|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1910-2235 |
3.18e-77 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438712 [Multi-domain] Cd Length: 218 Bit Score: 255.60 E-value: 3.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1910 FNEDQKKAIETAYAMVKhspsvaKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSD---------ENFNAKIKQNRVL 1980
Cdd:cd18042 1 LNESQLEAIASALQNSP------GITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKvkkklrklqRNLNNKKKKNRIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1981 VCAPSNAAVDELMKKIILEFKEKCKdkknplGNCGDINLVRLGPEKsintevlkfsldsqvnhrmkkdlpshiqemlrrk 2060
Cdd:cd18042 75 VCAPSNAAVDEIVLRLLSEGFLDGD------GRSYKPNVVRVGRQE---------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2061 eildaqldelsrqralcrggremqrqeldehiaivskerqelaskikevqgrpqrAQNTIILESHVICCTLSTSGGLLLE 2140
Cdd:cd18042 115 -------------------------------------------------------LRASILNEADIVCTTLSSSGSDLLE 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2141 SafrgqGGVPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLLEenveqn 2220
Cdd:cd18042 140 S-----LPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGY------ 208
|
330
....*....|....*
gi 568913773 2221 migrlPVLQLTIQYR 2235
Cdd:cd18042 209 -----PVLMLTTQYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1913-2194 |
2.97e-69 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 233.77 E-value: 2.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1913 DQKKAIETAYamvKHSPsvakICLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfNAKIKQNRVLVCAPSNAAVDEL 1992
Cdd:pfam13086 1 SQREAIRSAL---SSSH----FTLIQGPPGTGKTTTIVELIRQLLSYPA---------TSAAAGPRILVCAPSNAAVDNI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1993 MKKIILEfkekckdkknplGNCGDINLVRLGPEKSINTEVLKFSLDSQVNHRMKK-DLPSHIQEMLRRKEILDAQLDELS 2071
Cdd:pfam13086 65 LERLLRK------------GQKYGPKIVRIGHPAAISEAVLPVSLDYLVESKLNNeEDAQIVKDISKELEKLAKALRAFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2072 RQRALCRGGREM------QRQELDEhiaiVSKERQELASKIKEVQgrpQRAQNTIILESHVICCTLSTSGGLLLESAFrg 2145
Cdd:pfam13086 133 KEIIVEKLLKSRnkdkskLEQERRK----LRSERKELRKELRRRE---QSLEREILDEAQIVCSTLSGAGSRLLSSLA-- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568913773 2146 qggvPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISM 2194
Cdd:pfam13086 204 ----NFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVISK 248
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2201-2455 |
8.25e-59 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 201.62 E-value: 8.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2201 YDQSMMARFCKLleenveqnmiGRLPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCSSEW----PFQPYLVF 2276
Cdd:pfam13087 1 LDRSLFERLQEL----------GPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFhlpdPLGPLVFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2277 DVGDGSERRDN--DSYINVQEIKLVMEIIKLIKEKRKDISfRNIGIITHYKAQKTMIQKDLEKEFDKKGLLqpimmgesr 2354
Cdd:pfam13087 71 DVDGSEEEESDggTSYSNEAEAELVVQLVEKLIKSGPEEP-SDIGVITPYRAQVRLIRKLLKRKLGGKLEI--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2355 qqdseaskqqqkssefmhasdelgsstvtqsgisslengathtgpaEVDTVDAFQGRQKDCIIVTCVRASAvQGSIGFLA 2434
Cdd:pfam13087 141 ----------------------------------------------EVNTVDGFQGREKDVIIFSCVRSNE-KGGIGFLS 173
|
250 260
....*....|....*....|.
