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Conserved domains on  [gi|162951884|ref|NP_055740|]
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R3H domain-containing protein 2 isoform 2 [Homo sapiens]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein; MFS transporter( domain architecture ID 11552550)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein binds DNA and may function as a transcription factor; also contains a Med15 domain, a critical transducer of gene activation signals that control early metazoan development.| major facilitator superfamily (MFS) transporter facilitates the transport across cytoplasmic or internal membranes of one or more from a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides

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 ...
168-229 1.44e-26

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: 103.07  E-value: 1.44e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951884 168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
443-708 5.30e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 60.02  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  443 GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSFIMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYP 522
Cdd:pfam09606 186 GGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQ 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  523 PGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGL 600
Cdd:pfam09606 264 MQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVAL 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  601 VVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVPVS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPP 672
Cdd:pfam09606 344 GGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSPVPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 162951884  673 GSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVVVM 708
Cdd:pfam09606 424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV 460
 
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 ...
168-229 1.44e-26

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: 103.07  E-value: 1.44e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951884 168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.50e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILEFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
170-228 1.76e-10

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: 57.12  E-value: 1.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162951884  170 MMLLKLEQEILEFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
443-708 5.30e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 60.02  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  443 GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSFIMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYP 522
Cdd:pfam09606 186 GGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQ 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  523 PGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGL 600
Cdd:pfam09606 264 MQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVAL 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  601 VVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVPVS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPP 672
Cdd:pfam09606 344 GGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSPVPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 162951884  673 GSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVVVM 708
Cdd:pfam09606 424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV 460
PRK10263 PRK10263
DNA translocase FtsK; Provisional
458-609 1.03e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  458 PSAALFqTPLISqhPQQTSfimasTGQPLPTSNYSTSSH-APPTQQVLPPQGYMQPPQQiqvsYYPPGQYPNSNQQYRPL 536
Cdd:PRK10263  740 PHEPLF-TPIVE--PVQQP-----QQPVAPQQQYQQPQQpVAPQPQYQQPQQPVAPQPQ----YQQPQQPVAPQPQYQQP 807
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951884  537 SHPVAYSPQRGqqlpqpsqqpglQPMMPNQQQAAYqgmigvQQPQNQGLLSSQRSSM------GGQMQGLVVQYTPLPS 609
Cdd:PRK10263  808 QQPVAPQPQYQ------------QPQQPVAPQPQY------QQPQQPVAPQPQDTLLhpllmrNGDSRPLHKPTTPLPS 868
 
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 ...
168-229 1.44e-26

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: 103.07  E-value: 1.44e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951884 168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.50e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILEFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
172-228 3.14e-11

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: 59.55  E-value: 3.14e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162951884 172 LLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG--KAVIINK 228
Cdd:cd02325    1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
170-228 1.76e-10

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: 57.12  E-value: 1.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162951884  170 MMLLKLEQEILEFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
443-708 5.30e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 60.02  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  443 GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSFIMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYP 522
Cdd:pfam09606 186 GGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQ 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  523 PGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGL 600
Cdd:pfam09606 264 MQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVAL 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  601 VVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVPVS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPP 672
Cdd:pfam09606 344 GGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSPVPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 162951884  673 GSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVVVM 708
Cdd:pfam09606 424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV 460
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
484-619 2.34e-04

