSLNSKL-- 104
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALV-NQKEADLRERFGPLGKNVGLlt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 105 -SAQERKELLADLErekpqtkILYITPEMAASssfqpTLNSLVSRHL--LSYLVVDEAHCVSQwghdfrPDY-----LRL 176
Cdd:cd17921 82 gDPSVNKLLLAEAD-------ILVATPEKLDL-----LLRNGGERLIqdVRLVVVDEAHLIGD------GERgvvleLLL 143
|
170
....*....|....*....
gi 530413160 177 GALRSRLGHAPCVALTATA 195
Cdd:cd17921 144 SRLLRINKNARFVGLSATL 162
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
240-354 |
9.52e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 55.94 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 240 GNLKDFcLKALGQEADKGLsgcgiVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISF 319
Cdd:PTZ00110 364 GKLKML-LQRIMRDGDKIL-----IFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
|
90 100 110
....*....|....*....|....*....|....*
gi 530413160 320 GMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDG 354
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
252-352 |
1.81e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 55.28 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 252 QEADKGLSGCGIVYCRTREACEQLAIELscrGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDkanvrFV 331
Cdd:COG1202 420 TKSSKGYRGQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD-----FP 491
|
90 100 110
....*....|....*....|....*....|
gi 530413160 332 AHWNIAKSMA-G--------YYQESGRAGR 352
Cdd:COG1202 492 ASQVIFDSLAmGiewlsvqeFHQMLGRAGR 521
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
31-316 |
2.64e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 54.00 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPAL--LAKGI-----TIVVSP---LIALIQDQVDHLLT-LKVRVSS 99
Cdd:COG0513 26 TPIQAQAIPLILAG-RDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLALQVAEELRKLAKyLGLRVAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 100 L--NSKLSAQERKelladLEReKPQtkILYITP----EMAASSSFqptlnSLvsrHLLSYLVVDEAhcvsqwghD----- 168
Cdd:COG0513 105 VygGVSIGRQIRA-----LKR-GVD--IVVATPgrllDLIERGAL-----DL---SGVETLVLDEA--------Drmldm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 169 -FRPDylrlgaLRSRLGHAPCVALT----ATATPQVQEdvFAALHLKKPVAIFKTPCFRAN-----LFYDVQFKElisdp 238
Cdd:COG0513 161 gFIED------IERILKLLPKERQTllfsATMPPEIRK--LAKRYLKNPVRIEVAPENATAetieqRYYLVDKRD----- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530413160 239 ygnlKDFCLKALGQEADKGLsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVAT 316
Cdd:COG0513 228 ----KLELLRRLLRDEDPER---AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
261-355 |
1.54e-06 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 46.93 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 261 CGIVYCRTREACEQLAIELScrgvnakayhaglkasertlvqndwmeekvpVIVATISFGMGVDKANVRFVAHWNIAKSM 340
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|....*
gi 530413160 341 AGYYQESGRAGRDGK 355
Cdd:cd18785 54 ASYIQRVGRAGRGGK 68
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
31-211 |
3.35e-06 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 49.12 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPA----LLAKGITIVVSPLIALI-------QDQV-DHLLTL----- 93
Cdd:cd17961 18 TLIQSKAIPLALEG-KDILARARTGSGKTAAYALPIiqkiLKAKAESGEEQGTRALIlvptrelAQQVsKVLEQLtaycr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 94 -KVRVSSLNSKLSAQERKELLADlereKPQtkILYITPEMAASssfQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDfrpd 172
Cdd:cd17961 97 kDVRVVNLSASSSDSVQRALLAE----KPD--IVVSTPARLLS---HLESGSLLLLSTLKYLVIDEADLVLSYGYE---- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530413160 173 ylrlGALRSRLGHAP----CVALTATATPQVQEdvfaalhLKK 211
Cdd:cd17961 164 ----EDLKSLLSYLPknyqTFLMSATLSEDVEA-------LKK 195
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
632-929 |
3.56e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 632 EPPEPNEYDIPPASHVYSLKPKRVGagfPKGSCPFQTATELmettriREQAPqPErggehepPSRPCGLLDEDGSEPLPG 711
Cdd:PHA03247 2550 DPPPPLPPAAPPAAPDRSVPPPRPA---PRPSEPAVTSRAR------RPDAP-PQ-------SARPRAPVDDRGDPRGPA 2612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 712 PRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSiarffcRRVESPAllasapEAEGACPSC 791
