|
Name |
Accession |
Description |
Interval |
E-value |
| ERI-1_3'hExo_like |
cd06133 |
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ... |
50-243 |
8.81e-82 |
|
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.
Pssm-ID: 99836 [Multi-domain] Cd Length: 176 Bit Score: 257.15 E-value: 8.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 50 LIIIDFESTCWKDGKR-HYSQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNICLS 128
Cdd:cd06133 1 YLVIDFEATCWEGNSKpDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 129 QFSKWIQKIQKekkiifnsdvsshsvseaksSTFVTWSDWDLGVCLQYECKRKQLRKPDILNSWIDLRATYKLFY-TRKP 207
Cdd:cd06133 81 EFLEWLGKNGK--------------------YAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYgLKKR 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 2113270554 208 KGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMI 243
Cdd:cd06133 141 TGLSKALEYLGLEFEGRHHRGLDDARNIARILKRLL 176
|
|
| KapD |
COG5018 |
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ... |
48-246 |
7.23e-52 |
|
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];
Pssm-ID: 444042 [Multi-domain] Cd Length: 181 Bit Score: 177.74 E-value: 7.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 48 DYLIIIDFESTCW-KDGKRHYSQEIIEFPAVLLNtSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNIC 126
Cdd:COG5018 2 MKYLVIDLEATCWdGKPPPGFPMEIIEIGAVKVD-ENGEIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 127 LSQFSKWIqkiqkekkiifnsdvsshsvsEAKSSTFVTWSDWDLGVcLQYECKRKQLrKPDILNSWIDLRATYKLFY-TR 205
Cdd:COG5018 81 IEDFKKWI---------------------GSEDYILCSWGDYDRKQ-LERNCRFHGV-PYPFGDRHINLKKLFALYFgLK 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2113270554 206 KPKGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMICDG 246
Cdd:COG5018 138 KRIGLKKALELLGLEFEGTHHRALDDARNTAKLFKKILGDK 178
|
|
| PTZ00315 |
PTZ00315 |
2'-phosphotransferase; Provisional |
45-322 |
6.50e-29 |
|
2'-phosphotransferase; Provisional
Pssm-ID: 240356 [Multi-domain] Cd Length: 582 Bit Score: 122.31 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 45 QLFDYLIIIDFESTCWKDgKRHYSQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVD--EGVP 122
Cdd:PTZ00315 53 QPFDAYVVLDFEATCEAD-RRIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSraDPFP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 123 LNICLS-QFskwiqkiqkekkiifnsdVSSHSVSEA---KSSTFVTWSDWDLGVCLQYECK-RKQLRKPDILNSWIDLRA 197
Cdd:PTZ00315 132 VVYCEAlQF------------------LAEAGLGDApplRSYCVVTCGDWDLKTMLPSQMRvSGQQGTPLSFQRWCNLKK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 198 TYKLFYTRK-------------PKGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMICDGCVMKITRSLDKVQPKKNS 264
Cdd:PTZ00315 194 YMSQLGFGNgsgcgggatpplgPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPTFDTAPFRRWHAP 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113270554 265 VSRSLNVnpTEENPLGSDDGAEtsdkdrICNSSCPAENEHNKLDKMDINSSVKGKDQQ 322
Cdd:PTZ00315 274 TEASLPA--LDALPSTLADGAA------QHSRDCREPGRRHARTEGDARASDTVNNQQ 323
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
51-238 |
1.07e-28 |
|
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;
Pssm-ID: 395743 [Multi-domain] Cd Length: 164 Bit Score: 112.44 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 51 IIIDFESTCWKDGKrhysQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNICLSQF 130
Cdd:pfam00929 1 VVIDLETTGLDPEK----DEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 131 SKWIQKIQKEKKiifnsdvssHSVseaksSTFVTWSDWDLGVCLQYECKrkqlRKPDILNSWIDLRATYKLFYTRkpkGL 210
Cdd:pfam00929 77 LEFLRKGNLLVA---------HNA-----SFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPGR---SL 135
|
170 180
....*....|....*....|....*...