gi 568913773 2435 SLQRLNVTITRAKYSLFILGH 2455
Cdd:pfam13087 174 DPRRLNVALTRAKRGLIIVGN 194
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1905-2476 |
9.74e-55 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 204.28 E-value: 9.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1905 AYLKDFNEDQKKAIETAYamvkhspSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfnakikqnRVLVCAP 1984
Cdd:TIGR00376 153 FFDPNLNESQKEAVLFAL-------SSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL----------------RVLVTAP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1985 SNAAVDELMKKIILEfkekckdkknplgncgDINLVRLGPEKSINTEVLKFSLDSQVNHRMK----KDLPSHIQEMLRRK 2060
Cdd:TIGR00376 210 SNIAVDNLLERLALC----------------DQKIVRLGHPARLLKSNKQHSLDYLIENHPKyqivADIREKIDELIEER 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2061 EILDAQLDELSRQR--------ALCRGGREMQRQELDEHIAIVSKERQELASKIKEVQGRPQRAQNTIILESHViccTLS 2132
Cdd:TIGR00376 274 NKKTKPSPQKRRGLsdikilrkALKKREARGIESLKIASMAEWIETNKSIDRLLKLLPESEERIMNEILAESDA---TNS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2133 TSGGLLLEsafrgqgGVPFSCVIVDEAGQSCEVETLSPLIhRCNKLILVGDPKQLPPTVISMKAQEygydqsmmarfckl 2212
Cdd:TIGR00376 351 MAGSEILN-------GQYFDVAVIDEASQAMEPSCLIPLL-KARKLILAGDHKQLPPTILSHDAEE-------------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2213 LEENVEQNMIGRLP--VLQLTIQYRMHPDICLFPSNYVYNKNLK-----TNRL--------TESIRCSSEWPfQPYLVFD 2277
Cdd:TIGR00376 409 LSLTLFERLIKEYPerSRTLNVQYRMNQKIMEFPSREFYNGKLTahesvANILlrdlpkveATESEDDLETG-IPLLFID 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2278 VG--DGSERRDND--SYINVQEIKLVMEIIK-LIKEKRKDisfRNIGIITHYKAQKTMIQKDLEKefdkkgllqpimmge 2352
Cdd:TIGR00376 488 TSgcELFELKEADstSKYNPGEAELVSEIIQaLVKMGVPA---NDIGVITPYDAQVDLLRQLLEH--------------- 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2353 srqqdseaskqqqkssefmhasdelgsstvtqsgisslengatHTGPAEVDTVDAFQGRQKDCIIVTCVRaSAVQGSIGF 2432
Cdd:TIGR00376 550 -------------------------------------------RHIDIEVSSVDGFQGREKEVIIISFVR-SNRKGEVGF 585
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 568913773 2433 LASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDAQKRG 2476
Cdd:TIGR00376 586 LKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHG 629
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
2057-2475 |
5.45e-53 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 202.67 E-value: 5.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2057 LRRKEILDAQLDELSRQRALCRGGREMQRQELDEHIAIvskeRQELASKIKEVQGRPQRAQNTIILESHVICCTLSTSGG 2136
Cdd:COG1112 472 AAALLALALLESLLEELIEEHPEELEKLIAELREAARL----RRALRRELKKRRELRKLLWDALLELAPVVGMTPASVAR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2137 LLLEsafrgqGGVPFSCVIVDEAGQSCEVETLsPLIHRCNKLILVGDPKQLPPTVIS---MKAQEYGYDQSMMARFCKLL 2213
Cdd:COG1112 548 LLPL------GEGSFDLVIIDEASQATLAEAL-GALARAKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLARL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2214 EEnveqnmigrlPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCssEWPFQPYLVFDVgDGSERRDNDSYINV 2293
Cdd:COG1112 621 PE----------RGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL--ADPDSPLVFIDV-DGVYERRGGSRTNP 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2294 QEIKLVMEIIKLIKEKRKDIsfRNIGIITHYKAQKTMIQKDLEKEFDKKGLlqpimmgesrqqdseaskqqqkssefmha 2373
Cdd:COG1112 688 EEAEAVVELVRELLEDGPDG--ESIGVITPYRAQVALIRELLREALGDGLE----------------------------- 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2374 sdelgsstvtqsgisslengathtgPAEVDTVDAFQGRQKDCIIVTCVRASA--VQGSIGFLAS-LQRLNVTITRAKYSL 2450
Cdd:COG1112 737 -------------------------PVFVGTVDRFQGDERDVIIFSLVYSNDedVPRNFGFLNGgPRRLNVAVSRARRKL 791
|
410 420
....*....|....*....|....*...
gi 568913773 2451 FILGHLRTLME---NQHWYELIQDAQKR 2475
Cdd:COG1112 792 IVVGSRELLDSdpsTPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
2236-2473 |
2.09e-48 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350195 [Multi-domain] Cd Length: 184 Bit Score: 171.65 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2236 MHPDICLFPSNYVYNKNLK--TNRLTESIRCSSEWPFQPYLVFDVGDGSERRDND-SYINVQEIKLVMEIIKLIKEKRkd 2312
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKagVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGtSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2313 ISFRNIGIITHYKAQKTMIQKDLEKEFdkkGLLQPImmgesrqqdseaskqqqkssefmhasdelgsstvtqsgisslen 2392
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRG---GLLEDV-------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2393 gathtgpaEVDTVDAFQGRQKDCIIVTCVRASAVQGSIGFLASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDA 2472
Cdd:cd18808 112 --------EVGTVDNFQGREKDVIILSLVRSNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
.
