|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
9-349 |
2.48e-154 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 449.22 E-value: 2.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 9 RVSVLLPYPFDTPFTYAADEALP--PGTLVRVPLGARMAVGAVWSDPPDQGV---KTRPIAEIL-AFPPLPKPLMDFIDW 82
Cdd:PRK05580 4 IARVLLPVPLPRPFDYLIPEGLEvqPGDRVRVPFGNRKLIGVVVGVEEGSEVpadKLKPILEVLdLEPLLPPELLRLLDW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 83 VAGYTLAKRGEVLALALKESLLAAPP--------KRG--------KAFTFGEADPAHPGPTLSAAQAAAAQALRdsaAAQ 146
Cdd:PRK05580 84 AADYYLSPLGEVLRLALLAELALAASsavlkglvKKGlieleeveVLRLRPPPDPAFEPPTLNPEQAAAVEAIR---AAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 147 KFSVTLLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQG 226
Cdd:PRK05580 161 GFSPFLLDGVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQMLARFRARFGAPVAVLHSGLSDGERLDEWRKAKRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 227 RADVVVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRL 306
Cdd:PRK05580 241 EAKVVIGARSALFLPFKNLGLIIVDEEHDSSYKQQEGPRYHARDLAVVRAKLENIPVVLGSATPSLESLANAQQGRYRLL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1232327325 307 DLPARHGGAVLPRVSAVDLRAHPP-ERGKFLSPVLLEAVRETLA 349
Cdd:PRK05580 321 RLTKRAGGARLPEVEIIDMRELLRgENGSFLSPPLLEAIKQRLE 364
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
9-349 |
3.14e-145 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 427.23 E-value: 3.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 9 RVSVLLPYPFDTPFTYAADEALP---PGTLVRVPLGARMAVGAVWS---DPPDQGVKTRPIAEIL-AFPPLPKPLMDFID 81
Cdd:COG1198 3 IAEVALPVPLDRPFDYLVPEGLElvqPGSRVLVPFGRRQVVGIVVGlkeESDVDPAKLKPILAVLdDEPLLPEELLELLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 82 WVAGYTLAKRGEVLALAL------------------KESLLAAPPKRGKA------------------------------ 113
Cdd:COG1198 83 WVADYYLCPLGEVLRLALpaglrqgyparikteryvRLTLGEELPKRAPKqrrvlealrehggpltlselakeagvsrsv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 114 -------------------FTFGEADPAHPGPTLSAAQAAAAQALRdsAAAQKFSVTLLDGVTGSGKTEVYLEAVAQTLR 174
Cdd:COG1198 163 lkalvkkglleieerevdrDPFAPDVPAEPPPTLNEEQQAAVEAIR--AAAGGFSVFLLHGVTGSGKTEVYLQAIAEVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 175 ANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGRADVVVGARSALFLPFPALGLIVVDEEH 254
Cdd:COG1198 241 QGKQALVLVPEIALTPQTVERFRARFGARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRSALFAPFPNLGLIIVDEEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 255 ESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPARHGGAVLPRVSAVDLRAHPPERGK 334
Cdd:COG1198 321 DSSYKQEDGPRYHARDVAVVRAKLEGAPVVLGSATPSLESLYNAQKGRYRLLELPERAGGAPLPEVELVDMREEPLEGGR 400
|
410
....*....|....*
gi 1232327325 335 FLSPVLLEAVRETLA 349
Cdd:COG1198 401 ILSPPLLEAIEETLE 415
|
|
| priA |
TIGR00595 |
primosomal protein N'; All proteins in this family for which functions are known are ... |
152-349 |
1.29e-90 |
|
primosomal protein N'; All proteins in this family for which functions are known are components of the primosome which is involved in replication, repair, and recombination.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: 273162 [Multi-domain] Cd Length: 505 Bit Score: 280.42 E-value: 1.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGRADVV 231
Cdd:TIGR00595 1 LLFGVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRFGSQVAVLHSGLSDSEKLQAWRKVKNGEILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 232 VGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPAR 311
Cdd:TIGR00595 81 IGTRSALFLPFKNLGLIIVDEEHDSSYKQEEGPRYHARDVAVYRAKKFNCPVVLGSATPSLESYHNAKQKAYRLLVLTRR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1232327325 312 HGGAVLPRVSAVDLRAHPPErgKFLSPVLLEAVRETLA 349
Cdd:TIGR00595 161 VSGRKPPEVKLIDMRKEPRQ--SFLSPELITAIEQTLA 196
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
148-311 |
6.42e-85 |
|
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: 254.44 E-value: 6.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 148 FSVTLLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGR 227
Cdd:cd17929 15 FKTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGDKVAVLHSKLSDKERADEWRKIKRGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 228 ADVVVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLD 307
Cdd:cd17929 95 AKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPRYHARDVAIYRAKLENAPVVLGSATPSLESYYNAQQGKYRLLQ 174
|
....