gi 2113270554 211 NGALQDLGIEFAGREHSGLDDSRNTARL 238
Cdd:pfam00929 136 DALAEKLGLEHIGRAHRALDDARATAKL 163
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
49-238 |
2.14e-24 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 100.45 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 49 YLIIIDFESTCWKDGKrhysQEIIEFPAVllNTSTGEIESEFHMYVQPQEHpiLSEFCTELTGIKQNQVDEGVPLNICLS 128
Cdd:smart00479 1 TLVVIDCETTGLDPGK----DEIIEIAAV--DVDGGEIIEVFDTYVKPDRP--ITDYATEIHGITPEMLDDAPTFEEVLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 129 QFSKWIQKiqkEKKIIFNSdvsshsvseaksstfvtwSDWDLGVcLQYECKRKQLRKPdILNSWIDLRATYKLFYTRKPK 208
Cdd:smart00479 73 ELLEFLRG---RILVAGNS------------------AHFDLRF-LKLEHPRLGIKQP-PKLPVIDTLKLARATNPGLPK 129
|
170 180 190
....*....|....*....|....*....|.
gi 2113270554 209 -GLNGALQDLGIEFAGREHSGLDDSRNTARL 238
Cdd:smart00479 130 ySLKKLAKRLLLEVIQRAHRALDDARATAKL 160
|
|
| zf-GRF |
pfam06839 |
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ... |
617-662 |
2.74e-14 |
|
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.
Pssm-ID: 462017 Cd Length: 45 Bit Score: 67.43 E-value: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2113270554 617 PLCNCGRRAKRLNVSSAGPNHGKVFYSCPVgkheGKKRGCGYFKWE 662
Cdd:pfam06839 1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPV----GREKQCGFFQWA 42
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ERI-1_3'hExo_like |
cd06133 |
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ... |
50-243 |
8.81e-82 |
|
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.
Pssm-ID: 99836 [Multi-domain] Cd Length: 176 Bit Score: 257.15 E-value: 8.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 50 LIIIDFESTCWKDGKR-HYSQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNICLS 128
Cdd:cd06133 1 YLVIDFEATCWEGNSKpDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 129 QFSKWIQKIQKekkiifnsdvsshsvseaksSTFVTWSDWDLGVCLQYECKRKQLRKPDILNSWIDLRATYKLFY-TRKP 207
Cdd:cd06133 81 EFLEWLGKNGK--------------------YAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYgLKKR 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 2113270554 208 KGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMI 243
Cdd:cd06133 141 TGLSKALEYLGLEFEGRHHRGLDDARNIARILKRLL 176
|
|
| KapD |
COG5018 |
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ... |
48-246 |
7.23e-52 |
|
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];
Pssm-ID: 444042 [Multi-domain] Cd Length: 181 Bit Score: 177.74 E-value: 7.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 48 DYLIIIDFESTCW-KDGKRHYSQEIIEFPAVLLNtSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNIC 126
Cdd:COG5018 2 MKYLVIDLEATCWdGKPPPGFPMEIIEIGAVKVD-ENGEIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 127 LSQFSKWIqkiqkekkiifnsdvsshsvsEAKSSTFVTWSDWDLGVcLQYECKRKQLrKPDILNSWIDLRATYKLFY-TR 205
Cdd:COG5018 81 IEDFKKWI---------------------GSEDYILCSWGDYDRKQ-LERNCRFHGV-PYPFGDRHINLKKLFALYFgLK 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2113270554 206 KPKGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMICDG 246
Cdd:COG5018 138 KRIGLKKALELLGLEFEGTHHRALDDARNTAKLFKKILGDK 178
|
|
| PTZ00315 |
PTZ00315 |
2'-phosphotransferase; Provisional |
45-322 |
6.50e-29 |
|
2'-phosphotransferase; Provisional
Pssm-ID: 240356 [Multi-domain] Cd Length: 582 Bit Score: 122.31 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 45 QLFDYLIIIDFESTCWKDgKRHYSQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVD--EGVP 122
Cdd:PTZ00315 53 QPFDAYVVLDFEATCEAD-RRIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSraDPFP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 123 LNICLS-QFskwiqkiqkekkiifnsdVSSHSVSEA---KSSTFVTWSDWDLGVCLQYECK-RKQLRKPDILNSWIDLRA 197