Cdd:PHA03247 2613 PPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP------RRARRLG------RAAQASSPP 2680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 792 EGVQgPPMAPEKYTGEEDGAggHSPAPPQTEEClRERPRPPGMREPPGPSAVMPALPStstcPPRDQGTPEVQPTPAKDT 871
Cdd:PHA03247 2681 QRPR-RRAARPTVGSLTSLA--DPPPPPPTPEP-APHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPG 2752
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530413160 872 WKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAP 929
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
32-194 |
4.90e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 47.30 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 32 PLQESATMAVVKGNKDVF--VCMPTGAGKSLC-YQLPALLAKGITIVVSPLIALIQDQVDHLLTLkvrvsslnskLSAQE 108
Cdd:cd17926 3 PYQEEALEAWLAHKNNRRgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDF----------LGDSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 109 RKELLADLEREKPQTKILYITPEMAASSSFQPTLNSlvsrHLLSYLVVDEAH--CVSQWGHdfrpdylrlgaLRSRLGHA 186
Cdd:cd17926 73 IGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLF----DQFGLLIVDEAHhlPAKTFSE-----------ILKELNAK 137
|
....*...
gi 530413160 187 PCVALTAT 194
Cdd:cd17926 138 YRLGLTAT 145
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
31-167 |
8.69e-06 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 48.00 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 31 TPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLP---ALLA----KGITIVVSPLIALI-------QDQV-DHLLTLK- 94
Cdd:cd17946 14 TPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPileRLLSqkssNGVGGKQKPLRALIltptrelAVQVkDHLKAIAk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 95 ---VRVSSLNSKLSAQERKELLadleREKPQtkILYITP----EMAASSsfQPTLNSLvsrHLLSYLVVDEAHCVSQWGH 167
Cdd:cd17946 94 ytnIKIASIVGGLAVQKQERLL----KKRPE--IVVATPgrlwELIQEG--NEHLANL---KSLRFLVLDEADRMLEKGH 162
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
629-932 |
1.19e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 629 AQAEPPEPNEYDIPPAShvyslKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEP 708
Cdd:PHA03247 2753 GPARPARPPTTAGPPAP-----APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 709 LPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAhkdsqSIARFFCRRVESPALlasapeaegaC 788
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPA-----APARPPVRRLARPAV----------S 2892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 789 PSCEGVQGPPMAPEkytgeedgagghspappqteeclreRPRPPGMREPPGPSAVMPALPStSTCPPRDQGTPEVQPTPA 868
Cdd:PHA03247 2893 RSTESFALPPDQPE-------------------------RPPQPQAPPPPQPQPQPPPPPQ-PQPPPPPPPRPQPPLAPT 2946
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413160 869 KDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTaqdpfQLSAPGVS 932
Cdd:PHA03247 2947 TDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT-----GHSLSRVS 3005
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
47-159 |
2.34e-05 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 46.86 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 47 DVFVCMPTGAGKSLCYQLP---ALLAKGIT----IVVSPLIALIQdQVDHLLT-----LKVRVSSLNSKLS-AQERKELL 113
Cdd:cd17956 38 DLCVSAPTGSGKTLAYVLPivqALSKRVVPrlraLIVVPTKELVQ-QVYKVFEslckgTGLKVVSLSGQKSfKKEQKLLL 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530413160 114 ADLERE---KPQtkILYITP-----EMAASSSFqpTLNSlvsrhlLSYLVVDEA 159
Cdd:cd17956 117 VDTSGRylsRVD--ILVATPgrlvdHLNSTPGF--TLKH------LRFLVIDEA 160
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
22-159 |
2.60e-05 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 46.42 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 22 KVFGFDSFkTPLQeSATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGIT---------IVVSPLIALIQdQVDHL 90
Cdd:cd17960 6 AELGFTSM-TPVQ-AATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLKRKAnlkkgqvgaLIISPTRELAT-QIYEV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413160 91 LT--LKVRVSSLNSKL--SAQERKELLADLEREKPQtkILYITP----EMAASSSFQPTLNSlvsrhlLSYLVVDEA 159
Cdd:cd17960 83 LQsfLEHHLPKLKCQLliGGTNVEEDVKKFKRNGPN--ILVGTPgrleELLSRKADKVKVKS------LEVLVLDEA 151
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
263-355 |
2.98e-05 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 47.51 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 263 IVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAG 342
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|...
