ID   A0A1E5RR70_HANUV        Unreviewed;      1031 AA.
AC   A0A1E5RR70;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072};
GN   ORFNames=AWRI3580_g1636 {ECO:0000313|EMBL:OEJ89397.1};
OS   Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=29833 {ECO:0000313|EMBL:OEJ89397.1, ECO:0000313|Proteomes:UP000095358};
RN   [1] {ECO:0000313|Proteomes:UP000095358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3580 {ECO:0000313|Proteomes:UP000095358};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
CC   -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC       (CIA) complex, a multiprotein complex that mediates the incorporation
CC       of iron-sulfur cluster into apoproteins specifically involved in DNA
CC       metabolism and genomic integrity. In the CIA complex, MMS19 acts as an
CC       adapter between early-acting CIA components and a subset of cellular
CC       target iron-sulfur proteins. {ECO:0000256|RuleBase:RU367072}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU367072}.
CC   -!- SIMILARITY: Belongs to the MET18/MMS19 family.
CC       {ECO:0000256|ARBA:ARBA00009340, ECO:0000256|RuleBase:RU367072}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEJ89397.1}.
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DR   EMBL; LPNN01000004; OEJ89397.1; -; Genomic_DNA.
DR   STRING; 29833.A0A1E5RR70; -.
DR   VEuPathDB; FungiDB:AWRI3580_g1636; -.
DR   OrthoDB; 38995at2759; -.
DR   Proteomes; UP000095358; Unassembled WGS sequence.
DR   GO; GO:0097361; C:CIA complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039920; MET18/MMS19.
DR   InterPro; IPR024687; MMS19_C.
DR   InterPro; IPR029240; MMS19_N.
DR   PANTHER; PTHR12891; DNA REPAIR/TRANSCRIPTION PROTEIN MET18/MMS19; 1.
DR   PANTHER; PTHR12891:SF0; MMS19 NUCLEOTIDE EXCISION REPAIR PROTEIN HOMOLOG; 1.
DR   Pfam; PF12460; MMS19_C; 1.
DR   Pfam; PF14500; MMS19_N; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU367072};
KW   DNA repair {ECO:0000256|RuleBase:RU367072};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095358};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          56..321
FT                   /note="MMS19 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14500"
FT   DOMAIN          600..981
FT                   /note="MMS19 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12460"
SQ   SEQUENCE   1031 AA;  117846 MW;  AFD2E4A909EAF66C CRC64;
     MSFLEQQFXL FKNLFEKKNS NSLNETDDYY DNLMKEITFN LSNLLDEKKY TLLNVVTSIK
     DDITSVDDES RQCSLEYLSI ILSNIKKDTL LNNECNVIFD FFLSKILNSS IDFYCFKQIL
     NSFKTILTFE FLQKSFPGVQ HLLQFIQDEY NPNEFVASVR YSIFEILNLI RVNGFVQDES
     LYINAFLNVA NGEKDPRNLM ESFTLNKIIT STFNKDITYS HSQKLFDVLF CYFPITFKPP
     KNDPYKISSD DLKXALRAAI SNSDYFSIDV FPNLIDKLTA TSIIVKNETL KTLNECLIKY
     QKKSIVKYWQ PVWDALKNEV LRGSIDEVDE EYKVNNYKEA LNVIKTLFHR LADYETENFS
     FDTDLLNFSF EDIKHNFENN KNIKQSADIF STISTISIDM NEKVLKLVLP VFFEPINNNS
     ELDMESIKLI LMNISLFLKE VAAFKAEMNP NSSIVHXKDE LLVFLTKNLS SISDNEIHIK
     TLSIFQLTYL IKIPGYLKRD EIFMVSEILL NIFNSSIGAN KNIFLSCLEC IKSIVAANYT
     DVIKDVILSS LLQNLKTAES NQIFDKNLKT XANIVFSCSS LTSYVVSELV DYIQPSSVVD
     LESCFLVLST VYTIIDSRLK SVIQKDSFNA VVKIDNSADL REIXNELITP ETVDALYQII
     FMYDQIFDHD GILEVISLVF FNYVLVLTPD ERVLFCSKYI KPIMEQVFTN PNRLSILFVK
     VYAALDIEND VLPAELVYKN SLNVVFKIND QVSPITSMNY YMITALAVNK DKSLISSIDN
     LTEIYENSNH NVGLMFWLAK GLCLSSHKES KNIVKFLLDL LNDSVLGEQI AESLQILMVN
     IPIFRKITFL ESKNLNINNL NQQKVFHLIV PTLINKYKET DDESLKSKCL TALSHVLKST
     PINIKNNFTQ DLFPLLVSAL DASASDVVAA SLQTICDTFV SQPEILLSHV DTLIMKTLSL
     SKILKNGPKV RALSLQTLLL FVNVVPINVL QPYKNMIIKG LIPVLDDPNR NVRKLAVDTR
     QAYFDLGMAI A
//