Cdd:PTZ00315 132 VVYCEAlQF------------------LAEAGLGDApplRSYCVVTCGDWDLKTMLPSQMRvSGQQGTPLSFQRWCNLKK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 198 TYKLFYTRK-------------PKGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMICDGCVMKITRSLDKVQPKKNS 264
Cdd:PTZ00315 194 YMSQLGFGNgsgcgggatpplgPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPTFDTAPFRRWHAP 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113270554 265 VSRSLNVnpTEENPLGSDDGAEtsdkdrICNSSCPAENEHNKLDKMDINSSVKGKDQQ 322
Cdd:PTZ00315 274 TEASLPA--LDALPSTLADGAA------QHSRDCREPGRRHARTEGDARASDTVNNQQ 323
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
51-238 |
1.07e-28 |
|
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;
Pssm-ID: 395743 [Multi-domain] Cd Length: 164 Bit Score: 112.44 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 51 IIIDFESTCWKDGKrhysQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVPLNICLSQF 130
Cdd:pfam00929 1 VVIDLETTGLDPEK----DEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 131 SKWIQKIQKEKKiifnsdvssHSVseaksSTFVTWSDWDLGVCLQYECKrkqlRKPDILNSWIDLRATYKLFYTRkpkGL 210
Cdd:pfam00929 77 LEFLRKGNLLVA---------HNA-----SFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPGR---SL 135
|
170 180
....*....|....*....|....*...
gi 2113270554 211 NGALQDLGIEFAGREHSGLDDSRNTARL 238
Cdd:pfam00929 136 DALAEKLGLEHIGRAHRALDDARATAKL 163
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
49-238 |
2.14e-24 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 100.45 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 49 YLIIIDFESTCWKDGKrhysQEIIEFPAVllNTSTGEIESEFHMYVQPQEHpiLSEFCTELTGIKQNQVDEGVPLNICLS 128
Cdd:smart00479 1 TLVVIDCETTGLDPGK----DEIIEIAAV--DVDGGEIIEVFDTYVKPDRP--ITDYATEIHGITPEMLDDAPTFEEVLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 129 QFSKWIQKiqkEKKIIFNSdvsshsvseaksstfvtwSDWDLGVcLQYECKRKQLRKPdILNSWIDLRATYKLFYTRKPK 208
Cdd:smart00479 73 ELLEFLRG---RILVAGNS------------------AHFDLRF-LKLEHPRLGIKQP-PKLPVIDTLKLARATNPGLPK 129
|
170 180 190
....*....|....*....|....*....|.
gi 2113270554 209 -GLNGALQDLGIEFAGREHSGLDDSRNTARL 238
Cdd:smart00479 130 ySLKKLAKRLLLEVIQRAHRALDDARATAKL 160
|
|
| PRK07748 |
PRK07748 |
3'-5' exonuclease KapD; |
50-246 |
6.13e-22 |
|
3'-5' exonuclease KapD;
Pssm-ID: 236087 Cd Length: 207 Bit Score: 94.37 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 50 LIIIDFESTCwKDGKRH---YSQEIIEFPAVllNTSTGEIESEFHMYVQPQEHPILSEFCTELTGIKQNQVDEGVplnic 126
Cdd:PRK07748 6 FLFLDFEFTM-PQHKKKpkgFFPEIIEVGLV--SVVGCEVEDTFSSYVKPKTFPSLTERCKSFLGITQEDVDKGI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 127 lsQFSKWIQKIQKekkiifnsdvsshsVSEAKSSTFVTWSDWDLGVcLQYECKRKQLRKPdILNSWIDLRATYKLFYT-R 205
Cdd:PRK07748 78 --SFEELVEKLAE--------------YDKRCKPTIVTWGNMDMKV-LKHNCEKAGVPFP-FKGQCRDLSLEYKKFFGeR 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2113270554 206 KPKGLNGALQDLGIEFAGREHSGLDDSRNTARLAWRMICDG 246
Cdd:PRK07748 140 NQTGLWKAIEEYGKEGTGKHHCALDDAMTTYNIFKLVEKDK 180
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
50-243 |
1.74e-15 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 74.44 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 50 LIIIDFESTcwkdGKRHYSQEIIEFPAVLLNTstGEIESEFHMYVQPQEHpiLSEFCTELTGIKQNQVDEGVPLNICLSQ 129
Cdd:COG0847 2 FVVLDTETT----GLDPAKDRIIEIGAVKVDD--GRIVETFHTLVNPERP--IPPEATAIHGITDEDVADAPPFAEVLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 130 FSKWIQkiqkekkiifNSDVSSHSVSeaksstFvtwsdwDLGVcLQYECKRKQLRKPDilNSWIDLRATYKLFYTRKPK- 208
Cdd:COG0847 74 LLEFLG----------GAVLVAHNAA------F------DLGF-LNAELRRAGLPLPP--FPVLDTLRLARRLLPGLPSy 128
|
170 180 190
....*....|....*....|....*....|....*
gi 2113270554 209 GLNGALQDLGIEFAGReHSGLDDSRNTARLAWRMI 243
Cdd:COG0847 129 SLDALCERLGIPFDER-HRALADAEATAELFLALL 162
|
|
| zf-GRF |
pfam06839 |
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ... |
617-662 |
2.74e-14 |
|
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.