gi 530413160 343 YYQESGRAGRDGK 355
Cdd:PTZ00424 351 YIHRIGRSGRFGR 363
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
681-898 |
3.09e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 47.84 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 681 QAPQPERGgEHEPPSRPcglldEDGSEPLPGPRGEVPggsahyggPSPEKKAKSssggsslakgraSKKQQLLATAAHKD 760
Cdd:NF033839 160 ETPQPENP-EHQKPTTP-----APDTKPSPQPEGKKP--------SVPDINQEK------------EKAKLAVATYMSKI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 761 SQSIARFFCRRVESPALLASAPEAE----GACPSCEGVQgPPMAPEKyTGEEDGAGGHSPAPPQTEECLRERPRPPGMRE 836
Cdd:NF033839 214 LDDIQKHHLQKEKHRQIVALIKELDelkkQALSEIDNVN-TKVEIEN-TVHKIFADMDAVVTKFKKGLTQDTPKEPGNKK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530413160 837 PPGPSAVM---PALPSTSTCPPRDQGTPEVQPTPAKDTWKGKrPRSQQENPESQPQ-KRPRPSAKP 898
Cdd:NF033839 292 PSAPKPGMqpsPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK-PQPEKPKPEVKPQlETPKPEVKP 356
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
617-933 |
4.75e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 617 PYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQ---------TATELMETTRIREQAPQPER 687
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarpTVGSLTSLADPPPPPPTPEP 2710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 688 GGEHEPPSRPCGLLDEDGSEPLPGPRGE-----VPGGSAHYGGPSPEKKAKSSSGGSSLAKGRA-SKKQQLLATAAHKDS 761
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAApappaVPAGPATPGGPARPARPPTTAGPPAPAPPAApAAGPPRRLTRPAVAS 2790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 762 QSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEkyTGEEDGAGGHSPAPPQTEECLRERPRPPGMREPPGPS 841
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP--TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPS 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 842 AVMPALPSTSTCPP-RDQGTPEVQPTP---AKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLN 917
Cdd:PHA03247 2869 RSPAAKPAAPARPPvRRLARPAVSRSTesfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD 2948
|
330
....*....|....*.
gi 530413160 918 PTAQDPFQLSAPGVSL 933
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWL 2964
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
682-904 |
1.08e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 682 APQPERGGEHEP-----PSR--PCGLLDEDGSEPLPgPR------GEVPGGSAHYGGPSPEKKAksssggsslakgrask 748
Cdd:PHA03247 2495 APDPGGGGPPDPdappaPSRlaPAILPDEPVGEPVH-PRmltwirGLEELASDDAGDPPPPLPP---------------- 2557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 749 kqqLLATAAHKDSQSIARFFCRRVEsPALLASApeaegACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEeclreR 828
Cdd:PHA03247 2558 ---AAPPAAPDRSVPPPRPAPRPSE-PAVTSRA-----RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH-----A 2623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530413160 829 PRPPgmrePPGPSAVMPALPSTSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEV 904
Cdd:PHA03247 2624 PDPP----PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL 2695
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
25-216 |
3.76e-04 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350777 [Multi-domain] Cd Length: 214 Bit Score: 43.13 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 25 GFDSFKT--PLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKG-------------ITIV-VSPLIALIQDQVd 88
Cdd:cd18019 11 AFEGFKSlnRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGkhrnpdgtinldaFKIVyIAPMKALVQEMV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 89 hlLTLKVRVSSLNSKLSaqerkELLADLEREKPQ---TKILYITPE---MAASSSFQPTLNSLVsrhllSYLVVDEAHCV 162
