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Conserved domains on  [gi|145199237|ref|NP_065746|]
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RNA exonuclease 1 homolog [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EloA-BP1 pfam15870
ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically ...
802-960 3.31e-86

ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically between 144 and 167 amino acids in length.


:

Pssm-ID: 464914  Cd Length: 163  Bit Score: 276.56  E-value: 3.31e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   802 KPIIPKEFGGKVPTVIRQRYLNLFIEECLKFCTSNQEAIEKALNEEKVAYDRSPSKNIYLNVAVNTLKKLRGLAPSAVPG 881
Cdd:pfam15870    1 RPVIPTEFGSKVPTNIRQRYLNLFIDECLKICTSEQEAFERALEEEKAVYDRCSSKNIYLNVAVNTLKKLRKEVPSQSSA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   882 LSKT----SGRRVVSHEVVLGGRLAAKTSFSLSRPSSPRVEDLKGAALYSRLREYLLTQDQLKENGYPFPHPERPGGAII 957
Cdd:pfam15870   81 VTKSsaisSNNKVVSHEAVLGGKLAAKTSFSINRNSKSIEEDLKGATLYRMLKEYLLTEEQLKENGYPRPHPDKPGRAVL 160

                   ...
gi 145199237   958 FTA 960
Cdd:pfam15870  161 FTA 163
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
1061-1209 2.21e-78

DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They 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. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T.


:

Pssm-ID: 99848  Cd Length: 150  Bit Score: 254.33  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1061 YALDCEMSYTTYGLELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADTSVTLRDVQAVLLSMFSADTILI 1140
Cdd:cd06145     1 FALDCEMCYTTDGLELTRVTVVDENGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVTTTLEDVQKKLLSLISPDTILV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145199237 1141 GHSLESDLLALKVIHSTVVDTSVLFPHRLGLPYKRSLRNLMADYLRQIIQDNVDGHSSSEDAGACMHLV 1209
Cdd:cd06145    81 GHSLENDLKALKLIHPRVIDTAILFPHPRGPPYKPSLKNLAKKYLGRDIQQGEGGHDSVEDARAALELV 149
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
400-688 5.48e-05

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  400 KDKGRGRPVEKPRADKKGPQASSPrrkaERPEGTKKKPSSATPVATSGKGRPDRPARRPSPTsgdsRPAAGRGPPRPLQL 479
Cdd:PTZ00449  583 KDPKHPKDPEEPKKPKRPRSAQRP----TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQ----RPSSPERPEGPKII 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  480 PDRKSTKAPSGKLVERKARSLDEGASQDAPKLKKRALSHADLFGDES---EDEAAGPGVPSVWPSALPSLSSDSDSDSDS 556
Cdd:PTZ00449  655 KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESilkETLPETPGTPFTTPRPLPPKLPRDEEFPFE 734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  557 SLGFPEAQGP-------PKRLKASPPPSPAPSSSSSSSSSTSSAGADVDYSALEKEV-----------------DFDSDP 612
Cdd:PTZ00449  735 PIGDPDAEQPddiefftPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEamkrpdspsehedkppgDHPSLP 814
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  613 ME----ECLRIfneSTSVKTEDRGRLARQPPKE--EKSEEKGLSGLTTL-----FPGQKRRI-------------SHLSK 668
Cdd:PTZ00449  815 KKrhrlDGLAL---STTDLESDAGRIAKDASGKivKLKRSKSFDDLTTVeeaeeMGAEARKIvvdddgteaddedTHPPE 891
                         330       340
                  ....*....|....*....|
gi 145199237  669 QGQEVEPPRRGPAVPPARPP 688
Cdd:PTZ00449  892 EKHKSEVRRRRPPKKPSKPK 911
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
39-477 6.77e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   39 SGAPGDGGEAPPAAGLGYDPYNPELPKPPAQrengtlGLGEEPRPDVLELELVNQAIEAVRSEveleqrryrellettRE 118
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPG------PGTEAPANESRSTPTWSLSTLAPASP---------------AR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  119 HRSAEAPALAPRG--PNASPTVGPDEDAFPLAFDYSPGSHGLLSPDAGYQPTPLAAPAEPGSkyslasldrgqGRGGGGG 196
Cdd:PHA03307  103 EGSPTPPGPSSPDppPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS-----------DAASSRQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  197 GALeyvpkAVSQPRRHSRPVPSGKYVVDNSRPPTDLEYDPlsnySARHLSRASSRDERAAKRPRGSRGsepytPAPKKLC 276
Cdd:PHA03307  172 AAL-----PLSSPEETARAPSSPPAEPPPSTPPAAASPRP----PRRSSPISASASSPAPAPGRSAAD-----DAGASSS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  277 DPFGSCDARFSDSEDEAATVPGNEPTTASTPKARADPEIkatgQPPSKEGLEAEGGGLRETKETAVQCDVGDLQPPPAKP 356
Cdd:PHA03307  238 DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN----GPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  357 ASPAQVQSSQDG-GCPKEGKPKKKKTGAPPAPSCKDGAQGKDktkDKGRGRPVEKPRADKKGPQASSPRRKAERPEGTKK 435
Cdd:PHA03307  314 ASSSSSSSRESSsSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 145199237  436 KPSSATPVATSGK-GRPDRPARRPSPTSGDSRPAAGRGPPRPL 477
Cdd:PHA03307  391 RAAVAGRARRRDAtGRFPAGRPRPSPLDAGAASGAFYARYPLL 433
DUF1633 super family cl25927
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ...
680-884 1.66e-03

Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.


The actual alignment was detected with superfamily member pfam07794:

Pssm-ID: 116408 [Multi-domain]  Cd Length: 698  Bit Score: 42.57  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   680 PAVPPARPPTAQ-----EV--CYLRAQ-------QAQRASASLLQAPARLAEKSPSVHISAPGEKrriAHIPNPRLAAAP 745
Cdd:pfam07794  282 PADPAIALPAAQldpieEVpqIEFRPQadfpiknEIPKDSCSTSELPLIRRMRCGSLHVQRANAE---AHARADDLSAAV 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   746 TGAKRTLAASGSQSSNGpEPGGQQLKTRTLSGMASKTTTTiipkRIAHSPSLQSLKKPIIPKEFG-GKVPTVIRQRYLNL 824
Cdd:pfam07794  359 AAARNSLAASHAQASAS-HPSLPAANAANPAAAVAIAAGN----KPFHWSYTHDRDHPIIEDKAGlANLLAHIEGRLCQV 433
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   825 FIEECLKFCTSNQEAIEKALNEEKVAYDRSPSkniylNVAVNTLKKLRGLAPSAVPGLSK 884
Cdd:pfam07794  434 PGDCCYKQVGCSLRASAKEGEEGERAIREEDP-----HLGADQDREVRFGAEGIVPGIER 488
 
Name Accession Description Interval E-value
EloA-BP1 pfam15870
ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically ...
802-960 3.31e-86

ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically between 144 and 167 amino acids in length.


Pssm-ID: 464914  Cd Length: 163  Bit Score: 276.56  E-value: 3.31e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   802 KPIIPKEFGGKVPTVIRQRYLNLFIEECLKFCTSNQEAIEKALNEEKVAYDRSPSKNIYLNVAVNTLKKLRGLAPSAVPG 881
Cdd:pfam15870    1 RPVIPTEFGSKVPTNIRQRYLNLFIDECLKICTSEQEAFERALEEEKAVYDRCSSKNIYLNVAVNTLKKLRKEVPSQSSA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   882 LSKT----SGRRVVSHEVVLGGRLAAKTSFSLSRPSSPRVEDLKGAALYSRLREYLLTQDQLKENGYPFPHPERPGGAII 957
Cdd:pfam15870   81 VTKSsaisSNNKVVSHEAVLGGKLAAKTSFSINRNSKSIEEDLKGATLYRMLKEYLLTEEQLKENGYPRPHPDKPGRAVL 160

                   ...
gi 145199237   958 FTA 960
Cdd:pfam15870  161 FTA 163
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
1061-1209 2.21e-78

DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They 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. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T.