gi 1232327325 308 LPAR 311
Cdd:cd17929 175 LTER 178
|
|
| PriA_3primeBD |
pfam17764 |
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in ... |
11-99 |
3.72e-21 |
|
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in the PriA protein. The 3'BD, which has been shown to bind the 3' end of the leading-strand arm of replication fork structures.
Pssm-ID: 465491 [Multi-domain] Cd Length: 96 Bit Score: 86.74 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 11 SVLLPYPFDTPFTYAADEAL--PPGTLVRVPLGARMAVGAVWS---DPPDQGVKTRPIAEIL-AFPPLPKPLMDFIDWVA 84
Cdd:pfam17764 1 EVAVPLPLDRPFDYRVPEELavKIGMRVLVPFGKRKVTGIVVGlseESEVDPEKLKPILEVLdEEPLLTPELLELARWMA 80
|
90
....*....|....*
gi 1232327325 85 GYTLAKRGEVLALAL 99
Cdd:pfam17764 81 EYYLCPLGEVLRAAL 95
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
143-298 |
2.97e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.47 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 143 AAAQKFSVTLLDGVTGSGKTEVYLEAVAQTLRANR--QALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETL 220
Cdd:smart00487 19 ALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 221 RAVAQGRADVVVGARSALF-------LPFPALGLIVVDEEHESafkqedGVMYNARDMAVVRARLSGAP-CVLVSATPSL 292
Cdd:smart00487 99 RKLESGKTDILVTTPGRLLdllendkLSLSNVDLVILDEAHRL------LDGGFGDQLEKLLKLLPKNVqLLLLSATPPE 172
|
....*.
gi 1232327325 293 ESVENA 298
Cdd:smart00487 173 EIENLL 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
9-349 |
2.48e-154 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 449.22 E-value: 2.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 9 RVSVLLPYPFDTPFTYAADEALP--PGTLVRVPLGARMAVGAVWSDPPDQGV---KTRPIAEIL-AFPPLPKPLMDFIDW 82
Cdd:PRK05580 4 IARVLLPVPLPRPFDYLIPEGLEvqPGDRVRVPFGNRKLIGVVVGVEEGSEVpadKLKPILEVLdLEPLLPPELLRLLDW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 83 VAGYTLAKRGEVLALALKESLLAAPP--------KRG--------KAFTFGEADPAHPGPTLSAAQAAAAQALRdsaAAQ 146
Cdd:PRK05580 84 AADYYLSPLGEVLRLALLAELALAASsavlkglvKKGlieleeveVLRLRPPPDPAFEPPTLNPEQAAAVEAIR---AAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 147 KFSVTLLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQG 226
Cdd:PRK05580 161 GFSPFLLDGVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQMLARFRARFGAPVAVLHSGLSDGERLDEWRKAKRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 227 RADVVVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRL 306
Cdd:PRK05580 241 EAKVVIGARSALFLPFKNLGLIIVDEEHDSSYKQQEGPRYHARDLAVVRAKLENIPVVLGSATPSLESLANAQQGRYRLL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1232327325 307 DLPARHGGAVLPRVSAVDLRAHPP-ERGKFLSPVLLEAVRETLA 349
Cdd:PRK05580 321 RLTKRAGGARLPEVEIIDMRELLRgENGSFLSPPLLEAIKQRLE 364
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
9-349 |
3.14e-145 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 427.23 E-value: 3.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 9 RVSVLLPYPFDTPFTYAADEALP---PGTLVRVPLGARMAVGAVWS---DPPDQGVKTRPIAEIL-AFPPLPKPLMDFID 81