Cdd:cd18019 90 --GNFSKRLAPYGITVA-----ELTGDQQLTKEQiseTQIIVTTPEkwdIITRKSGDRTYTQLV-----RLIIIDEIHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530413160 163 sqwgHDFRPDYLRlgALRSR------LGHAPC--VALTATaTPQVqEDVFAALHLKKPVAIF 216
Cdd:cd18019 158 ----HDDRGPVLE--SIVARtirqieQTQEYVrlVGLSAT-LPNY-EDVATFLRVDPKKGLF 211
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
40-160 |
5.59e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.50 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 40 AVVKGNKDVFVCMPTGAGKSLCY-QLPALLAK----GITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKella 114
Cdd:pfam04851 18 SIKNGQKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKD---- 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530413160 115 dleREKPQTKILYITPEMAASSSFQPTLNSLVSRHLlsYLVVDEAH 160
Cdd:pfam04851 94 ---ESVDDNKIVVTTIQSLYKALELASLELLPDFFD--VIIIDEAH 134
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
41-194 |
8.62e-04 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 41.58 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 41 VVKGNKDVFVCMPTGAGKSLC--YQLPALLA---KGITIVVSPLIALIQDQVdhlltlkVRVSSLNSKLSAQERKELLAD 115
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFIsyYCMEKVLResdDGVVVYVAPTKALVNQVV-------AEVYARFSKKYPPSGKSLWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 116 LERE----KPQT-KILYITPEMAASSSFQPTLNSLVSRhlLSYLVVDEAHCVSQWGHDFRPDYLRLgalrsrLGHAPCVA 190
Cdd:cd18025 85 FTRDyrhnNPMNcQVLITVPECLEILLLSPHNASWVPR--IKYVIFDEIHSIGQSEDGAVWEQLLL------LIPCPFLA 156
|
....
gi 530413160 191 LTAT 194
Cdd:cd18025 157 LSAT 160
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
22-211 |
1.06e-03 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 41.41 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 22 KVFGFDSfKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGI---------TIVVSP---LIALIQDQV 87
Cdd:cd17964 10 TRMGFET-MTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIqsLLNTKpagrrsgvsALIISPtreLALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 88 DHLLTL--KVRVSSLnskLSAQERKELLADLEREKPQtkILYITP----EMAASSSFQPTLNSlvsrhlLSYLVVDEAHC 161
Cdd:cd17964 89 KKLLQGlrKLRVQSA---VGGTSRRAELNRLRRGRPD--ILVATPgrliDHLENPGVAKAFTD------LDYLVLDEADR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530413160 162 VSQWGhdFRPDylrlgaLRSRLGHAPCVALT--------ATATPQVQEdvFAALHLKK 211
Cdd:cd17964 158 LLDMG--FRPD------LEQILRHLPEKNADprqtllfsATVPDEVQQ--IARLTLKK 205
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
642-931 |
1.28e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.75 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 642 PPASHVYSLKPKRVGAGFPKgscPFQTATELMETTRIReqAPQPERGGEHEPPSRPCGLldedgseplpGPRGEVPGGSA 721
Cdd:PHA03378 580 PTTSQLASSAPSYAQTPWPV---PHPSQTPEPPTTQSH--IPETSAPRQWPMPLRPIPM----------RPLRMQPITFN 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 722 HYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQsiarffcRRVESPALLASAPEAEGACPscegvqgPPMAP 801
Cdd:PHA03378 645 VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTML-------PIQWAPGTMQPPPRAPTPMR-------PPAAP 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 802 EKYTGEEDGAGGHSPAPPQTEECLRERPRPPGMREPP--GPSAVMP--ALPSTSTCPPRDQGTPEVQPTPakdtwkgKRP 877
Cdd:PHA03378 711 PGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaAPGRARPpaAAPGRARPPAAAPGAPTPQPPP-------QAP 783
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 530413160 878 RSQQENPESQPQKRPRPSAKPSVVaEVKGSVSASEQGtlnPTAQDPFQLSAPGV 931
Cdd:PHA03378 784 PAPQQRPRGAPTPQPPPQAGPTSM-QLMPRAAPGQQG---PTKQILRQLLTGGV 833
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
34-160 |
2.02e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 40.49 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 34 QESATMAVVKGnKDVFVCMPTGAGKS-----LC----YQLPAlLAKGITIVVSPLIALIQDQVD----HLLTLKVRVSSL 100
