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Conserved domains on  [gi|755563683|ref|XP_011245653|]
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MMS19 nucleotide excision repair protein homolog isoform X3 [Mus musculus]

Protein Classification

MMS19_N and MMS19_C domain-containing protein( domain architecture ID 12168124)

MMS19_N and MMS19_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
54-312 1.00e-109

Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal part, pfam12460, is an essential component of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly.


:

Pssm-ID: 433995  Cd Length: 258  Bit Score: 335.68  E-value: 1.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683   54 LGSSLENAEPRTRARGAQLLSQVLLQCHSL-LSEKEVVHLILFYENRLKDHhLVVPSVLQGLRALSMSVALPPGLAVSVL 132
Cdd:pfam14500   1 LGEYLTSEDDLIRAKAVLLLSEVLERLPKDkLSRQEVHVLVTFYCSRLDDL-ACLPEALKGLLALVRMKNFPPVEAVSVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  133 KAIFQEVHVQSLLQVDRHTVFSIITNFMRSREEELKGLGADFTFGFIQVMDGEKDPRNLLLAFRIVHDLISKdYSLGPFV 212
Cdd:pfam14500  80 RSLFQEVHVQSLLQADRYLVFQILDTLLEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLRVILSE-FDLGPFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  213 EELFEVTSCYFPIDFTPPPNDPYGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEILSAKLDSLQTLNACCAVYGQ 292
Cdd:pfam14500 159 EDLFDILFCYFPITFRPPPNDPYGITREDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGA 238
                         250       260
                  ....*....|....*....|
gi 755563683  293 KELKDFLPSLWASIRREVFQ 312
Cdd:pfam14500 239 EAVEPHLLTLWSALKFEILN 258
MMS19_C super family cl28783
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
556-805 3.42e-51

RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision repair (NER) and RNA polymerase II (RNAP II) transcription. This C-terminal domain, along with the N-terminal, MMS19_N, form part of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly. This domain has a HEAT-like repeat structure.


The actual alignment was detected with superfamily member pfam12460:

Pssm-ID: 463594  Cd Length: 426  Bit Score: 185.16  E-value: 3.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  556 CLQALSAVSTHPSIVKETLPLLLQHLCQANKGNMVteSSEVVAVCQSLQQVAE-KCQQDPESYWYFHKTAVPCLFALAVQ 634
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYLLEnKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  635 ASMPEKESSVLRkvllEDEVLAALASVIGTATTHLSPELAAQSVTCIVPLFLDGNTsfLPENSFPDQFQPFQDGSS-GQR 713
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  714 RLVALLTAFVCSLPRNVEIPQLNRLMRELLKQSCGHSC-PFSSTAATKCFAGLLNKQPPGQQLEEFLQLAVGTVEAGLAS 792
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNLTS 232
                         250
                  ....*....|...
gi 755563683  793 ESSRdQAFTLLLW 805
Cdd:pfam12460 233 KIST-QALEILIW 244
 
Name Accession Description Interval E-value
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
54-312 1.00e-109

Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal part, pfam12460, is an essential component of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly.


Pssm-ID: 433995  Cd Length: 258  Bit Score: 335.68  E-value: 1.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683   54 LGSSLENAEPRTRARGAQLLSQVLLQCHSL-LSEKEVVHLILFYENRLKDHhLVVPSVLQGLRALSMSVALPPGLAVSVL 132
Cdd:pfam14500   1 LGEYLTSEDDLIRAKAVLLLSEVLERLPKDkLSRQEVHVLVTFYCSRLDDL-ACLPEALKGLLALVRMKNFPPVEAVSVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  133 KAIFQEVHVQSLLQVDRHTVFSIITNFMRSREEELKGLGADFTFGFIQVMDGEKDPRNLLLAFRIVHDLISKdYSLGPFV 212
Cdd:pfam14500  80 RSLFQEVHVQSLLQADRYLVFQILDTLLEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLRVILSE-FDLGPFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  213 EELFEVTSCYFPIDFTPPPNDPYGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEILSAKLDSLQTLNACCAVYGQ 292
Cdd:pfam14500 159 EDLFDILFCYFPITFRPPPNDPYGITREDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGA 238
                         250       260
                  ....*....|....*....|
gi 755563683  293 KELKDFLPSLWASIRREVFQ 312
Cdd:pfam14500 239 EAVEPHLLTLWSALKFEILN 258
MMS19_C pfam12460
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
556-805 3.42e-51

RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision repair (NER) and RNA polymerase II (RNAP II) transcription. This C-terminal domain, along with the N-terminal, MMS19_N, form part of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly. This domain has a HEAT-like repeat structure.