Pssm-ID: 462017 Cd Length: 45 Bit Score: 67.43 E-value: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2113270554 617 PLCNCGRRAKRLNVSSAGPNHGKVFYSCPVgkheGKKRGCGYFKWE 662
Cdd:pfam06839 1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPV----GREKQCGFFQWA 42
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
51-238 |
1.41e-13 |
|
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.
Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 68.87 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 51 IIIDFESTcwkdGKRHYSQEIIEFPAVLLNTStGEIESEFHMYVQPQEhPIlSEFCTELTGIKQNQVDEGVPLNICLSQF 130
Cdd:cd06127 1 VVFDTETT----GLDPKKDRIIEIGAVKVDGG-IEIVERFETLVNPGR-PI-PPEATAIHGITDEMLADAPPFEEVLPEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 131 SKWIqkiqkekkiifnsdvsshsvseaKSSTFVTW-SDWDLGVcLQYECKRKQLRKPDilNSWIDLRATYKLFYTRKPKG 209
Cdd:cd06127 74 LEFL-----------------------GGRVLVAHnASFDLRF-LNRELRRLGGPPLP--NPWIDTLRLARRLLPGLRSH 127
|
170 180 190
....*....|....*....|....*....|.
gi 2113270554 210 LNGAL--QDLGIEFAGReHSGLDDSRNTARL 238
Cdd:cd06127 128 RLGLLlaERYGIPLEGA-HRALADALATAEL 157
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
70-243 |
1.24e-11 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 68.33 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 70 EIIEFPAVLLNTstGEIESEFHMYVQPQEHpiLSEFCTELTGIKQNQVDEGVPLNICLSQFSKWIQKiqkekkiifnsdv 149
Cdd:PRK00448 437 EIIEIGAVKIKN--GEIIDKFEFFIKPGHP--LSAFTTELTGITDDMVKDAPSIEEVLPKFKEFCGD------------- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 150 sshSVSEAKSSTFvtwsdwDLGvCLQYECKRKQLRKPDilNSWID-LRATYKLFYTRKPKGLNGALQDLGIEFAgREHSG 228
Cdd:PRK00448 500 ---SILVAHNASF------DVG-FINTNYEKLGLEKIK--NPVIDtLELSRFLYPELKSHRLNTLAKKFGVELE-HHHRA 566
|
170
....*....|....*
gi 2113270554 229 LDDSRNTARLAWRMI 243
Cdd:PRK00448 567 DYDAEATAYLLIKFL 581
|
|
| PRK06722 |
PRK06722 |
exonuclease; Provisional |
49-238 |
1.82e-07 |
|
exonuclease; Provisional
Pssm-ID: 180670 [Multi-domain] Cd Length: 281 Bit Score: 53.13 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 49 YLIIIDFESTcWKDGKRHYSQEIIEFPAVLLNTSTGEIESEFHMYVQPQEHpiLSEFCTELTGIKQNQvdegvplnicLS 128
Cdd:PRK06722 6 HFIVFDIERN-FRPYKSEDPSEIVDIGAVKIEASTMKVIGEFSELVKPGAR--LTRHTTKLTGITKKD----------LI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 129 QFSKWIQKIQKEKKIIfnsdvsshsvseAKSSTFVTWSDWDLGVcLQYECKRKQLRKPDI-LNSWIDLRA----TYKLFY 203
Cdd:PRK06722 73 GVEKFPQIIEKFIQFI------------GEDSIFVTWGKEDYRF-LSHDCTLHSVECPCMeKERRIDLQKfvfqAYEELF 139
|
170 180 190