Cdd:cd17927 7 QLELAQPALKG-KNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEvfrkHFERPGYKVTGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530413160 101 NSKLSAQERKELLADlerekpQTKILYITPemaasssfQPTLNSL-----VSRHLLSYLVVDEAH 160
Cdd:cd17927 85 SGDTSENVSVEQIVE------SSDVIIVTP--------QILVNDLksgtiVSLSDFSLLVFDECH 135
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
676-903 |
3.03e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 676 TRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLAT 755
Cdd:PRK12323 356 TLLRMLAFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAA 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 756 AahkdSQSIARFFCRRVESPALLASAPeAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTeeclrerprPPGMR 835
Cdd:PRK12323 436 A----RQASARGPGGAPAPAPAPAAAP-AAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP---------PPWEE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530413160 836 EPPGPSAVMPALPSTSTCPPRDQGTPEVQPTPAKDTWKGKRP-RSQQENPESQPQKRPRPSAKPSVVAE 903
Cdd:PRK12323 502 LPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPaPAAAPAPRAAAATEPVVAPRPPRASA 570
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
772-937 |
3.03e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 772 VESPALLASAPEAEGACPScEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPRPPGMREP-PGPSAVMPALPST 850
Cdd:PRK12323 382 VAQPAPAAAAPAAAAPAPA-APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGaPAPAPAPAAAPAA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 851 STCPPrdqgTPEVQPTPAKDTwkgKRPRSQQENPESQPQKRPRPS--------AKPSVVAEVKGSVSASEQGTLNPTAQD 922
Cdd:PRK12323 461 AARPA----AAGPRPVAAAAA---AAPARAAPAAAPAPADDDPPPweelppefASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170
....*....|....*
gi 530413160 923 PfqlSAPGVSLKEAA 937
Cdd:PRK12323 534 P---DDAFETLAPAP 545
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
779-902 |
3.17e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 779 ASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPRPPGMREPPGPSAVMPALPSTSTCPPRDQ 858
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530413160 859 GTPEVQPTPAkdtwkGKRPRSQQENPESQPQKRPRPSAKPSVVA 902
Cdd:PRK07764 697 APAQPAPAPA-----ATPPAGQADDPAAQPPQAAQGASAPSPAA 735
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
827-922 |
4.71e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.91 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 827 ERPRPPGMREPPGPSAVM---PALPSTSTCPPRDQGTPEVQPTPAKDTWKGKrPRSQQENPESQPQ-KRPRPSAKPSVVA 902
Cdd:NF033839 392 EKPKPEVKPQPEKPKPEVkpqPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVK-PQPEKPKPEVKPQpETPKPEVKPQPEK 470
|
90 100
....*....|....*....|...
gi 530413160 903 ---EVKGSVSASEQGTLNPTAQD 922
Cdd:NF033839 471 pkpEVKPQPEKPKPDNSKPQADD 493
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
262-356 |
4.72e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 40.54 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 262 GIVYCRTREACEQLAIELS-CRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSM 340
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90
....*....|....*.
gi 530413160 341 AGYYQESGRAGRDGKP 356
Cdd:PLN00206 450 KEYIHQIGRASRMGEK 465
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
37-128 |
4.79e-03 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 40.27 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 37 ATMAVVK-GNKDVFV-CMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL--------KVRVSSLnSKLSA 106
Cdd:TIGR03158 4 ATFEALQsKDADIIFnTAPTGAGKTLAWLTPLLHGENDTIALYPTNALIEDQTEAIKEFvdvfkperDVNLLHV-SKATL 82
|
90 100
....*....|....*....|..