Cdd:COG1198 3 IAEVALPVPLDRPFDYLVPEGLElvqPGSRVLVPFGRRQVVGIVVGlkeESDVDPAKLKPILAVLdDEPLLPEELLELLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 82 WVAGYTLAKRGEVLALAL------------------KESLLAAPPKRGKA------------------------------ 113
Cdd:COG1198 83 WVADYYLCPLGEVLRLALpaglrqgyparikteryvRLTLGEELPKRAPKqrrvlealrehggpltlselakeagvsrsv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 114 -------------------FTFGEADPAHPGPTLSAAQAAAAQALRdsAAAQKFSVTLLDGVTGSGKTEVYLEAVAQTLR 174
Cdd:COG1198 163 lkalvkkglleieerevdrDPFAPDVPAEPPPTLNEEQQAAVEAIR--AAAGGFSVFLLHGVTGSGKTEVYLQAIAEVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 175 ANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGRADVVVGARSALFLPFPALGLIVVDEEH 254
Cdd:COG1198 241 QGKQALVLVPEIALTPQTVERFRARFGARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRSALFAPFPNLGLIIVDEEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 255 ESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPARHGGAVLPRVSAVDLRAHPPERGK 334
Cdd:COG1198 321 DSSYKQEDGPRYHARDVAVVRAKLEGAPVVLGSATPSLESLYNAQKGRYRLLELPERAGGAPLPEVELVDMREEPLEGGR 400
|
410
....*....|....*
gi 1232327325 335 FLSPVLLEAVRETLA 349
Cdd:COG1198 401 ILSPPLLEAIEETLE 415
|
|
| priA |
TIGR00595 |
primosomal protein N'; All proteins in this family for which functions are known are ... |
152-349 |
1.29e-90 |
|
primosomal protein N'; All proteins in this family for which functions are known are components of the primosome which is involved in replication, repair, and recombination.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: 273162 [Multi-domain] Cd Length: 505 Bit Score: 280.42 E-value: 1.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGRADVV 231
Cdd:TIGR00595 1 LLFGVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRFGSQVAVLHSGLSDSEKLQAWRKVKNGEILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 232 VGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPAR 311
Cdd:TIGR00595 81 IGTRSALFLPFKNLGLIIVDEEHDSSYKQEEGPRYHARDVAVYRAKKFNCPVVLGSATPSLESYHNAKQKAYRLLVLTRR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1232327325 312 HGGAVLPRVSAVDLRAHPPErgKFLSPVLLEAVRETLA 349
Cdd:TIGR00595 161 VSGRKPPEVKLIDMRKEPRQ--SFLSPELITAIEQTLA 196
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
148-311 |
6.42e-85 |
|
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: 254.44 E-value: 6.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 148 FSVTLLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGR 227
Cdd:cd17929 15 FKTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGDKVAVLHSKLSDKERADEWRKIKRGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 228 ADVVVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLD 307
Cdd:cd17929 95 AKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPRYHARDVAIYRAKLENAPVVLGSATPSLESYYNAQQGKYRLLQ 174
|
....