gi 568913773 2473 Q 2473
Cdd:cd18808 184 E 184
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1844-1999 |
2.25e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 46.51 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1844 PASVKNLTRCIVISSLVTTQRKLKAMSLLSSRNQLARAVLNPNPMDFCTKDLLTTTSERIVAYLKDFNEDQKKAIETAYA 1923
Cdd:COG0507 59 AEDIEAALAALVESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAALEPRAGITLSDEQREAVALALT 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913773 1924 MvkhspsvAKICLIHGPPGTGKSKTIVGLLyRLLTENQRkghsdenfnakikqnRVLVCAPSNAAVDELMKKIILE 1999
Cdd:COG0507 139 T-------RRVSVLTGGAGTGKTTTLRALL-AALEALGL---------------RVALAAPTGKAAKRLSESTGIE 191
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1910-2235 |
3.18e-77 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438712 [Multi-domain] Cd Length: 218 Bit Score: 255.60 E-value: 3.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1910 FNEDQKKAIETAYAMVKhspsvaKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSD---------ENFNAKIKQNRVL 1980
Cdd:cd18042 1 LNESQLEAIASALQNSP------GITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKvkkklrklqRNLNNKKKKNRIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1981 VCAPSNAAVDELMKKIILEFKEKCKdkknplGNCGDINLVRLGPEKsintevlkfsldsqvnhrmkkdlpshiqemlrrk 2060
Cdd:cd18042 75 VCAPSNAAVDEIVLRLLSEGFLDGD------GRSYKPNVVRVGRQE---------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2061 eildaqldelsrqralcrggremqrqeldehiaivskerqelaskikevqgrpqrAQNTIILESHVICCTLSTSGGLLLE 2140
Cdd:cd18042 115 -------------------------------------------------------LRASILNEADIVCTTLSSSGSDLLE 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2141 SafrgqGGVPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLLEenveqn 2220
Cdd:cd18042 140 S-----LPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGY------ 208
|
330
....*....|....*
gi 568913773 2221 migrlPVLQLTIQYR 2235
Cdd:cd18042 209 -----PVLMLTTQYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1913-2194 |
2.97e-69 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 233.77 E-value: 2.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1913 DQKKAIETAYamvKHSPsvakICLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfNAKIKQNRVLVCAPSNAAVDEL 1992
Cdd:pfam13086 1 SQREAIRSAL---SSSH----FTLIQGPPGTGKTTTIVELIRQLLSYPA---------TSAAAGPRILVCAPSNAAVDNI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1993 MKKIILEfkekckdkknplGNCGDINLVRLGPEKSINTEVLKFSLDSQVNHRMKK-DLPSHIQEMLRRKEILDAQLDELS 2071
Cdd:pfam13086 65 LERLLRK------------GQKYGPKIVRIGHPAAISEAVLPVSLDYLVESKLNNeEDAQIVKDISKELEKLAKALRAFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2072 RQRALCRGGREM------QRQELDEhiaiVSKERQELASKIKEVQgrpQRAQNTIILESHVICCTLSTSGGLLLESAFrg 2145
Cdd:pfam13086 133 KEIIVEKLLKSRnkdkskLEQERRK----LRSERKELRKELRRRE---QSLEREILDEAQIVCSTLSGAGSRLLSSLA-- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568913773 2146 qggvPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISM 2194
Cdd:pfam13086 204 ----NFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVISK 248
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2201-2455 |
8.25e-59 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 201.62 E-value: 8.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2201 YDQSMMARFCKLleenveqnmiGRLPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCSSEW----PFQPYLVF 2276
Cdd:pfam13087 1 LDRSLFERLQEL----------GPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFhlpdPLGPLVFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2277 DVGDGSERRDN--DSYINVQEIKLVMEIIKLIKEKRKDISfRNIGIITHYKAQKTMIQKDLEKEFDKKGLLqpimmgesr 2354
Cdd:pfam13087 71 DVDGSEEEESDggTSYSNEAEAELVVQLVEKLIKSGPEEP-SDIGVITPYRAQVRLIRKLLKRKLGGKLEI--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2355 qqdseaskqqqkssefmhasdelgsstvtqsgisslengathtgpaEVDTVDAFQGRQKDCIIVTCVRASAvQGSIGFLA 2434
Cdd:pfam13087 141 ----------------------------------------------EVNTVDGFQGREKDVIIFSCVRSNE-KGGIGFLS 173
|
250 260
....*....|....*....|.
