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Conserved domains on  [gi|1046900791|ref|XP_017451242|]
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cAMP-regulated phosphoprotein 21 isoform X3 [Rattus norvegicus]

Protein Classification

R3H and SUZ domain-containing protein( domain architecture ID 10119061)

R3H and SUZ domain-containing protein may bind single-stranded nucleic acids through its R3H domain and RNA through its SUZ domain, similar to Zea mays DBF1-interactor protein 1 that is a potential regulator of DBF1 activity in stress responses

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 2.06e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.60  E-value: 2.06e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046900791 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-299 7.78e-13

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.88  E-value: 7.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900791 244 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 299
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
590-818 1.28e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 590 QLSMSRQSSGDTPEPPSgPVYPASLMQAAQPPSYVITSAGQQLSTG--GFSDSGPPISQQVLQA----PPSPQGFVQQPP 663
Cdd:pfam09770  99 QVRFNRQQPAARAAQSS-AQPPASSLPQYQYASQQSQQPSKPVRTGyeKYKEPEPIPDLQVDASlwgvAPKKAAAPAPAP 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 664 PAQMSvyyypsgqyPTSTTQQYRPLASVQY--SAQRSQQIPQTAQQA-------GYQPVLSGQQSFQGLMGVQQSAHSQG 734
Cdd:pfam09770 178 QPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQQQPQQ 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 735 VMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQTGQ--GSLPATGMPVYCNITPPSPQNN 807
Cdd:pfam09770 249 QPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPGVQPAP 328
                         250
                  ....*....|.
gi 1046900791 808 LRLMGPHCPSS 818
Cdd:pfam09770 329 AHQAHRQQGSF 339
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
335-791 7.02e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 335 SSGRTSGSRQSSSETELRWPDHQRAWSSTDSD--SSNRNLKPTMTKTASfggitvltrgDSTSSTRSAGKLSKTGSESSS 412
Cdd:pfam03154  41 SSGRNSPSAASTSSNDSKAESMKKSSKKIKEEapSPLKSAKRQREKGAS----------DTEEPERATAKKSKTQEISRP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 413 SAGSSGSLSRTH------------PPLQSTALTSSVAAGSP-----GCMAYSENGMGGQVPPSSTSYILLPLESATGIPP 475
Cdd:pfam03154 111 NSPSEGEGESSDgrsvndegssdpKDIDQDNRSTSPSIPSPqdnesDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 476 GSILLN--PHTGQPFVNPDGTPAIYNPPGSQQTLRGTVSGQPQQPPPQQPSPQPQQQVQASQPQMTGPLVTqSVQGLQPS 553
Cdd:pfam03154 191 TTQAATagPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQP 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 554 SQSVQYPAVSFP----PQHLLPVSPTQHFPLREEMAAQFSQLSMSRQSSGDTPEPPSGPVyPASLMQAAQPPSYvitsag 629
Cdd:pfam03154 270 SLHGQMPPMPHSlqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP-SQSQLQSQQPPRE------ 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 630 QQLSTGGFS--DSGPPISQQVLQApPSPQG-----FVQQPPPAQM-SVYYYPSGQYPTSTTQQYRPLASVQYSAQ---RS 698
Cdd:pfam03154 343 QPLPPAPLSmpHIKPPPTTPIPQL-PNPQShkhppHLSGPSPFQMnSNLPPPPALKPLSSLSTHHPPSAHPPPLQlmpQS 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 699 QQIPQTAQQAgyqPVLSGQQSFQGLMGVQQSAHSQGVMSSQQGAPVHGVMVSYPT-MSSYQVPMTQGSQAVPqqTYQPPI 777
Cdd:pfam03154 422 QQLPPPPAQP---PVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPpITPPSGPPTSTSSAMP--GIQPPS 496
                         490
                  ....*....|....
gi 1046900791 778 MLPSQTGqGSLPAT 791
Cdd:pfam03154 497 SASVSSS-GPVPAA 509
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 2.06e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.60  E-value: 2.06e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046900791 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-299 7.78e-13