gi 1232327325 308 LPAR 311
Cdd:cd17929 175 LTER 178
|
|
| PRK14873 |
PRK14873 |
primosomal protein N'; |
9-349 |
6.24e-24 |
|
primosomal protein N';
Pssm-ID: 237844 [Multi-domain] Cd Length: 665 Bit Score: 102.71 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 9 RVSVLLPYP-FDTPFTYAADEALP----PGTLVRVPLGARMAVGAVWS--DPPDQGVKTRPIAE-ILAFPPLPKPLMDFI 80
Cdd:PRK14873 15 RVLPDLGLPhLDRLFDYLVPEELSddaqPGVRVRVRFGGRLVDGFVLErrSDSDHEGKLRWLERvVSPEPVLTPEIRRLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 81 DWVAGYTLAKRGEVLALALkesllaaPPKRGKAftfgEADPAHPGPTLSAAQAAAAQALRDSAAAQKFSVTLLDGVT--- 157
Cdd:PRK14873 95 RAVADRYAGTRADVLRLAV-------PPRHARV----EKEPVATPPPPLTAPPPDPSGWAAYGRGPRFLAALAAGRAara 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 158 ------GSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGA-APAVWHSELTPAARRETLRAVAQGRADV 230
Cdd:PRK14873 164 vwqalpGEDWARRLAAAAAATLRAGRGALVVVPDQRDVDRLEAALRALLGAgDVAVLSAGLGPADRYRRWLAVLRGQARV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 231 VVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYNARDMAVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPA 310
Cdd:PRK14873 244 VVGTRSAVFAPVEDLGLVAIWDDGDDLLAEPRAPYPHAREVALLRAHQHGCALLIGGHARTAEAQALVESGWAHDLVAPR 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1232327325 311 RHGGAVLPRVSAV-----DLRAHPPERGKFLSPVLLEAVRETLA 349
Cdd:PRK14873 324 PVVRARAPRVRALgdsglALERDPAARAARLPSLAFRAARDALE 367
|
|
| PriA_3primeBD |
pfam17764 |
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in ... |
11-99 |
3.72e-21 |
|
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in the PriA protein. The 3'BD, which has been shown to bind the 3' end of the leading-strand arm of replication fork structures.
Pssm-ID: 465491 [Multi-domain] Cd Length: 96 Bit Score: 86.74 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 11 SVLLPYPFDTPFTYAADEAL--PPGTLVRVPLGARMAVGAVWS---DPPDQGVKTRPIAEIL-AFPPLPKPLMDFIDWVA 84
Cdd:pfam17764 1 EVAVPLPLDRPFDYRVPEELavKIGMRVLVPFGKRKVTGIVVGlseESEVDPEKLKPILEVLdEEPLLTPELLELARWMA 80
|
90
....*....|....*
gi 1232327325 85 GYTLAKRGEVLALAL 99
Cdd:pfam17764 81 EYYLCPLGEVLRAAL 95
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
143-298 |
2.97e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.47 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 143 AAAQKFSVTLLDGVTGSGKTEVYLEAVAQTLRANR--QALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETL 220
Cdd:smart00487 19 ALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 221 RAVAQGRADVVVGARSALF-------LPFPALGLIVVDEEHESafkqedGVMYNARDMAVVRARLSGAP-CVLVSATPSL 292
Cdd:smart00487 99 RKLESGKTDILVTTPGRLLdllendkLSLSNVDLVILDEAHRL------LDGGFGDQLEKLLKLLPKNVqLLLLSATPPE 172
|
....*.
gi 1232327325 293 ESVENA 298
Cdd:smart00487 173 EIENLL 178
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
152-291 |
9.42e-18 |
|
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: 79.59 E-value: 9.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANR---QALVLLPEIALSVQFLQRFERRFGAAPAVWHSELTPAARRETLRAVAqgRA 228
Cdd:pfam00270 18 LVQAPTGSGKTLAFLLPALEALDKLDngpQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKLK--GP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 229 DVVVGARSALFL------PFPALGLIVVDEEHESafkqedGVMYNARDMAVVRARL-SGAPCVLVSATPS 291
Cdd:pfam00270 96 DILVGTPGRLLDllqerkLLKNLKLLVLDEAHRL------LDMGFGPDLEEILRRLpKKRQILLLSATLP 159
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
149-289 |
5.61e-16 |
|
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: 73.98 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 149 SVTLLDGVTGSGKTEVYLEAVAQTLRANR-QALVLLPEIALSVQFLQRFERRF--GAAPAVWHSELTPaarrETLRAVAQ 225