Pssm-ID: 463594  Cd Length: 426  Bit Score: 185.16  E-value: 3.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  556 CLQALSAVSTHPSIVKETLPLLLQHLCQANKGNMVteSSEVVAVCQSLQQVAE-KCQQDPESYWYFHKTAVPCLFALAVQ 634
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYLLEnKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  635 ASMPEKESSVLRkvllEDEVLAALASVIGTATTHLSPELAAQSVTCIVPLFLDGNTsfLPENSFPDQFQPFQDGSS-GQR 713
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  714 RLVALLTAFVCSLPRNVEIPQLNRLMRELLKQSCGHSC-PFSSTAATKCFAGLLNKQPPGQQLEEFLQLAVGTVEAGLAS 792
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNLTS 232
                         250
                  ....*....|...
gi 755563683  793 ESSRdQAFTLLLW 805
Cdd:pfam12460 233 KIST-QALEILIW 244
 
Name Accession Description Interval E-value
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
54-312 1.00e-109

Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal part, pfam12460, is an essential component of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly.


Pssm-ID: 433995  Cd Length: 258  Bit Score: 335.68  E-value: 1.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683   54 LGSSLENAEPRTRARGAQLLSQVLLQCHSL-LSEKEVVHLILFYENRLKDHhLVVPSVLQGLRALSMSVALPPGLAVSVL 132
Cdd:pfam14500   1 LGEYLTSEDDLIRAKAVLLLSEVLERLPKDkLSRQEVHVLVTFYCSRLDDL-ACLPEALKGLLALVRMKNFPPVEAVSVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  133 KAIFQEVHVQSLLQVDRHTVFSIITNFMRSREEELKGLGADFTFGFIQVMDGEKDPRNLLLAFRIVHDLISKdYSLGPFV 212
Cdd:pfam14500  80 RSLFQEVHVQSLLQADRYLVFQILDTLLEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLRVILSE-FDLGPFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  213 EELFEVTSCYFPIDFTPPPNDPYGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEILSAKLDSLQTLNACCAVYGQ 292
Cdd:pfam14500 159 EDLFDILFCYFPITFRPPPNDPYGITREDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGA 238
                         250       260
                  ....*....|....*....|
gi 755563683  293 KELKDFLPSLWASIRREVFQ 312
Cdd:pfam14500 239 EAVEPHLLTLWSALKFEILN 258
MMS19_C pfam12460
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
556-805 3.42e-51

RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision repair (NER) and RNA polymerase II (RNAP II) transcription. This C-terminal domain, along with the N-terminal, MMS19_N, form part of a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-epsilon). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly. This domain has a HEAT-like repeat structure.


Pssm-ID: 463594  Cd Length: 426  Bit Score: 185.16  E-value: 3.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  556 CLQALSAVSTHPSIVKETLPLLLQHLCQANKGNMVteSSEVVAVCQSLQQVAE-KCQQDPESYWYFHKTAVPCLFALAVQ 634
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYLLEnKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  635 ASMPEKESSVLRkvllEDEVLAALASVIGTATTHLSPELAAQSVTCIVPLFLDGNTsfLPENSFPDQFQPFQDGSS-GQR 713
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  714 RLVALLTAFVCSLPRNVEIPQLNRLMRELLKQSCGHSC-PFSSTAATKCFAGLLNKQPPGQQLEEFLQLAVGTVEAGLAS 792
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNLTS 232
                         250
                  ....*....|...
gi 755563683  793 ESSRdQAFTLLLW 805
Cdd:pfam12460 233 KIST-QALEILIW 244
Pdase_M17_N2 pfam18295
M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 ...
512-599 4.66e-03

M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 aminopeptidase (pfam00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyze the removal of unsubstituted amino acid residues from the N-terminus of peptides.


Pssm-ID: 408104  Cd Length: 121  Bit Score: 37.76  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563683  512 GTLATLYPGAFS--RHLLPKLAEE---LHKGESDVARADG------------PTKCSRH---FRClQALSA-VSTHPSIV 570
Cdd:pfam18295   7 GTLETLNELTLQdvAHLEPRVAELidrVASAHTYLPVADGcslvlsvtvaqlPTKASRHntpARP-HAISKlVKANVSGV 85
                          90       100
                  ....*....|....*....|....*....
gi 755563683  571 KETLPLLLqhlcqankgnmVTESSEVVAV 599
Cdd:pfam18295  86 KEVVVDVL-----------VCESENVLAS 103
 
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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