gi 568913773 2435 SLQRLNVTITRAKYSLFILGH 2455
Cdd:pfam13087 174 DPRRLNVALTRAKRGLIIVGN 194
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1905-2476 |
9.74e-55 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 204.28 E-value: 9.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1905 AYLKDFNEDQKKAIETAYamvkhspSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfnakikqnRVLVCAP 1984
Cdd:TIGR00376 153 FFDPNLNESQKEAVLFAL-------SSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL----------------RVLVTAP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1985 SNAAVDELMKKIILEfkekckdkknplgncgDINLVRLGPEKSINTEVLKFSLDSQVNHRMK----KDLPSHIQEMLRRK 2060
Cdd:TIGR00376 210 SNIAVDNLLERLALC----------------DQKIVRLGHPARLLKSNKQHSLDYLIENHPKyqivADIREKIDELIEER 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2061 EILDAQLDELSRQR--------ALCRGGREMQRQELDEHIAIVSKERQELASKIKEVQGRPQRAQNTIILESHViccTLS 2132
Cdd:TIGR00376 274 NKKTKPSPQKRRGLsdikilrkALKKREARGIESLKIASMAEWIETNKSIDRLLKLLPESEERIMNEILAESDA---TNS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2133 TSGGLLLEsafrgqgGVPFSCVIVDEAGQSCEVETLSPLIhRCNKLILVGDPKQLPPTVISMKAQEygydqsmmarfckl 2212
Cdd:TIGR00376 351 MAGSEILN-------GQYFDVAVIDEASQAMEPSCLIPLL-KARKLILAGDHKQLPPTILSHDAEE-------------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2213 LEENVEQNMIGRLP--VLQLTIQYRMHPDICLFPSNYVYNKNLK-----TNRL--------TESIRCSSEWPfQPYLVFD 2277
Cdd:TIGR00376 409 LSLTLFERLIKEYPerSRTLNVQYRMNQKIMEFPSREFYNGKLTahesvANILlrdlpkveATESEDDLETG-IPLLFID 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2278 VG--DGSERRDND--SYINVQEIKLVMEIIK-LIKEKRKDisfRNIGIITHYKAQKTMIQKDLEKefdkkgllqpimmge 2352
Cdd:TIGR00376 488 TSgcELFELKEADstSKYNPGEAELVSEIIQaLVKMGVPA---NDIGVITPYDAQVDLLRQLLEH--------------- 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2353 srqqdseaskqqqkssefmhasdelgsstvtqsgisslengatHTGPAEVDTVDAFQGRQKDCIIVTCVRaSAVQGSIGF 2432
Cdd:TIGR00376 550 -------------------------------------------RHIDIEVSSVDGFQGREKEVIIISFVR-SNRKGEVGF 585
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 568913773 2433 LASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDAQKRG 2476
Cdd:TIGR00376 586 LKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHG 629
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
2057-2475 |
5.45e-53 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 202.67 E-value: 5.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2057 LRRKEILDAQLDELSRQRALCRGGREMQRQELDEHIAIvskeRQELASKIKEVQGRPQRAQNTIILESHVICCTLSTSGG 2136
Cdd:COG1112 472 AAALLALALLESLLEELIEEHPEELEKLIAELREAARL----RRALRRELKKRRELRKLLWDALLELAPVVGMTPASVAR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2137 LLLEsafrgqGGVPFSCVIVDEAGQSCEVETLsPLIHRCNKLILVGDPKQLPPTVIS---MKAQEYGYDQSMMARFCKLL 2213
Cdd:COG1112 548 LLPL------GEGSFDLVIIDEASQATLAEAL-GALARAKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLARL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2214 EEnveqnmigrlPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCssEWPFQPYLVFDVgDGSERRDNDSYINV 2293
Cdd:COG1112 621 PE----------RGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL--ADPDSPLVFIDV-DGVYERRGGSRTNP 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2294 QEIKLVMEIIKLIKEKRKDIsfRNIGIITHYKAQKTMIQKDLEKEFDKKGLlqpimmgesrqqdseaskqqqkssefmha 2373
Cdd:COG1112 688 EEAEAVVELVRELLEDGPDG--ESIGVITPYRAQVALIRELLREALGDGLE----------------------------- 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2374 sdelgsstvtqsgisslengathtgPAEVDTVDAFQGRQKDCIIVTCVRASA--VQGSIGFLAS-LQRLNVTITRAKYSL 2450
Cdd:COG1112 737 -------------------------PVFVGTVDRFQGDERDVIIFSLVYSNDedVPRNFGFLNGgPRRLNVAVSRARRKL 791
|
410 420
....*....|....*....|....*...