Pssm-ID: 99848  Cd Length: 150  Bit Score: 254.33  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1061 YALDCEMSYTTYGLELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADTSVTLRDVQAVLLSMFSADTILI 1140
Cdd:cd06145     1 FALDCEMCYTTDGLELTRVTVVDENGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVTTTLEDVQKKLLSLISPDTILV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145199237 1141 GHSLESDLLALKVIHSTVVDTSVLFPHRLGLPYKRSLRNLMADYLRQIIQDNVDGHSSSEDAGACMHLV 1209
Cdd:cd06145    81 GHSLENDLKALKLIHPRVIDTAILFPHPRGPPYKPSLKNLAKKYLGRDIQQGEGGHDSVEDARAALELV 149
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
1060-1215 7.67e-28

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 110.85  E-value: 7.67e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   1060 IYALDCEMSYTTYG----LELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADTSvTLRDVQAVLLSMFSA 1135
Cdd:smart00479    2 LVVIDCETTGLDPGkdeiIEIAAVDVDGGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAP-TFEEVLEELLEFLRG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   1136 DTILIGHSLESDLLALKVIH----------STVVDTSVLFPHRLGLPYKRSLRNLMADYLRQIIQdnvDGHSSSEDAGAC 1205
Cdd:smart00479   81 RILVAGNSAHFDLRFLKLEHprlgikqppkLPVIDTLKLARATNPGLPKYSLKKLAKRLLLEVIQ---RAHRALDDARAT 157
                           170
                    ....*....|
gi 145199237   1206 MHLVIWKVRE 1215
Cdd:smart00479  158 AKLFKKLLER 167
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
400-688 5.48e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  400 KDKGRGRPVEKPRADKKGPQASSPrrkaERPEGTKKKPSSATPVATSGKGRPDRPARRPSPTsgdsRPAAGRGPPRPLQL 479
Cdd:PTZ00449  583 KDPKHPKDPEEPKKPKRPRSAQRP----TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQ----RPSSPERPEGPKII 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  480 PDRKSTKAPSGKLVERKARSLDEGASQDAPKLKKRALSHADLFGDES---EDEAAGPGVPSVWPSALPSLSSDSDSDSDS 556
Cdd:PTZ00449  655 KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESilkETLPETPGTPFTTPRPLPPKLPRDEEFPFE 734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  557 SLGFPEAQGP-------PKRLKASPPPSPAPSSSSSSSSSTSSAGADVDYSALEKEV-----------------DFDSDP 612
Cdd:PTZ00449  735 PIGDPDAEQPddiefftPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEamkrpdspsehedkppgDHPSLP 814
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  613 ME----ECLRIfneSTSVKTEDRGRLARQPPKE--EKSEEKGLSGLTTL-----FPGQKRRI-------------SHLSK 668
Cdd:PTZ00449  815 KKrhrlDGLAL---STTDLESDAGRIAKDASGKivKLKRSKSFDDLTTVeeaeeMGAEARKIvvdddgteaddedTHPPE 891
                         330       340
                  ....*....|....*....|
gi 145199237  669 QGQEVEPPRRGPAVPPARPP 688
Cdd:PTZ00449  892 EKHKSEVRRRRPPKKPSKPK 911
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
39-477 6.77e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   39 SGAPGDGGEAPPAAGLGYDPYNPELPKPPAQrengtlGLGEEPRPDVLELELVNQAIEAVRSEveleqrryrellettRE 118
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPG------PGTEAPANESRSTPTWSLSTLAPASP---------------AR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  119 HRSAEAPALAPRG--PNASPTVGPDEDAFPLAFDYSPGSHGLLSPDAGYQPTPLAAPAEPGSkyslasldrgqGRGGGGG 196
Cdd:PHA03307  103 EGSPTPPGPSSPDppPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS-----------DAASSRQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  197 GALeyvpkAVSQPRRHSRPVPSGKYVVDNSRPPTDLEYDPlsnySARHLSRASSRDERAAKRPRGSRGsepytPAPKKLC 276
Cdd:PHA03307  172 AAL-----PLSSPEETARAPSSPPAEPPPSTPPAAASPRP----PRRSSPISASASSPAPAPGRSAAD-----DAGASSS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  277 DPFGSCDARFSDSEDEAATVPGNEPTTASTPKARADPEIkatgQPPSKEGLEAEGGGLRETKETAVQCDVGDLQPPPAKP 356
Cdd:PHA03307  238 DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN----GPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  357 ASPAQVQSSQDG-GCPKEGKPKKKKTGAPPAPSCKDGAQGKDktkDKGRGRPVEKPRADKKGPQASSPRRKAERPEGTKK 435
Cdd:PHA03307  314 ASSSSSSSRESSsSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 145199237  436 KPSSATPVATSGK-GRPDRPARRPSPTSGDSRPAAGRGPPRPL 477
Cdd:PHA03307  391 RAAVAGRARRRDAtGRFPAGRPRPSPLDAGAASGAFYARYPLL 433
DUF1633 pfam07794
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ...
680-884 1.66e-03

Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.


Pssm-ID: 116408 [Multi-domain]  Cd Length: 698  Bit Score: 42.57  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   680 PAVPPARPPTAQ-----EV--CYLRAQ-------QAQRASASLLQAPARLAEKSPSVHISAPGEKrriAHIPNPRLAAAP 745
Cdd:pfam07794  282 PADPAIALPAAQldpieEVpqIEFRPQadfpiknEIPKDSCSTSELPLIRRMRCGSLHVQRANAE---AHARADDLSAAV 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   746 TGAKRTLAASGSQSSNGpEPGGQQLKTRTLSGMASKTTTTiipkRIAHSPSLQSLKKPIIPKEFG-GKVPTVIRQRYLNL 824
Cdd:pfam07794  359 AAARNSLAASHAQASAS-HPSLPAANAANPAAAVAIAAGN----KPFHWSYTHDRDHPIIEDKAGlANLLAHIEGRLCQV 433
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   825 FIEECLKFCTSNQEAIEKALNEEKVAYDRSPSkniylNVAVNTLKKLRGLAPSAVPGLSK 884
Cdd:pfam07794  434 PGDCCYKQVGCSLRASAKEGEEGERAIREEDP-----HLGADQDREVRFGAEGIVPGIER 488
 
Name Accession Description Interval E-value
EloA-BP1 pfam15870
ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically ...
802-960 3.31e-86

ElonginA binding-protein 1; This domain family is found in eukaryotes, and is typically between 144 and 167 amino acids in length.


Pssm-ID: 464914  Cd Length: 163  Bit Score: 276.56  E-value: 3.31e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   802 KPIIPKEFGGKVPTVIRQRYLNLFIEECLKFCTSNQEAIEKALNEEKVAYDRSPSKNIYLNVAVNTLKKLRGLAPSAVPG 881
Cdd:pfam15870    1 RPVIPTEFGSKVPTNIRQRYLNLFIDECLKICTSEQEAFERALEEEKAVYDRCSSKNIYLNVAVNTLKKLRKEVPSQSSA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   882 LSKT----SGRRVVSHEVVLGGRLAAKTSFSLSRPSSPRVEDLKGAALYSRLREYLLTQDQLKENGYPFPHPERPGGAII 957
Cdd:pfam15870   81 VTKSsaisSNNKVVSHEAVLGGKLAAKTSFSINRNSKSIEEDLKGATLYRMLKEYLLTEEQLKENGYPRPHPDKPGRAVL 160

                   ...
gi 145199237   958 FTA 960
Cdd:pfam15870  161 FTA 163
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
1061-1209 2.21e-78

DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They 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. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T.


