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Conserved domains on  [gi|574957012|ref|NP_001276333|]
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MMS19 nucleotide excision repair protein homolog isoform 3 [Homo sapiens]

Protein Classification

MET18/MMS19 family protein( domain architecture ID 12168131)

MET18/MMS19 family protein similar to Saccharomyces cerevisiae DNA repair/transcription protein MET18/MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MMS19_C pfam12460
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
396-823 4.32e-123

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: 378.53  E-value: 4.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  396 CLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVaqSSDVIAVCQSLRQ-MAEKCQQDPESCWYFHQTAIPCLLALAVQ 474
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYlLENKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  475 ASMPEKEPSVLRkvllEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVsfLPENSFPSRFQPFQDGSS-GQR 553
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  554 RLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSC-PFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLgS 632
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNL-T 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  633 GPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTD 712
Cdd:pfam12460 232 SKISTQALEILIWITKALVLRNHPLATELLDKLLELLSDEELGQLAAKGFGILVSDDDDVLSKENHANIRLLYKQRFFNT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  713 NVPALVQGFHAA-PQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDCVVQLSTLSCLQPLLLEAPQVMSL 791
Cdd:pfam12460 312 VLPKLVEGFKSAdDSSIKPNYLTALSLILKNVPKSLLLPELPTLLPLLLQALDLPDAEVRLSTLETLLSLLEEAPQLVSE 391
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 574957012  792 HVDTLVTKFLNLS---SSPSMAVRIAALQCMHALT 823
Cdd:pfam12460 392 HLSSLVPRLLKLStpsSMNSAKVRIAALQCLGLLP 426
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
1-153 8.89e-70

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: 231.29  E-value: 8.89e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012    1 MRTREEELKSLGADFTFGFIQVMDGEKDPRNLLVAFRIVHdLISRDYSLGPFVEELFEVTSCYFPIDFTPPPNDPHGIQR 80
Cdd:pfam14500 107 LEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLR-VILSEFDLGPFAEDLFDILFCYFPITFRPPPNDPYGITR 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574957012   81 EDLILSLRAVLASTPRFAEFLLPLLIEKVDSEVLSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQ 153
Cdd:pfam14500 186 EDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGAEAVEPHLLTLWSALKFEILN 258
 
Name Accession Description Interval E-value
MMS19_C pfam12460
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
396-823 4.32e-123

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: 378.53  E-value: 4.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  396 CLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVaqSSDVIAVCQSLRQ-MAEKCQQDPESCWYFHQTAIPCLLALAVQ 474
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYlLENKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  475 ASMPEKEPSVLRkvllEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVsfLPENSFPSRFQPFQDGSS-GQR 553
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  554 RLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSC-PFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLgS 632
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNL-T 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  633 GPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTD 712
Cdd:pfam12460 232 SKISTQALEILIWITKALVLRNHPLATELLDKLLELLSDEELGQLAAKGFGILVSDDDDVLSKENHANIRLLYKQRFFNT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  713 NVPALVQGFHAA-PQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDCVVQLSTLSCLQPLLLEAPQVMSL 791
Cdd:pfam12460 312 VLPKLVEGFKSAdDSSIKPNYLTALSLILKNVPKSLLLPELPTLLPLLLQALDLPDAEVRLSTLETLLSLLEEAPQLVSE 391
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 574957012  792 HVDTLVTKFLNLS---SSPSMAVRIAALQCMHALT 823
Cdd:pfam12460 392 HLSSLVPRLLKLStpsSMNSAKVRIAALQCLGLLP 426
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
1-153 8.89e-70

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: 231.29  E-value: 8.89e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012    1 MRTREEELKSLGADFTFGFIQVMDGEKDPRNLLVAFRIVHdLISRDYSLGPFVEELFEVTSCYFPIDFTPPPNDPHGIQR 80
Cdd:pfam14500 107 LEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLR-VILSEFDLGPFAEDLFDILFCYFPITFRPPPNDPYGITR 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574957012   81 EDLILSLRAVLASTPRFAEFLLPLLIEKVDSEVLSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQ 153
Cdd:pfam14500 186 EDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGAEAVEPHLLTLWSALKFEILN 258
 
Name Accession Description Interval E-value
MMS19_C pfam12460
RNAPII transcription regulator C-terminal; MMS19 is required for both nucleotide excision ...
396-823 4.32e-123

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: 378.53  E-value: 4.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  396 CLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVaqSSDVIAVCQSLRQ-MAEKCQQDPESCWYFHQTAIPCLLALAVQ 474
Cdd:pfam12460   1 ILEALADLSTEPQLFETLVIRLLNKLDLVCKAESS--SAYAFALLSTLLYlLENKKLIKQFDVNSYYDRIVPRLLNLFID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  475 ASMPEKEPSVLRkvllEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVsfLPENSFPSRFQPFQDGSS-GQR 553
Cdd:pfam12460  79 AALISSDDSVLT----DERLLELLGRIINLIVRSLSVEKQQEILNDVYTLFLTGDV--LQSIPAPSNFLPLQPSASsLQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  554 RLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSC-PFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLgS 632
Cdd:pfam12460 153 RLVILFTAILAALDKEVKLPDLSELLDKLVRLLASSATsPFQRLAYLRLLALLVNKFLDDDRLEELLDFLDDLLDSNL-T 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  633 GPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTD 712
Cdd:pfam12460 232 SKISTQALEILIWITKALVLRNHPLATELLDKLLELLSDEELGQLAAKGFGILVSDDDDVLSKENHANIRLLYKQRFFNT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012  713 NVPALVQGFHAA-PQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDCVVQLSTLSCLQPLLLEAPQVMSL 791
Cdd:pfam12460 312 VLPKLVEGFKSAdDSSIKPNYLTALSLILKNVPKSLLLPELPTLLPLLLQALDLPDAEVRLSTLETLLSLLEEAPQLVSE 391
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 574957012  792 HVDTLVTKFLNLS---SSPSMAVRIAALQCMHALT 823
Cdd:pfam12460 392 HLSSLVPRLLKLStpsSMNSAKVRIAALQCLGLLP 426
MMS19_N pfam14500
Dos2-interacting transcription regulator of RNA-Pol-II; This domain, along with the C-terminal ...
1-153 8.89e-70

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: 231.29  E-value: 8.89e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957012    1 MRTREEELKSLGADFTFGFIQVMDGEKDPRNLLVAFRIVHdLISRDYSLGPFVEELFEVTSCYFPIDFTPPPNDPHGIQR 80
Cdd:pfam14500 107 LEKHREALKTLGEDFVYGFIQLIDGEKDPRNLLLSFSLLR-VILSEFDLGPFAEDLFDILFCYFPITFRPPPNDPYGITR 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574957012   81 EDLILSLRAVLASTPRFAEFLLPLLIEKVDSEVLSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQ 153
Cdd:pfam14500 186 EDLKAALRDCLSATPLFAPFAFPLLLEKLDSTSPSAKLDSLKTLTACIENYGAEAVEPHLLTLWSALKFEILN 258
 
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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