gi 568913773 2451 FILGHLRTLME---NQHWYELIQDAQKR 2475
Cdd:COG1112 792 IVVGSRELLDSdpsTPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
2236-2473 |
2.09e-48 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350195 [Multi-domain] Cd Length: 184 Bit Score: 171.65 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2236 MHPDICLFPSNYVYNKNLK--TNRLTESIRCSSEWPFQPYLVFDVGDGSERRDND-SYINVQEIKLVMEIIKLIKEKRkd 2312
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKagVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGtSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2313 ISFRNIGIITHYKAQKTMIQKDLEKEFdkkGLLQPImmgesrqqdseaskqqqkssefmhasdelgsstvtqsgisslen 2392
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRG---GLLEDV-------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2393 gathtgpaEVDTVDAFQGRQKDCIIVTCVRASAVQGSIGFLASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDA 2472
Cdd:cd18808 112 --------EVGTVDNFQGREKDVIILSLVRSNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
.
gi 568913773 2473 Q 2473
Cdd:cd18808 184 E 184
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
1909-2235 |
2.91e-41 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350797 [Multi-domain] Cd Length: 234 Bit Score: 152.79 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1909 DFNEDQKKAIETAYAmvkhspsvAKICLIHGPPGTGKSKTIVGLLYRLltenqrkghsdenfnAKIKQNRVLVCAPSNAA 1988
Cdd:cd18039 1 ELNHSQVDAVKTALQ--------RPLSLIQGPPGTGKTVTSATIVYHL---------------VKQGNGPVLVCAPSNVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1989 VDELMKKIilefkekckdkkNPLGncgdINLVRLgpeKSINTEVLKFSLDSQVNHRMKKDLPSHIQEMLRRKEILDaqLD 2068
Cdd:cd18039 58 VDQLTEKI------------HQTG----LKVVRL---CAKSREAVESPVSFLALHNQVRNLDSAEKLELLKLLKLE--TG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2069 ELSrqralcrggremqrqELDEhiaivsKERQELASKIKevqgrpqraqNTIILESHVICCTLSTSGGLLLesafrgqGG 2148
Cdd:cd18039 117 ELS---------------SADE------KRYRKLKRKAE----------RELLRNADVICCTCVGAGDPRL-------SK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2149 VPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLleenveqnmiGRLPVL 2228
Cdd:cd18039 159 MKFRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQL----------GIRPIR 228
|
....*..
gi 568913773 2229 qLTIQYR 2235
Cdd:cd18039 229 -LQVQYR 234
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1910-2235 |
1.28e-35 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350802 [Multi-domain] Cd Length: 191 Bit Score: 135.04 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1910 FNEDQKKAIETAYAmvkhSPSVAkicLIHGPPGTGKSKTIVGLLYRLLTENQRkghsdenfnakikqnrVLVCAPSNAAV 1989
Cdd:cd18044 2 LNDSQKEAVKFALS----QKDVA---LIHGPPGTGKTTTVVEIILQAVKRGEK----------------VLACAPSNIAV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1990 DELMKKIIlefkekckdkknplgNCGdINLVRLGPEKSINTEVLKFSLDSQVnhrmkkdlpshiqemlrrkeildaqlde 2069
Cdd:cd18044 59 DNLVERLV---------------ALK-VKVVRIGHPARLLESVLDHSLDALV---------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2070 lsrqralcrggremqrqeldehiaivskerqelaskikevqgrpqraqntiilESHVICCTLSTSGGLLLesafrgQGGV 2149
Cdd:cd18044 95 -----------------------------------------------------AAQVVLATNTGAGSRQL------LPNE 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2150 PFSCVIVDEAGQSCEVETLSPLIhRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARfcklLEenveqNMIGRLPVLQ 2229
Cdd:cd18044 116 LFDVVVIDEAAQALEASCWIPLL-KARRCILAGDHKQLPPTILSDKAARGGLGVTLFER----LV-----NLYGESVVRM 185
|
....*.