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.88  E-value: 7.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900791 244 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 299
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 8.55e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 64.24  E-value: 8.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  146 IDLHEFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
164-222 8.10e-12

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 60.97  E-value: 8.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046900791 164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
590-818 1.28e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 590 QLSMSRQSSGDTPEPPSgPVYPASLMQAAQPPSYVITSAGQQLSTG--GFSDSGPPISQQVLQA----PPSPQGFVQQPP 663
Cdd:pfam09770  99 QVRFNRQQPAARAAQSS-AQPPASSLPQYQYASQQSQQPSKPVRTGyeKYKEPEPIPDLQVDASlwgvAPKKAAAPAPAP 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 664 PAQMSvyyypsgqyPTSTTQQYRPLASVQY--SAQRSQQIPQTAQQA-------GYQPVLSGQQSFQGLMGVQQSAHSQG 734
Cdd:pfam09770 178 QPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQQQPQQ 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 735 VMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQTGQ--GSLPATGMPVYCNITPPSPQNN 807
Cdd:pfam09770 249 QPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPGVQPAP 328
                         250
                  ....*....|.
gi 1046900791 808 LRLMGPHCPSS 818
Cdd:pfam09770 329 AHQAHRQQGSF 339
PRK10263 PRK10263
DNA translocase FtsK; Provisional
567-762 1.09e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  567 QHLLPVSPTQHFPLRE-EMAAQFSQLSMSRQSSgdtpEPPSGpVYPASLMQAAQPPSYVITSAGQqlSTGGFSDSGPPIS 645
Cdd:PRK10263   681 QHDVPVNAEDADAAAEaELARQFAQTQQQRYSG----EQPAG-ANPFSLDDFEFSPMKALLDDGP--HEPLFTPIVEPVQ 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  646 QQVLQAPPSPQGFVQQPPPAQMSVYYYPsgQYPTSTTQQYR-PLASVQYSAQRSQ-QIPQTAQQAGYQPV--LSGQQSFQ 721
Cdd:PRK10263   754 QPQQPVAPQQQYQQPQQPVAPQPQYQQP--QQPVAPQPQYQqPQQPVAPQPQYQQpQQPVAPQPQYQQPQqpVAPQPQYQ 831
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1046900791  722 glmgvqqsAHSQGVMSSQQGAPVHGVMVSYPTMSSYQVPMT 762
Cdd:PRK10263   832 --------QPQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTT 864
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
581-717 1.21e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 581 REEMAAQFSQLSM-SRQSSGDTPEPPSgpvypaslmqAAQPPSYviTSAGQQLSTG---GFSDSGPPISQQVLQAPPSPQ 656
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA----------MGQPPYY--GQGPQQQFNGqplGWPRMSMMPTPMGPGGPLRPN 435
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046900791 657 GFVQQPPPAQMSVYYYPSGQYPTSTTQQYRPLASVQYSAQRSQQIPQTAQQAGYQPVLSGQ 717
Cdd:TIGR01628 436 GLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
335-791 7.02e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 335 SSGRTSGSRQSSSETELRWPDHQRAWSSTDSD--SSNRNLKPTMTKTASfggitvltrgDSTSSTRSAGKLSKTGSESSS 412
Cdd:pfam03154  41 SSGRNSPSAASTSSNDSKAESMKKSSKKIKEEapSPLKSAKRQREKGAS----------DTEEPERATAKKSKTQEISRP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 413 SAGSSGSLSRTH------------PPLQSTALTSSVAAGSP-----GCMAYSENGMGGQVPPSSTSYILLPLESATGIPP 475
Cdd:pfam03154 111 NSPSEGEGESSDgrsvndegssdpKDIDQDNRSTSPSIPSPqdnesDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 476 GSILLN--PHTGQPFVNPDGTPAIYNPPGSQQTLRGTVSGQPQQPPPQQPSPQPQQQVQASQPQMTGPLVTqSVQGLQPS 553
Cdd:pfam03154 191 TTQAATagPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQP 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 554 SQSVQYPAVSFP----PQHLLPVSPTQHFPLREEMAAQFSQLSMSRQSSGDTPEPPSGPVyPASLMQAAQPPSYvitsag 629
Cdd:pfam03154 270 SLHGQMPPMPHSlqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP-SQSQLQSQQPPRE------ 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 630 QQLSTGGFS--DSGPPISQQVLQApPSPQG-----FVQQPPPAQM-SVYYYPSGQYPTSTTQQYRPLASVQYSAQ---RS 698
Cdd:pfam03154 343 QPLPPAPLSmpHIKPPPTTPIPQL-PNPQShkhppHLSGPSPFQMnSNLPPPPALKPLSSLSTHHPPSAHPPPLQlmpQS 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 699 QQIPQTAQQAgyqPVLSGQQSFQGLMGVQQSAHSQGVMSSQQGAPVHGVMVSYPT-MSSYQVPMTQGSQAVPqqTYQPPI 777
Cdd:pfam03154 422 QQLPPPPAQP---PVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPpITPPSGPPTSTSSAMP--GIQPPS 496
                         490
                  ....*....|....
gi 1046900791 778 MLPSQTGqGSLPAT 791
Cdd:pfam03154 497 SASVSSS-GPVPAA 509
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 2.06e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.60  E-value: 2.06e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046900791 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-299 7.78e-13

