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Database: UniProt
Entry: B9WDB5_CANDC
LinkDB: B9WDB5_CANDC
Original site: B9WDB5_CANDC 
ID   B9WDB5_CANDC            Unreviewed;      1171 AA.
AC   B9WDB5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072};
GN   OrderedLocusNames=Cd36_81370 {ECO:0000313|CGD:CAL0000170382};
GN   ORFNames=CD36_81370 {ECO:0000313|EMBL:CAX42667.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42667.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX42667.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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|RuleBase:RU367072}.
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DR   EMBL; FM992690; CAX42667.1; -; Genomic_DNA.
DR   RefSeq; XP_002419082.1; XM_002419037.1.
DR   AlphaFoldDB; B9WDB5; -.
DR   GeneID; 8047024; -.
DR   KEGG; cdu:CD36_81370; -.
DR   CGD; CAL0000170382; Cd36_81370.
DR   VEuPathDB; FungiDB:CD36_81370; -.
DR   eggNOG; KOG1967; Eukaryota.
DR   HOGENOM; CLU_005943_1_0_1; -.
DR   OrthoDB; 38995at2759; -.
DR   Proteomes; UP000002605; Chromosome 3.
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   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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          47..324
FT                   /note="MMS19 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14500"
FT   DOMAIN          614..1128
FT                   /note="MMS19 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12460"
SQ   SEQUENCE   1171 AA;  135023 MW;  15F53EC99D435D2A CRC64;
     MVEHNIPILI NQYIAASSGN DEEAVSNYIF ELSNLITNDE LSLLQFIQHL GPSLTSDKDL
     IRSKSIECLS KTIISLSDSK LTKQDINVLM EFLLNKLIDN DQICLQYSLM GINSLICKKN
     FLADTNIEKI LQNLYKNYDP KKNLAKIRFE TFQILLNLLN QFNQYLKSSI QLTNLYIKTF
     IHIASGEKDP RNLLLSFELN SKINENFQFL VDNNELHQQF ITDLFDICFC YFPISFKPPS
     NDPYKITSEQ LKVALRKTIA SQSKFASEAF PNLIEKLTST NPTIRNDTLK TLQLCIENYS
     NNDPTIIEQY WMTIWNALKF EILHNDIRSN FNPTNNTIVA LDYDEIDDND EFKPLVLTLV
     ILNQLIMKLP QPEIMLHTVV EELKPNLEII KEKSIKSSLI LSSLGSTSIE NLNYIVDFLF
     QYQVWGKFLN IDKKEEPNQK QEIDTNDDIS LNIAKQRDLI DSIGFVLTAY QVLKPTTTNC
     HLLDYKDYIL IFLGQLLNIT SNLEKTLKCK IIQQLIKLIK LPGFLNINEL ELILGNYFKD
     FFLLGTTTTT SSSSSSAGKK KDVILQEIIN GLIEVSQDSQ ITSMTIEFII NPILNQLLNN
     DDTEIDIETF QFQLEIVGDL CINYQILEVI SIRLLNKLSL IINNQSNDNL QLYKLIINLF
     IESIKKIESI QQFLTNSWYK HFIPKFMENL LIILPVKKSF FDDNDYKSDN YELFEIVGDL
     LGLIIKFIDV SKHQEILDQL NQAFITNNDQ TNENYGLGPF KYPSNLLIEP TNYINIYNKI
     LSSIDKSCVF KTNIDQQVIE LVINLIYKIG SKDEYLRLQY LQTLCLLINK FIKNVDIDII
     ESILKLKLLE EFNHKEFPIT EKDFISFEIF IWILKGLIIK LDKLGINYLN QLLELFVITK
     NYKFKQLIGK SLQILFIDLK IFTNEKITST TTTTTTTTTT TNSVDTSSND LKSSNQLISK
     VKNLQIKSLY KQHIFVIILP YLINNDDSNN FGTDNDFNLK FNSLSLIIEN LSINGNNNIL
     INQLSEILPI TLYSLIKIPI DSNSNSNLLA SLIILNIILK EEEKEEKEKE KDINNTNLSL
     LTKDNIIELI PILIKLITTT TTNRKSKSKS NSSNIDIKIL SLKNLKLIIE KFDDIINKSK
     LLNDLLPGLD DKKRVVRKLT IDLRQLLYDS K
//
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