gi 568913773 2230 LTIQYR 2235
Cdd:cd18044 186 LTVQYR 191
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
1911-2235 |
3.65e-28 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 115.02 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIETAYAMVKHSPSVakicLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfnakikQNRVLVCAPSNAAVD 1990
Cdd:cd18038 3 NDEQKLAVRNIVTGTSRPPPY----IIFGPPGTGKTVTLVEAILQVLRQPP--------------EARILVCAPSNSAAD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1991 ELMKKIILEFKEKckdkknplgncgdINLVRLgpeksintevlkfsLDSQvnhRMKKDLPSHIqemlrrkeildaqldel 2070
Cdd:cd18038 65 LLAERLLNALVTK-------------REILRL--------------NAPS---RDRASVPPEL----------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2071 srqRALCRGGREmqrqeldEHIAIVSKERqelaskikevqgrpqraqntiILESHVICCTLSTSGglLLESAFRGQGGvp 2150
Cdd:cd18038 98 ---LPYCNSKAE-------GTFRLPSLEE---------------------LKKYRIVVCTLMTAG--RLVQAGVPNGH-- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2151 FSCVIVDEAGQSCEVETLSPLIHRCNK---LILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKL--LEENVEQNMigrL 2225
Cdd:cd18038 143 FTHIFIDEAGQATEPEALIPLSELASKntqIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERplYYKDGEYNP---S 219
|
330
....*....|
gi 568913773 2226 PVLQLTIQYR 2235
Cdd:cd18038 220 YITKLLKNYR 229
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1911-2235 |
7.13e-24 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350799 [Multi-domain] Cd Length: 203 Bit Score: 101.93 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIETAYamvkhspsVAK-ICLIHGPPGTGKSKTIVGLLYRLLTENqrkghsdenfnakikqNRVLVCAPSNAAV 1989
Cdd:cd18041 3 NKDQRQAIKKVL--------NAKdYALILGMPGTGKTTTIAALVRILVALG----------------KSVLLTSYTHSAV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1990 DelmkKIILEFKEKckdkknplgncgDINLVRLGPEKSINTEVLKFSLDSqvnhrmkkdlpshiqemlrrkeildaqlde 2069
Cdd:cd18041 59 D----NILLKLKKF------------GVNFLRLGRLKKIHPDVQEFTLEA------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2070 lsrqralcrggremqrqeldehIAIVSKERQELASKIKEVQgrpqraqntiileshVICCTLSTsgglLLESAFRGQggv 2149
Cdd:cd18041 93 ----------------------ILKSCKSVEELESKYESVS---------------VVATTCLG----INHPIFRRR--- 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2150 PFSCVIVDEAGQSCEVETLSPLIHrCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLLEENveqnmigrlpVLQ 2229
Cdd:cd18041 129 TFDYCIVDEASQITLPICLGPLRL-AKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDA----------VVQ 197
|
....*.
gi 568913773 2230 LTIQYR 2235
Cdd:cd18041 198 LTIQYR 203
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1911-2235 |
1.09e-22 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350798 [Multi-domain] Cd Length: 271 Bit Score: 100.29 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIETAYAmvkhspsvAKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSDENFNAKikqNRVLVCAPSNAAVD 1990
Cdd:cd18040 3 NPSQNHAVRTALT--------KPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSGEGDGG---PCVLYCGPSNKSVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1991 ---ELMK-----KIILEFKEKCKDKKNPLGNCGDINLVRLGPEKSINTEVLKFSLdsqvNHRMKKDLPSHIQEMLrrkei 2062
Cdd:cd18040 72 vvaELLLkvpglKILRVYSEQIETTEYPIPNEPRHPNKKSERESKPNSELSSITL----HHRIRQPSNPHSQQIK----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2063 ldaqldelSRQRALCRGGREMQRQELDEHIAIVSKER-QELASKikevqgrpqraqntiilesHVICCTLSTSGGLLLES 2141
Cdd:cd18040 143 --------AFEARFERTQEKITEEDIKTYKILIWEARfEELETV-------------------DVILCTCSEAASQKMRT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2142 AfrgqggVPFSCVIVDEAGQSCEVETLSPLI--HRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKlleenveq 2219
Cdd:cd18040 196 H------ANVKQCIVDECGMCTEPESLIPIVsaPRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE-------- 261
|
330
....*....|....*.
gi 568913773 2220 nmigrlPVLQLTIQYR 2235
Cdd:cd18040 262 ------KACMLDTQYR 271
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
2154-2235 |
5.93e-16 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438708 [Multi-domain] Cd Length: 121 Bit Score: 76.12 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2154 VIVDEAGQSCEVETLsPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFcklleenVEQNMIGRLPVLQLTIQ 2233
Cdd:cd17934 48 VIIDEASQITEPELL-IALIRAKKVVLVGDPKQLPPVVQEDHAALLGLSFILSLLL-------LFRLLLPGSPKVMLDTQ 119
|
..