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGkKVLVLVPTKALALQTAERLRELFgpGIRVAVLVGGSSA----EEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232327325 226 GRADVVVGARSALFLP--------FPALGLIVVDEEHESAFKQEDGVMYnarDMAVVRARLSGAPCVLVSAT 289
Cdd:cd00046 78 GDADIIIATPDMLLNLllredrlfLKDLKLIIVDEAHALLIDSRGALIL---DLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
152-290 |
7.12e-15 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 72.22 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAP---AVWHSELTPAARRETLRAVAQGRA 228
Cdd:cd17991 40 LICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFANFPvnvELLSRFTTAAEQREILEGLKEGKV 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232327325 229 DVVVGARSALF--LPFPALGLIVVDEEHEsaFkqedGVMYNARdmavVRARLSGAPCVLVSATP 290
Cdd:cd17991 120 DIVIGTHRLLSkdVEFKNLGLLIIDEEQR--F----GVKQKEK----LKELRPNVDVLTLSATP 173
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
158-290 |
1.91e-10 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 61.99 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 158 GSGKTEVYLEAVAQTLRANRQALVLLP-EIaLSVQFLQRFERRFGAA--PAVWhseLT----PAARRETLRAVAQGRADV 230
Cdd:COG1200 290 GSGKTVVALLAMLAAVEAGYQAALMAPtEI-LAEQHYRSLSKLLEPLgiRVAL---LTgstkAKERREILAALASGEADI 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232327325 231 VVGARsALF---LPFPALGLIVVDEEHEsaFkqedGVMYnardmavvRARLSG---APCVLV-SATP 290
Cdd:COG1200 366 VVGTH-ALIqddVEFKNLGLVVIDEQHR--F----GVEQ--------RLALREkgeAPHVLVmTATP 417
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
152-290 |
3.36e-10 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 59.47 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLP-EIaLSVQFLQRFERRFGAAP---AVWHSELTPAARRETLRAVAQGR 227
Cdd:cd17992 70 LLQGDVGSGKTVVAALAMLAAVENGYQVALMAPtEI-LAEQHYDSLKKLLEPLGirvALLTGSTKAKEKREILEKIASGE 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 228 ADVVVGARsALF---LPFPALGLIVVDEEHESAFKQedgvmynardmavvRARLS---GAPCVLV-SATP 290
Cdd:cd17992 149 IDIVIGTH-ALIqedVEFHNLGLVIIDEQHRFGVEQ--------------RLKLRekgETPHVLVmTATP 203
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
152-290 |
1.12e-09 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 57.04 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFgaaPAVwHSELTPAARRETLRAvaqgRADVV 231
Cdd:cd17918 40 LLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFL---PFI-NVELVTGGTKAQILS----GISLL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232327325 232 VGARSALFL--PFPALGLIVVDEEHESAFKQEDGvMYNARDMAVVRArlsgapcvlvSATP 290
Cdd:cd17918 112 VGTHALLHLdvKFKNLDLVIVDEQHRFGVAQREA-LYNLGATHFLEA----------TATP 161
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
152-290 |
4.53e-08 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 54.77 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLP-EIaLSVQ---FLQRFERRFGAAPAVWHSELTPAARRETLRAVAQGR 227
Cdd:PRK10917 286 LLQGDVGSGKTVVAALAALAAIEAGYQAALMAPtEI-LAEQhyeNLKKLLEPLGIRVALLTGSLKGKERREILEAIASGE 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 228 ADVVVGARsALF---LPFPALGLIVVDEEHEsaFkqedGVMYnardmavvRARLS---GAPCVLV-SATP 290
Cdd:PRK10917 365 ADIVIGTH-ALIqddVEFHNLGLVIIDEQHR--F----GVEQ--------RLALRekgENPHVLVmTATP 419
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
156-349 |
7.23e-08 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 53.72 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 156 VTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAP-AVWHSELTPAARretlravaqgRADVVVGA 234
Cdd:COG4098 137 VCGAGKTEMLFPAIAEALKQGGRVCIATPRVDVVLELAPRLQQAFPGVDiAALYGGSEEKYR----------YAQLVIAT 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 235 RSALfLPF-PALGLIVVDEehESAFKqedgvmYNARDM---AVVRARLSGAPCVLVSATPSLESVENAASGRYTRLDLPA 310