Pssm-ID: 99848  Cd Length: 150  Bit Score: 254.33  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1061 YALDCEMSYTTYGLELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADTSVTLRDVQAVLLSMFSADTILI 1140
Cdd:cd06145     1 FALDCEMCYTTDGLELTRVTVVDENGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVTTTLEDVQKKLLSLISPDTILV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145199237 1141 GHSLESDLLALKVIHSTVVDTSVLFPHRLGLPYKRSLRNLMADYLRQIIQDNVDGHSSSEDAGACMHLV 1209
Cdd:cd06145    81 GHSLENDLKALKLIHPRVIDTAILFPHPRGPPYKPSLKNLAKKYLGRDIQQGEGGHDSVEDARAALELV 149
DEDDh_RNase cd06137
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX) ...
1061-1209 2.57e-39

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX)-1,-3, and -4, ISG20, and similar proteins; This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p), REX4 (or Rex4p), ISG20, and similar proteins. They 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. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. REX proteins are required for the processing and maturation of many RNA species, and ISG20 is an interferon-induced antiviral exonuclease with a strong preference for single-stranded RNA.


Pssm-ID: 99840  Cd Length: 161  Bit Score: 143.57  E-value: 2.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1061 YALDCEMSYTTYGL-ELTRVTV-VDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLAD---TSVTLR--DVQAVLLSMF 1133
Cdd:cd06137     1 VALDCEMVGLADGDsEVVRISAvDVLTGEVLIDSLVRPSVRVTDWRTRFSGVTPADLEEaakAGKTIFgwEAARAALWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1134 S-ADTILIGHSLESDLLALKVIHSTVVDTSVLFPHRLGLPY---KRSLRNLMADYLRQIIQDNVDGHSSSEDAGACMHLV 1209
Cdd:cd06137    81 IdPDTILVGHSLQNDLDALRMIHTRVVDTAILTREAVKGPLakrQWSLRTLCRDFLGLKIQGGGEGHDSLEDALAAREVV 160
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
1060-1215 7.67e-28

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 110.85  E-value: 7.67e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   1060 IYALDCEMSYTTYG----LELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADTSvTLRDVQAVLLSMFSA 1135
Cdd:smart00479    2 LVVIDCETTGLDPGkdeiIEIAAVDVDGGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAP-TFEEVLEELLEFLRG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   1136 DTILIGHSLESDLLALKVIH----------STVVDTSVLFPHRLGLPYKRSLRNLMADYLRQIIQdnvDGHSSSEDAGAC 1205
Cdd:smart00479   81 RILVAGNSAHFDLRFLKLEHprlgikqppkLPVIDTLKLARATNPGLPKYSLKKLAKRLLLEVIQ---RAHRALDDARAT 157
                           170
                    ....*....|
gi 145199237   1206 MHLVIWKVRE 1215
Cdd:smart00479  158 AKLFKKLLER 167
REX4_like cd06144
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product ...
1090-1208 2.61e-22

DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product of 20 kDa, and similar proteins; This subfamily is composed of RNA exonuclease 4 (REX4 or Rex4p), XPMC2, Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20), and similar proteins. REX4 is involved in pre-rRNA processing. It controls the ratio between the two forms of 5.8S rRNA in yeast. XPMC2 is a Xenopus gene which was identified through its ability to correct a mitotic defect in fission yeast. The human homolog of XPMC2 (hPMC2) may be involved in angiotensin II-induced adrenal cell cycle progression and cell proliferation. ISG20 is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. These proteins 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. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherchia coli RNase T.


Pssm-ID: 99847  Cd Length: 152  Bit Score: 94.50  E-value: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1090 YDTFVKPDNEIVDYNTRFSGVTEADLADtSVTLRDVQAVLLSMFsADTILIGHSLESDLLALKVIHST--VVDTSVLFP- 1166
Cdd:cd06144    33 YDTYVKPQEPVTDYRTAVSGIRPEHLKD-APDFEEVQKKVAELL-KGRILVGHALKNDLKVLKLDHPKklIRDTSKYKPl 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 145199237 1167 HRLGLPYKRSLRNLMADYLRQIIQDnvDGHSSSEDAGACMHL 1208
Cdd:cd06144   111 RKTAKGKSPSLKKLAKQLLGLDIQE--GEHSSVEDARAAMRL 150
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
1062-1208 2.49e-18

DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease 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. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.