gi 568913773 2234 YR 2235
Cdd:cd17934 120 YR 121
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
1909-2209 |
1.57e-15 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350836 [Multi-domain] Cd Length: 230 Bit Score: 78.56 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1909 DFNEDQKKAIETAYAMV-KHSPSVakiclIHGPPGTGKSKTIVGLLYRLLTEnqrkghsdenfnakIKQNRVLVCAPSNA 1987
Cdd:cd18078 1 DLNELQKEAVKRILGGEcRPLPYI-----LFGPPGTGKTVTIIEAILQVVYN--------------LPRSRILVCAPSNS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1988 AVDELMKKIIlefkekckdkknplgncgDINLVRLGPEKSINTevlkfsldsqvNHRMKKDLPSHIQEMLRRKEildaQL 2067
Cdd:cd18078 62 AADLVTSRLH------------------ESKVLKPGDMVRLNA-----------VNRFESTVIDARKLYCRLGE----DL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2068 DELSRQRalcrggremqrqeldehiaivskerqelaskikevqgrpqraqntiileshvICCTLSTSGGLLLesafrgQG 2147
Cdd:cd18078 109 SKASRHR----------------------------------------------------IVISTCSTAGLLY------QM 130
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568913773 2148 GVP---FSCVIVDEAGQSCEVETLSPL--IH-RCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARF 2209
Cdd:cd18078 131 GLPvghFTHVFVDEAGQATEPESLIPLglISsRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERL 198
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
2123-2247 |
2.47e-12 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 68.61 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2123 ESHVICCT---LSTSGGLLLESAFRgqggvpFSCVIVDEAGQSCEVETLSPLI--------HRCNKLILVGDPKQLPPTV 2191
Cdd:cd17935 86 GAKIIAMTcthAALKRGELVELGFK------YDNILMEEAAQILEIETFIPLLlqnpedgpNRLKRLIMIGDHHQLPPVI 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568913773 2192 ISMKAQEYGY-DQSMMARFCKLleenveqnmigRLPVLQLTIQYRMHPDIC-LFPSNY 2247
Cdd:cd17935 160 KNMAFQKYSNmEQSLFTRLVRL-----------GVPTVDLDAQGRARASISsLYNWRY 206
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
2151-2189 |
6.38e-08 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350801 [Multi-domain] Cd Length: 127 Bit Score: 53.36 E-value: 6.38e-08
10 20 30
....*....|....*....|....*....|....*....
gi 568913773 2151 FSCVIVDEAGQsCEVETLSPLIHRCNKLILVGDPKQLPP 2189
Cdd:cd18043 81 FDLVIFDEASQ-IPIEEALPALFRGKQVVVVGDDKQLPP 118
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
2126-2234 |
1.18e-07 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350694 [Multi-domain] Cd Length: 178 Bit Score: 54.09 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2126 VICCTlsTSGGLLLESAFRGQGgvpFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMK--AQEYGYDQ 2203
Cdd:cd17936 84 VIGMT--TTGAAKYRELLQALG---PKVVIVEEAAEVLEAHILAALTPSTEHLILIGDHKQLRPKVNVYEltAKKYNLDV 158
|
90 100 110
....*....|....*....|....*....|.
gi 568913773 2204 SMMARFCKLleenveqnmigRLPVLQLTIQY 2234
Cdd:cd17936 159 SLFERLVKN-----------GLPFVTLNVQR 178
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1911-1998 |
1.31e-07 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350801 [Multi-domain] Cd Length: 127 Bit Score: 52.58 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIETAYamvkHSPSVakicLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfnakikqnRVLVCAPSNAAVD 1990
Cdd:cd18043 1 DSSQEAAIISAR----NGKNV----VIQGPPGTGKSQTIANIIANALARGK----------------RVLFVSEKKAALD 56
|
....*...
gi 568913773 1991 ELMKKIIL 1998
Cdd:cd18043 57 VVRFPCWI 64
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
2112-2216 |
5.49e-07 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350835 [Multi-domain] Cd Length: 226 Bit Score: 53.26 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2112 RPQRAQntiILESHVICCTLSTSGGLLLESAFRGQggvpFSCVIVDEAGQSCEVETLSP--LIHRCNKLILVGDPKQLPP 2189
Cdd:cd18077 115 MPTRED---VMRHRVVVVTLSTSQYLCQLDLEPGF----FTHILLDEAAQAMECEAIMPlaLATKSTRIVLAGDHMQLSP 187
|
90 100 110
....*....|....*....|....*....|....*..