Cdd:COG4098 207 THQL-LRFyQAFDLLIIDE--VDAFP------YSGDPMlqyAVKRARKPDGKLIYLTATPSKALQRQVKRGKLKVVKLPA 277
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1232327325 311 RHGGAVLP---RVSAVDLRaHPPERGKfLSPVLLEAVRETLA 349
Cdd:COG4098 278 RYHGHPLPvpkFKWLGNWK-KRLRRGK-LPRKLLKWLKKRLK 317
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
152-259 |
9.60e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.05 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRAN--RQALVLLPEIALSVQFLQRFERRFGA---APAVWHSELTPAARREtlravaqg 226
Cdd:pfam04851 27 LIVMATGSGKTLTAAKLIARLFKKGpiKKVLFLVPRKDLLEQALEEFKKFLPNyveIGEIISGDKKDESVDD-------- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1232327325 227 rADVVVGARSALFLPFP---------ALGLIVVDEEHESAFK 259
Cdd:pfam04851 99 -NKIVVTTIQSLYKALElaslellpdFFDVIIIDEAHRSGAS 139
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
152-254 |
4.83e-06 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 48.59 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 152 LLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRFGAAPAvwHSELTP---AARRET--LRAVAQG 226
Cdd:PRK10689 625 LVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPV--RIEMLSrfrSAKEQTqiLAEAAEG 702
|
90 100 110
....*....|....*....|....*....|
gi 1232327325 227 RADVVVGARSALF--LPFPALGLIVVDEEH 254
Cdd:PRK10689 703 KIDILIGTHKLLQsdVKWKDLGLLIVDEEH 732
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
157-290 |
1.16e-05 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 46.94 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVYLEAVAQTLRANRqALVLLPEIALSVQFLQRFERRFGAAPAVwhseltpAARRETlravaqgRADVVV---- 232
Cdd:COG1061 109 TGTGKTVLALALAAELLRGKR-VLVLVPRRELLEQWAEELRRFLGDPLAG-------GGKKDS-------DAPITVatyq 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 233 --GARSALFLPFPALGLIVVDEEHESAfkqedgvmynARDMAVVRARLSGAPCVLVSATP 290
Cdd:COG1061 174 slARRAHLDELGDRFGLVIIDEAHHAG----------APSYRRILEAFPAAYRLGLTATP 223
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
151-289 |
6.65e-05 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain] Cd Length: 143 Bit Score: 42.29 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 151 TLLDGVTGSGKTEVYLEAVAQTLRANRQALVLLPEIALSVQFLQRFERRF-GAAPAVWHseltpAARRETLRavaqgRAD 229
Cdd:cd17925 19 LLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFpGAAIVLLH-----GGSEDQYQ-----RSP 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 230 VVVGARSALFLPFPALGLIVVDEEHESAFKQEDGVMYnardmAVVRARLSGAPCVLVSAT 289
Cdd:cd17925 89 LVIATTHQLLRFYRAFDLLIIDEVDAFPYAGDPMLYY-----AVEKARKEEGSLIYLTAT 143
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
157-254 |
7.38e-05 |
|
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: 43.01 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVY-LEAVAQTLRANRQALVLLPEIAL---SVQFLQRFERrfgaaPAVWHSELTPAARRETLRAVAQGRADVV- 231
Cdd:cd18018 36 TGAGKSLCYqLPALLLRRRGPGLTLVVSPLIALmkdQVDALPRAIK-----AAALNSSLTREERRRILEKLRAGEVKILy 110
|
90 100 110
....*....|....*....|....*....|.
gi 1232327325 232 --------VGARSALFLPfPALGLIVVDEEH 254
Cdd:cd18018 111 vsperlvnESFRELLRQT-PPISLLVVDEAH 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
157-289 |
4.81e-04 |
|
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: 40.65 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVY----LEAVAQtlRANRQALVLLPEIALSVQFLQRFERR-----FGAAPAVWHSElTPAARRetlRAVAQGR 227
Cdd:cd17923 24 TASGKSLCYqlpiLEALLR--DPGSRALYLYPTKALAQDQLRSLRELleqlgLGIRVATYDGD-TPREER---RAIIRNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 228 ADVVV-------------GARSALFLpfPALGLIVVDEEHesafkqedgvMYNAR---DMAVVRARL--------SGAPC 283
Cdd:cd17923 98 PRILLtnpdmlhyallphHDRWARFL--RNLRYVVLDEAH----------TYRGVfgsHVALLLRRLrrlcrrygADPQF 165
|
....*.