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.88  E-value: 7.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900791 244 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 299
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 8.55e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 64.24  E-value: 8.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  146 IDLHEFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
166-222 4.81e-12

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 61.48  E-value: 4.81e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046900791 166 LLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINK 222
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
164-222 8.10e-12

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 60.97  E-value: 8.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046900791 164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
590-818 1.28e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 590 QLSMSRQSSGDTPEPPSgPVYPASLMQAAQPPSYVITSAGQQLSTG--GFSDSGPPISQQVLQA----PPSPQGFVQQPP 663
Cdd:pfam09770  99 QVRFNRQQPAARAAQSS-AQPPASSLPQYQYASQQSQQPSKPVRTGyeKYKEPEPIPDLQVDASlwgvAPKKAAAPAPAP 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 664 PAQMSvyyypsgqyPTSTTQQYRPLASVQY--SAQRSQQIPQTAQQA-------GYQPVLSGQQSFQGLMGVQQSAHSQG 734
Cdd:pfam09770 178 QPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQQQPQQ 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 735 VMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQTGQ--GSLPATGMPVYCNITPPSPQNN 807
Cdd:pfam09770 249 QPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPGVQPAP 328
                         250
                  ....*....|.
gi 1046900791 808 LRLMGPHCPSS 818
Cdd:pfam09770 329 AHQAHRQQGSF 339
PRK10263 PRK10263
DNA translocase FtsK; Provisional
567-762 1.09e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  567 QHLLPVSPTQHFPLRE-EMAAQFSQLSMSRQSSgdtpEPPSGpVYPASLMQAAQPPSYVITSAGQqlSTGGFSDSGPPIS 645
Cdd:PRK10263   681 QHDVPVNAEDADAAAEaELARQFAQTQQQRYSG----EQPAG-ANPFSLDDFEFSPMKALLDDGP--HEPLFTPIVEPVQ 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  646 QQVLQAPPSPQGFVQQPPPAQMSVYYYPsgQYPTSTTQQYR-PLASVQYSAQRSQ-QIPQTAQQAGYQPV--LSGQQSFQ 721
Cdd:PRK10263   754 QPQQPVAPQQQYQQPQQPVAPQPQYQQP--QQPVAPQPQYQqPQQPVAPQPQYQQpQQPVAPQPQYQQPQqpVAPQPQYQ 831
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1046900791  722 glmgvqqsAHSQGVMSSQQGAPVHGVMVSYPTMSSYQVPMT 762
Cdd:PRK10263   832 --------QPQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTT 864
PRK10263 PRK10263
DNA translocase FtsK; Provisional
605-796 1.12e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  605 PSGPVYPASLMQAAQPPSYVITSAGQQLStggfsdsGPPISQQVLQapPSPQGFVQQPPPAQMSVYYYPSGQYPTSTTQQ 684
Cdd:PRK10263   336 PVEPVTQTPPVASVDVPPAQPTVAWQPVP-------GPQTGEPVIA--PAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQP 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  685 YRPLASVQYSAQrsQQIPQTAQQAGYQPVLSGQqsfqglmgVQQSAHSQGVMSSQQGaPVHGVMVSYPTMSSYQVPMTQG 764
Cdd:PRK10263   407 YYAPAAEQPAQQ--PYYAPAPEQPAQQPYYAPA--------PEQPVAGNAWQAEEQQ-STFAPQSTYQTEQTYQQPAAQE 475