Pssm-ID: 99852  Cd Length: 157  Bit Score: 83.26  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1062 ALDCEMSYTTYGL---ELTRVTVVDTDVHVVYDTFVKPDNEIVDYNTRFSGVTEADLADtSVTLRDVQAVLLSMFSAdTI 1138
Cdd:cd06149     2 AIDCEMVGTGPGGresELARCSIVNYHGDVLYDKYIRPEGPVTDYRTRWSGIRRQHLVN-ATPFAVAQKEILKILKG-KV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145199237 1139 LIGHSLESDLLALKVIHS--TVVDTS--VLFPHRLGLPYKR--SLRNLMADYLRQIIQDNVDGHSSSEDAGACMHL 1208
Cdd:cd06149    80 VVGHAIHNDFKALKYFHPkhMTRDTStiPLLNRKAGFPENCrvSLKVLAKRLLHRDIQVGRQGHSSVEDARATMEL 155
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
1091-1208 7.11e-14

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with 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.


Pssm-ID: 99846  Cd Length: 174  Bit Score: 71.11  E-value: 7.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237 1091 DTFVKPDNEIVDYNTRFSGVTEADL-ADTS----VTLRDVQAVLLSMFSADTILIGHSLESDL--LALKVIHSTVVDTSV 1163
Cdd:cd06143    52 DDYISTTEPVVDYLTRFSGIKPGDLdPKTSsknlTTLKSAYLKLRLLVDLGCIFVGHGLAKDFrvINIQVPKEQVIDTVE 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 145199237 1164 LFphRLGLPYKRSLRNLMADYLRQIIQDnvDGHSSSEDAGACMHL 1208
Cdd:cd06143   132 LF--HLPGQRKLSLRFLAWYLLGEKIQS--ETHDSIEDARTALKL 172
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
400-688 5.48e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  400 KDKGRGRPVEKPRADKKGPQASSPrrkaERPEGTKKKPSSATPVATSGKGRPDRPARRPSPTsgdsRPAAGRGPPRPLQL 479
Cdd:PTZ00449  583 KDPKHPKDPEEPKKPKRPRSAQRP----TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQ----RPSSPERPEGPKII 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  480 PDRKSTKAPSGKLVERKARSLDEGASQDAPKLKKRALSHADLFGDES---EDEAAGPGVPSVWPSALPSLSSDSDSDSDS 556
Cdd:PTZ00449  655 KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESilkETLPETPGTPFTTPRPLPPKLPRDEEFPFE 734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  557 SLGFPEAQGP-------PKRLKASPPPSPAPSSSSSSSSSTSSAGADVDYSALEKEV-----------------DFDSDP 612
Cdd:PTZ00449  735 PIGDPDAEQPddiefftPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEamkrpdspsehedkppgDHPSLP 814
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  613 ME----ECLRIfneSTSVKTEDRGRLARQPPKE--EKSEEKGLSGLTTL-----FPGQKRRI-------------SHLSK 668
Cdd:PTZ00449  815 KKrhrlDGLAL---STTDLESDAGRIAKDASGKivKLKRSKSFDDLTTVeeaeeMGAEARKIvvdddgteaddedTHPPE 891
                         330       340
                  ....*....|....*....|
gi 145199237  669 QGQEVEPPRRGPAVPPARPP 688
Cdd:PTZ00449  892 EKHKSEVRRRRPPKKPSKPK 911
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
39-477 6.77e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   39 SGAPGDGGEAPPAAGLGYDPYNPELPKPPAQrengtlGLGEEPRPDVLELELVNQAIEAVRSEveleqrryrellettRE 118
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPG------PGTEAPANESRSTPTWSLSTLAPASP---------------AR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  119 HRSAEAPALAPRG--PNASPTVGPDEDAFPLAFDYSPGSHGLLSPDAGYQPTPLAAPAEPGSkyslasldrgqGRGGGGG 196
Cdd:PHA03307  103 EGSPTPPGPSSPDppPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS-----------DAASSRQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  197 GALeyvpkAVSQPRRHSRPVPSGKYVVDNSRPPTDLEYDPlsnySARHLSRASSRDERAAKRPRGSRGsepytPAPKKLC 276