gi 1232327325 284 VLVSAT 289
Cdd:cd17923 166 ILTSAT 171
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
160-254 |
6.50e-04 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 41.59 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 160 GKTEVyleavAqtLRA-------NRQALVLLPEIALSVQFLQRFERRFGAAP---AVwhseL----TPAARRETLRAVAQ 225
Cdd:COG1197 619 GKTEV-----A--LRAafkavmdGKQVAVLVPTTLLAQQHYETFKERFAGFPvrvEV----LsrfrTAKEQKETLEGLAD 687
|
90 100 110
....*....|....*....|....*....|..
gi 1232327325 226 GRADVVVGArSALFLP---FPALGLIVVDEEH 254
Cdd:COG1197 688 GKVDIVIGT-HRLLSKdvkFKDLGLLIIDEEQ 718
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
157-289 |
9.91e-04 |
|
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: 39.83 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVY-LEAVAqtlrANRQALVLLPEIAL---SVQFLQRFerrfGAAPAVWHSELTPAARRETLRAVAQGRADVV- 231
Cdd:cd17920 36 TGGGKSLCYqLPALL----LDGVTLVVSPLISLmqdQVDRLQQL----GIRAAALNSTLSPEEKREVLLRIKNGQYKLLy 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232327325 232 VG---ARSALFLPF-------PALGLIVVDEEH---------ESAFKQedgvmynardMAVVRARLSGAPCVLVSAT 289
Cdd:cd17920 108 VTperLLSPDFLELlqrlperKRLALIVVDEAHcvsqwghdfRPDYLR----------LGRLRRALPGVPILALTAT 174
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
157-254 |
1.44e-03 |
|
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: 39.17 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVYLEAVAQTLRANRQ-ALVLLPEIALSVQFLQRFERRFGAAPAVwHSELTPAarrETLRAVAQGRADVVV--- 232
Cdd:cd17921 26 TSSGKTLIAELAILRALATSGGkAVYIAPTRALVNQKEADLRERFGPLGKN-VGLLTGD---PSVNKLLLAEADILVatp 101
|
90 100 110
....*....|....*....|....*....|
gi 1232327325 233 --------GARSALFLPfpaLGLIVVDEEH 254
Cdd:cd17921 102 ekldlllrNGGERLIQD---VRLVVVDEAH 128
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
157-254 |
1.69e-03 |
|
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: 40.20 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVYLEAVAQTLRANRQ--ALVLLPEIALS---VQFLQRFERRFGAA--PAVWHSElTPAARRETLRAvaqgRAD 229
Cdd:COG1205 80 TASGKSLAYLLPVLEALLEDPGatALYLYPTKALArdqLRRLRELAEALGLGvrVATYDGD-TPPEERRWIRE----HPD 154
|
90 100 110
....*....|....*....|....*....|....*...
gi 1232327325 230 VVV-------------GARSALFlpFPALGLIVVDEEH 254
Cdd:COG1205 155 IVLtnpdmlhygllphHTRWARF--FRNLRYVVIDEAH 190
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
157-290 |
2.72e-03 |
|
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: 37.67 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327325 157 TGSGKTEVYLeAVAQTLRANRqALVLLPEIALSVQFLQRFERRFGAApavwhseltPAARRETLRAVAQGRADVVVGARS 236
Cdd:cd17926 27 TGSGKTLTAL-ALIAYLKELR-TLIVVPTDALLDQWKERFEDFLGDS---------SIGLIGGGKKKDFDDANVVVATYQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232327325 237 ALF-------LPFPALGLIVVDEEHEsafkqedgvmYNARDMAVVRARLSGAPCVLVSATP 290
Cdd:cd17926 96 SLSnlaeeekDLFDQFGLLIVDEAHH----------LPAKTFSEILKELNAKYRLGLTATP 146
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