gi 530413160 107 QERKELLADLEREKPQTKILYI 128
Cdd:TIGR03158 83 KDIKEYANDKVGSSKGEKLYNL 104
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
34-163 |
6.93e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 39.12 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 34 QESATMAVVKGNKDVFVCMPTGAGKSLCYQL----PALLAKGITIVVSPLIALIQDQVDHLltlkvrvSSLNSKLSAQER 109
Cdd:cd18026 22 KECLSLPGLLEGRNLVYSLPTSGGKTLVAEIlmlkRLLERRKKALFVLPYVSIVQEKVDAL-------SPLFEELGFRVE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413160 110 kELLADLEREKP----QTKILYITPEMAASssfqpTLNSLV---SRHLLSYLVVDEAHCVS 163
Cdd:cd18026 95 -GYAGNKGRSPPkrrkSLSVAVCTIEKANS-----LVNSLIeegRLDELGLVVVDELHMLG 149
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
585-912 |
7.97e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.15 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 585 HETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPN------EYDIPPASHVYSLKPKRVGAG 658
Cdd:PHA03307 77 TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPPAASPPAAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 659 FPKGSCPFQTAT--ELMETTRIREQA------PQPERGGEHEPP--SRPCGLLDE------DGSEPLPGPRGEVPGGSAH 722
Cdd:PHA03307 157 ASPAAVASDAASsrQAALPLSSPEETarapssPPAEPPPSTPPAaaSPRPPRRSSpisasaSSPAPAPGRSAADDAGASS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 723 YGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPE 802
Cdd:PHA03307 237 SDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 803 KYTGE-EDGAGGHSPAPPQTEECL----RERPRPPGMREPPGPSAV-MPALPSTSTCPPRDQGTPEVQPTPAKDTWKGKR 876
Cdd:PHA03307 317 SSSSSrESSSSSTSSSSESSRGAAvspgPSPSRSPSPSRPPPPADPsSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
|
330 340 350
....*....|....*....|....*....|....*.
gi 530413160 877 PRSQQENPESQPQKRPRPSakPSVVAEVKGSVSASE 912
Cdd:PHA03307 397 RARRRDATGRFPAGRPRPS--PLDAGAASGAFYARY 430
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
34-197 |
8.08e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 38.34 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 34 QESATMAVVK---GNKDVFVCMPTGAGKSLCY--QLPALLAKGIT-IVVSPLIALIQDQVDHLltlKVR----VSSLNSK 103
Cdd:cd17929 1 QRKAYEAIVSslgGFKTFLLHGVTGSGKTEVYieLIEKVLAKGKQvLVLVPEISLTPQLIKRF---KKRfgdkVAVLHSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 104 LSAQERKELLADLEREKPQTKIlyitpeMAASSSFQPTLNslvsrhlLSYLVVDEAHcVSQWGHDFRPDY-LRLGAL-RS 181
Cdd:cd17929 78 LSDKERADEWRKIKRGEAKVVI------GARSALFAPFKN-------LGLIIVDEEH-DSSYKQDSGPRYhARDVAIyRA 143
|
170
....*....|....*.
gi 530413160 182 RLGHAPCValTATATP 197
Cdd:cd17929 144 KLENAPVV--LGSATP 157
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
574-857 |
9.40e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.97 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 574 ADLRAKAVELEHET------FRNAKVANLYKASVLKK---------VADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNE 638
Cdd:PRK07764 541 LGVRGDTLVLGFSTgglarrFASPGNAEVLVTALAEElggdwqveaVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAA 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 639 YDIPPASHvyslkpkrvgagfpkgscpfqtatelmettriREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPG 718
Cdd:PRK07764 621 PAAPAAPA--------------------------------PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 719 GSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQllatAAHKDSQSIARffcrRVESPALLASAPEAEGACPSCEGVQGPP 798
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQP----APAPAATPPAG----QADDPAAQPPQAAQGASAPSPAADDPVP 740
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413160 799 MAPE-KYTGEEDGAGGHSPAPPQTEECLRERPRPPGMREPPGPSAVMPALPSTSTCPPRD 857
Cdd:PRK07764 741 LPPEpDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
|
|
| |