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: 45.03  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  484 QPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQvsyyPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQPSQQPGLQPMM 563
Cdd:pfam09770 211 AQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQ----QPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQ 286
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 162951884  564 PNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPSYQVPVGSDSQ 619
Cdd:pfam09770 287 QFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQ 342
PRK10263 PRK10263
DNA translocase FtsK; Provisional
458-609 1.03e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  458 PSAALFqTPLISqhPQQTSfimasTGQPLPTSNYSTSSH-APPTQQVLPPQGYMQPPQQiqvsYYPPGQYPNSNQQYRPL 536
Cdd:PRK10263  740 PHEPLF-TPIVE--PVQQP-----QQPVAPQQQYQQPQQpVAPQPQYQQPQQPVAPQPQ----YQQPQQPVAPQPQYQQP 807
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951884  537 SHPVAYSPQRGqqlpqpsqqpglQPMMPNQQQAAYqgmigvQQPQNQGLLSSQRSSM------GGQMQGLVVQYTPLPS 609
Cdd:PRK10263  808 QQPVAPQPQYQ------------QPQQPVAPQPQY------QQPQQPVAPQPQDTLLhpllmrNGDSRPLHKPTTPLPS 868
PRK10263 PRK10263
DNA translocase FtsK; Provisional
434-675 1.55e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  434 QADDLSNPFGQMSLSRQGST-------EAADPSAALfQTPLISQ--HPQQTSFimaSTGQPLPTSNYSTSSHAPPTQQVL 504
Cdd:PRK10263  660 QQDELARQFAQTQQQRYGEQyqhdvpvNAEDADAAA-EAELARQfaQTQQQRY---SGEQPAGANPFSLDDFEFSPMKAL 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  505 PPQGYMQPpqqiqvsYYPPGQYPNSNQQYRPLSHPVAYSPQRgqqlPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQG 584
Cdd:PRK10263  736 LDDGPHEP-------LFTPIVEPVQQPQQPVAPQQQYQQPQQ----PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  585 LLSSQrssmggqmqglvvQYTPLPSYQVPvgsDSQNVVQPPFQQPMlVPVSQSVQGGLpaagvpvyysMIPPAQQNGTS- 663
Cdd:PRK10263  805 QQPQQ-------------PVAPQPQYQQP---QQPVAPQPQYQQPQ-QPVAPQPQDTL----------LHPLLMRNGDSr 857
                         250       260
                  ....*....|....*....|.
gi 162951884  664 ---------PSVGFLQPPGSE 675
Cdd:PRK10263  858 plhkpttplPSLDLLTPPPSE 878
PRK10263 PRK10263
DNA translocase FtsK; Provisional
427-651 4.58e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  427 LNNHMISQADDLSNPFGQMSLSRQGSTEAADPSAALFQTPLISQHPQqtsfimaSTGQPLPTSNYSTSSHAPPTQQVLPP 506
Cdd:PRK10263  311 LNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPT-------VAWQPVPGPQTGEPVIAPAPEGYPQQ 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  507 QGYMQPPQQIQVSY---YPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQ 583
Cdd:PRK10263  384 SQYAQPAVQYNEPLqqpVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQ 463
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162951884  584 gllssqrssmggqmqglvvqytPLPSYQVPVGSDSQNVVQPPFQQPMLV---PVSQSVQGGLPaagvPVYY 651
Cdd:PRK10263  464 ----------------------TEQTYQQPAAQEPLYQQPQPVEQQPVVepePVVEETKPARP----PLYY 508
PHA03377 PHA03377
EBNA-3C; Provisional
464-668 6.96e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.42  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  464 QTPL-ISQHPQQTsfimastgqPLPTSNYSTSSHAPPTQQVLPPQGYMQPP--------------QQIQVSYYPPGQYP- 527
Cdd:PHA03377  727 DDPLdLSLHPDQA---------PPPSHQAPYSGHEEPQAQQAPYPGYWEPRppqapylgyqepqaQGVQVSSYPGYAGPw 797
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951884  528 NSNQQYRPLSHPVAYSPQRGQQLPQPSQQPGLQPMMPNQqqaaYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPL 607
Cdd:PHA03377  798 GLRAQHPRYRHSWAYWSQYPGHGHPQGPWAPRPPHLPPQ----WDGSAGHGQDQVSQFPHLQSETGPPRLQLSQVPQLPY 873
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162951884  608 PsyQVPVGSDSQNVVQPPFQQPMlvpvsQSVQGGLPAAGVPVYYSMIPPAQQNGTS-PSVGF 668
Cdd:PHA03377  874 S--QTLVSSSAPSWSSPQPRAPI-----RPIPTRFPPPPMPLQDSMAVGCDSSGTAcPSMPF 928
 
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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