Cdd:PHA03307  172 AAL-----PLSSPEETARAPSSPPAEPPPSTPPAAASPRP----PRRSSPISASASSPAPAPGRSAAD-----DAGASSS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  277 DPFGSCDARFSDSEDEAATVPGNEPTTASTPKARADPEIkatgQPPSKEGLEAEGGGLRETKETAVQCDVGDLQPPPAKP 356
Cdd:PHA03307  238 DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN----GPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  357 ASPAQVQSSQDG-GCPKEGKPKKKKTGAPPAPSCKDGAQGKDktkDKGRGRPVEKPRADKKGPQASSPRRKAERPEGTKK 435
Cdd:PHA03307  314 ASSSSSSSRESSsSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 145199237  436 KPSSATPVATSGK-GRPDRPARRPSPTSGDSRPAAGRGPPRPL 477
Cdd:PHA03307  391 RAAVAGRARRRDAtGRFPAGRPRPSPLDAGAASGAFYARYPLL 433
PHA03247 PHA03247
large tegument protein UL36; Provisional
115-481 1.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  115 TTREHRSAEAP----ALAPRGPNASPTVGPDEDAFPlafdysPGSHGLLSPdagyQPTPLAAPAEPGSKYSLASLDRGQG 190
Cdd:PHA03247 2583 TSRARRPDAPPqsarPRAPVDDRGDPRGPAPPSPLP------PDTHAPDPP----PPSPSPAANEPDPHPPPTVPPPERP 2652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  191 RGGGGggaleyvPKAVSQPRRHSRPVPSGKYVVDNSRPPTDLEYDPLSNYSArhLSRASSRDERAAKRPRGSRGSEPYTP 270
Cdd:PHA03247 2653 RDDPA-------PGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS--LADPPPPPPTPEPAPHALVSATPLPP 2723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  271 APKKLCDPFGSCDAR-FSDSEDEAATVPGNE-----PTTASTPKARADPEIKATGQPPSKEglEAEGGGLRETKETA-VQ 343
Cdd:PHA03247 2724 GPAAARQASPALPAApAPPAVPAGPATPGGParparPPTTAGPPAPAPPAAPAAGPPRRLT--RPAVASLSESRESLpSP 2801
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237  344 CDVGDLQPPPAKPASPAQVQSSQDGGCPKEGKPKKKKTGAPPAPS------CKDGAQGKDKtkdkgRGRPVEKPRADKKG 417
Cdd:PHA03247 2802 WDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplGGSVAPGGDV-----RRRPPSRSPAAKPA 2876
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145199237  418 PQASSPRRKAERPEGTKKKPSSATPVATSGKGRPDRPARRPSPTSGDSRPAAGRGPPRPLQLPD 481
Cdd:PHA03247 2877 APARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
DUF1633 pfam07794
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ...
680-884 1.66e-03

Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.


Pssm-ID: 116408 [Multi-domain]  Cd Length: 698  Bit Score: 42.57  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   680 PAVPPARPPTAQ-----EV--CYLRAQ-------QAQRASASLLQAPARLAEKSPSVHISAPGEKrriAHIPNPRLAAAP 745
Cdd:pfam07794  282 PADPAIALPAAQldpieEVpqIEFRPQadfpiknEIPKDSCSTSELPLIRRMRCGSLHVQRANAE---AHARADDLSAAV 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   746 TGAKRTLAASGSQSSNGpEPGGQQLKTRTLSGMASKTTTTiipkRIAHSPSLQSLKKPIIPKEFG-GKVPTVIRQRYLNL 824
Cdd:pfam07794  359 AAARNSLAASHAQASAS-HPSLPAANAANPAAAVAIAAGN----KPFHWSYTHDRDHPIIEDKAGlANLLAHIEGRLCQV 433
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145199237   825 FIEECLKFCTSNQEAIEKALNEEKVAYDRSPSkniylNVAVNTLKKLRGLAPSAVPGLSK 884
Cdd:pfam07794  434 PGDCCYKQVGCSLRASAKEGEEGERAIREEDP-----HLGADQDREVRFGAEGIVPGIER 488
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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