....*....|....*....|....*....|....*
gi 2113270554 204 TRKPKgLNGALQDLGIEFAGREHSGLDDSRNTARL 238
Cdd:PRK06722 140 EHTPS-LQSAVEQLGLIWEGKQHRALADAENTANI 173
|
|
| PRK08074 |
PRK08074 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
51-123 |
3.22e-04 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236148 [Multi-domain] Cd Length: 928 Bit Score: 44.17 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113270554 51 IIIDFEST--CWKDGKRhysqeIIEFPAVLLntSTGEIESEFHMYVQPqEHPIlSEFCTELTGIKQNQVdEGVPL 123
Cdd:PRK08074 6 VVVDLETTgnSPKKGDK-----IIQIAAVVV--EDGEILERFSSFVNP-ERPI-PPFITELTGISEEMV-KQAPL 70
|
|
| DUF730 |
pfam05325 |
Protein of unknown function (DUF730); This family consists of several uncharacterized ... |
610-666 |
7.47e-04 |
|
Protein of unknown function (DUF730); This family consists of several uncharacterized Arabidopsis thaliana proteins of unknown function.
Pssm-ID: 114071 Cd Length: 122 Bit Score: 40.13 E-value: 7.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113270554 610 KSDKLTPPLCNCGrrAKRLNVSSAGP-NHGKVFYSCPVGKHEGKKRGCGYFKWEHVLL 666
Cdd:pfam05325 14 RRDKGVPIECDCN--AKVVVATSRDPvTSGKLYFSCPYEISDGPGRGCGFKRWWTVAL 69
|
|
| PRK07740 |
PRK07740 |
hypothetical protein; Provisional |
51-240 |
2.42e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236085 [Multi-domain] Cd Length: 244 Bit Score: 40.42 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 51 IIIDFESTCWkdgkrhYSQ---EIIEFPAVllNTSTGEIESE-FHMYVQPqEHPIlSEFCTELTGIKQNQVDEGVPLNIC 126
Cdd:PRK07740 62 VVFDLETTGF------SPQqgdEILSIGAV--KTKGGEVETDtFYSLVKP-KRPI-PEHILELTGITAEDVAFAPPLAEV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 127 LSQFSKWIqkiqkEKKIIfnsdVSSHSVSEAKSSTFVTWsdwdlgvclqyeckrKQLRKPdILNSWIDLRATYKLFYtrk 206
Cdd:PRK07740 132 LHRFYAFI-----GAGVL----VAHHAGHDKAFLRHALW---------------RTYRQP-FTHRLIDTMFLTKLLA--- 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 2113270554 207 PKGLNGALQDL----GIEFAGReHSGLDDSRNTARLaW 240
Cdd:PRK07740 184 HERDFPTLDDAlayyGIPIPRR-HHALGDALMTAKL-W 219
|
|
| PRK06807 |
PRK06807 |
3'-5' exonuclease; |
42-134 |
7.34e-03 |
|
3'-5' exonuclease;
Pssm-ID: 235864 [Multi-domain] Cd Length: 313 Bit Score: 39.03 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113270554 42 KSRQLFDYLIIIDFESTcwkdGKRHYSQEIIEFPAVllNTSTGEIESEFHMYVQPqEHPILSEFcTELTGIKQNQVDEGV 121
Cdd:PRK06807 2 GNISLPLDYVVIDFETT----GFNPYNDKIIQVAAV--KYRNHELVDQFVSYVNP-ERPIPDRI-TSLTGITNYRVSDAP 73
|
90
....*....|...
gi 2113270554 122 PLNICLSQFSKWI 134
Cdd:PRK06807 74 TIEEVLPLFLAFL 86
|
|
|