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1046900791  765 SQAVPQQTYQPPIMLPSQTGQGSLPATGMPVY 796
Cdd:PRK10263   476 PLYQQPQPVEQQPVVEPEPVVEETKPARPPLY 507
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
581-717 1.21e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 581 REEMAAQFSQLSM-SRQSSGDTPEPPSgpvypaslmqAAQPPSYviTSAGQQLSTG---GFSDSGPPISQQVLQAPPSPQ 656
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA----------MGQPPYY--GQGPQQQFNGqplGWPRMSMMPTPMGPGGPLRPN 435
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046900791 657 GFVQQPPPAQMSVYYYPSGQYPTSTTQQYRPLASVQYSAQRSQQIPQTAQQAGYQPVLSGQ 717
Cdd:TIGR01628 436 GLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
PRK10927 PRK10927
cell division protein FtsN;
631-744 2.01e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 41.20  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 631 QLSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQMSVYYYPSGQYPTSTTQQyrplasvQYSAQRSQQIPQTAQQAGY 710
Cdd:PRK10927  135 QLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPY 207
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1046900791 711 QPVLsgqqsfqglmgvQQSAHSQGVMSSQQGAPV 744
Cdd:PRK10927  208 QDLL------------QTPAHTTAQSKPQQAAPV 229
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
597-720 2.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 597 SSGDTPEPPSGP---VYPASLMQAAQPPSYVITSAGQQLSTGGFSDSgPPISQQVLQAPPSPQGFVQQPPPAQMSVyyyP 673
Cdd:PRK14971  364 QKGDDASGGRGPkqhIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQ-PSAPQSATQPAGTPPTVSVDPPAAVPVN---P 439
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900791 674 SGQYPTSTTQQYRP---------LASVQYSAQRSQQIPQTAQQAGYQPVLSGQQSF 720
Cdd:PRK14971  440 PSTAPQAVRPAQFKeekkipvskVSSLGPSTLRPIQEKAEQATGNIKEAPTGTQKE 495
R3H_sperm-antigen cd02636
R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. ...
168-207 3.49e-03

R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100065  Cd Length: 61  Bit Score: 36.54  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1046900791 168 KMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGL 207
Cdd:cd02636     3 SMEKEVSKFIKDSVRTREKFQPMDKVERSIVHDVAEVAGL 42
PRK10263 PRK10263
DNA translocase FtsK; Provisional
581-802 3.71e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  581 REEMAAQFSQlsMSRQSSGDTPEPPSgPVYPASLMQAAQPPSYVITSAGQQLSTGGFSDSGP-PISQQVLQAPPSpQGFV 659
Cdd:PRK10263   661 QDELARQFAQ--TQQQRYGEQYQHDV-PVNAEDADAAAEAELARQFAQTQQQRYSGEQPAGAnPFSLDDFEFSPM-KALL 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  660 QQPPPAQMsvyyYPSGQYPTSTTQQyRPLASVQYSAQRSQQIPQTAQQAGYQPVLSGQQSFQGLMGVQQSAHSQGVMSSQ 739
Cdd:PRK10263   737 DDGPHEPL----FTPIVEPVQQPQQ-PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 811
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046900791  740 QGAPvhgvmvsyptmsSYQVPMtqgSQAVPQQTYQPPIMLPSQTGQGSL----------------PATGMPVYCNITPP 802
Cdd:PRK10263   812 APQP------------QYQQPQ---QPVAPQPQYQQPQQPVAPQPQDTLlhpllmrngdsrplhkPTTPLPSLDLLTPP 875
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
176-220 7.01e-03