gi 568913773 2190 TVISMKAQEYGYDQSMMARF---------CK-LLEEN 2216
Cdd:cd18077 188 EVYSEFARERNLHISLLERLyehypsehpCRiLLCEN 224
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
2404-2454 |
6.57e-06 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350173 [Multi-domain] Cd Length: 89 Bit Score: 46.66 E-value: 6.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568913773 2404 TVDAFQGRQKDCIIVTCVRAsavqgsigFLASLQRLNVTITRAKYSLFILG 2454
Cdd:cd18786 47 TIDSSQGLTFDVVTLYLPTA--------NSLTPRRLYVALTRARKRLVIYD 89
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
1914-1992 |
2.55e-05 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 46.44 E-value: 2.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568913773 1914 QKKAIETAyamvkhspSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQRKghsdenfnakikqNRVLVCAPSNAAVDEL 1992
Cdd:pfam13245 1 QREAVRTA--------LPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVS-------------FPILLAAPTGRAAKRL 58
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
1911-2186 |
4.03e-05 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 48.01 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIEtayamvkhspSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQrkghsdenfnakIKQNRVLVCAPSNAAVD 1990
Cdd:pfam00580 2 NPEQRKAVT----------HLGGPLLVLAGAGSGKTRVLTERIAYLILEGG------------IDPEEILAVTFTNKAAR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1991 ELMKKIILEFKEKCKDkknplgncgdinlvrlgpeksintEVLKFSLDSqVNHRMKKDLPSHIQeMLRRKEILDaQLDel 2070
Cdd:pfam00580 60 EMKERILKLLGKAELS------------------------ELNISTFHS-FCLRILRKYANRIG-LLPNFSILD-ELD-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 2071 srQRALCRGGREMQRQELDEHI-------AIVS--KERQELASKIKEVQGRPQRAQNTIILESHV--------------- 2126
Cdd:pfam00580 111 --QLALLKELLEKDRLNLDPKLlrklelkELISkaKNRLLSPEELQQGAADPRDKLAAEFYQEYQerlkennaldfddll 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568913773 2127 -ICCTLSTSGGLLLEsAFRGQggvpFSCVIVDEAgQ---SCEVETLSPLIHRCNKLILVGDPKQ 2186
Cdd:pfam00580 189 lLTLELLRSDPELLE-AYRER----FKYILVDEF-QdtnPIQYRLLKLLAGGHENLFLVGDPDQ 246
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1936-2002 |
4.85e-05 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 45.17 E-value: 4.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568913773 1936 LIHGPPGTGKSKTIVGLLYRLLTenqrkghsdenfNAKIKQNRVLVCAPSNAAVDELMKKIILEFKE 2002
Cdd:cd17914 3 LIQGPPGTGKTRVLVKIVAALMQ------------NKNGEPGRILLVTPTNKAAAQLDNILVDEAAQ 57
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
2154-2212 |
2.01e-04 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 43.24 E-value: 2.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568913773 2154 VIVDEAGQSCEVET--LSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKL 2212
Cdd:cd17914 50 ILVDEAAQILEPETsrLIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRL 110
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1844-1999 |
2.25e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 46.51 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1844 PASVKNLTRCIVISSLVTTQRKLKAMSLLSSRNQLARAVLNPNPMDFCTKDLLTTTSERIVAYLKDFNEDQKKAIETAYA 1923
Cdd:COG0507 59 AEDIEAALAALVESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAALEPRAGITLSDEQREAVALALT 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913773 1924 MvkhspsvAKICLIHGPPGTGKSKTIVGLLyRLLTENQRkghsdenfnakikqnRVLVCAPSNAAVDELMKKIILE 1999
Cdd:COG0507 139 T-------RRVSVLTGGAGTGKTTTLRALL-AALEALGL---------------RVALAAPTGKAAKRLSESTGIE 191
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
1913-1996 |
1.43e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 41.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1913 DQKKAIETAyamVKHspsvaKICLIHGPPGTGKSKTIVGLLyrlltenqrkghsdENFNAKIKqnRVLVCAPSNAAVDEL 1992
Cdd:cd17933 1 EQKAAVRLV---LRN-----RVSVLTGGAGTGKTTTLKALL--------------AALEAEGK--RVVLAAPTGKAAKRL 56
|
....
gi 568913773 1993 MKKI 1996
Cdd:cd17933 57 SEST 60
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1911-1994 |
2.06e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 41.78 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913773 1911 NEDQKKAIETAYAmvkhspSVAKICLIHGPPGTGKSkTIVGLLyrlltenqRKGHSDENFnakikqnRVLVCAPSNAAVD 1990
Cdd:pfam13604 3 NAEQAAAVRALLT------SGDRVAVLVGPAGTGKT-TALKAL--------REAWEAAGY-------RVIGLAPTGRAAK 60
|
....
gi 568913773 1991 ELMK 1994
Cdd:pfam13604 61 VLGE 64
|
|
| |