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100070  Cd Length: 60  Bit Score: 35.79  E-value: 7.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1046900791 176 FIADSNNHYKKFP-QMSSYQRMLVHRVAAYFGLDHNVDQTGKSVII 220
Cdd:cd02641    11 FMKDPKATELEFPpTLSSHDRLLVHELAEELGLRHESTGEGSDRVI 56
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
335-791 7.02e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 335 SSGRTSGSRQSSSETELRWPDHQRAWSSTDSD--SSNRNLKPTMTKTASfggitvltrgDSTSSTRSAGKLSKTGSESSS 412
Cdd:pfam03154  41 SSGRNSPSAASTSSNDSKAESMKKSSKKIKEEapSPLKSAKRQREKGAS----------DTEEPERATAKKSKTQEISRP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 413 SAGSSGSLSRTH------------PPLQSTALTSSVAAGSP-----GCMAYSENGMGGQVPPSSTSYILLPLESATGIPP 475
Cdd:pfam03154 111 NSPSEGEGESSDgrsvndegssdpKDIDQDNRSTSPSIPSPqdnesDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 476 GSILLN--PHTGQPFVNPDGTPAIYNPPGSQQTLRGTVSGQPQQPPPQQPSPQPQQQVQASQPQMTGPLVTqSVQGLQPS 553
Cdd:pfam03154 191 TTQAATagPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQP 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 554 SQSVQYPAVSFP----PQHLLPVSPTQHFPLREEMAAQFSQLSMSRQSSGDTPEPPSGPVyPASLMQAAQPPSYvitsag 629
Cdd:pfam03154 270 SLHGQMPPMPHSlqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP-SQSQLQSQQPPRE------ 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 630 QQLSTGGFS--DSGPPISQQVLQApPSPQG-----FVQQPPPAQM-SVYYYPSGQYPTSTTQQYRPLASVQYSAQ---RS 698
Cdd:pfam03154 343 QPLPPAPLSmpHIKPPPTTPIPQL-PNPQShkhppHLSGPSPFQMnSNLPPPPALKPLSSLSTHHPPSAHPPPLQlmpQS 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791 699 QQIPQTAQQAgyqPVLSGQQSFQGLMGVQQSAHSQGVMSSQQGAPVHGVMVSYPT-MSSYQVPMTQGSQAVPqqTYQPPI 777
Cdd:pfam03154 422 QQLPPPPAQP---PVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPpITPPSGPPTSTSSAMP--GIQPPS 496
                         490
                  ....*....|....
gi 1046900791 778 MLPSQTGqGSLPAT 791
Cdd:pfam03154 497 SASVSSS-GPVPAA 509
PRK10263 PRK10263
DNA translocase FtsK; Provisional
539-687 9.27e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.68  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900791  539 TGPLVTQSVQGLQPSSQSVQYPAVSFPPQHLLPvSPTQHFPlreemAAQFSQLSMSRQSSGDTPEPPSGPVYPASLMQAA 618
Cdd:PRK10263   343 TPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAP-APEGYPQ-----QSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPA 416
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046900791  619 QPPSYVITSAGQQLSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQMSVYYYPSGQYPTSTTQQYRP 687
Cdd:PRK10263   417 QQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVE 485
 
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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