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Database: UniProt
Entry: W9I3F9_FUSOX
LinkDB: W9I3F9_FUSOX
Original site: W9I3F9_FUSOX 
ID   W9I3F9_FUSOX            Unreviewed;      1164 AA.
AC   W9I3F9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072};
GN   ORFNames=FOYG_11313 {ECO:0000313|EMBL:EWY87031.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY87031.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY87031.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; JH717845; EWY87031.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9I3F9; -.
DR   OrthoDB; 38995at2759; -.
DR   Proteomes; UP000030753; 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   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; 2.
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:UP000030753};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          65..324
FT                   /note="MMS19 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14500"
FT   DOMAIN          761..1084
FT                   /note="MMS19 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12460"
SQ   SEQUENCE   1164 AA;  128172 MW;  1AEFBCA5625D15DB CRC64;
     MADFRQWALE FVLADNEGQQ TAIAKKAANE IQTAAANTNP VARWVEAVQP WMPGGGNEAE
     NETPDWTARA KALEFLSRTL DFLSNDILKP SQVKLLVSFF GAMFEVDHKA GIMPSASALS
     RIVAMKSFQR HMGHDIIQKV CSLKDDFPRQ VSKTRLEIYE LIRLLMTTPG VASDLQNTHG
     SSAGFMLDLI QLCRSERDPE CLMMWFDILR LFMSEYTVSQ DVLEEVYGVF KPYFPISLPR
     ASQVAITPEE LKLQLRKCFS ANHLLADKVF PFLLGKLDQG DAVTVNVKLD ILKTMQACLD
     EYSHPQKAIA PYANQIWGSL KYEVRNGEIE DTIWGTLEVL KSLTRRLAGD SLRDYTLSVT
     RDCVPDLATT MYASSAGRLM VSVLSSKPSA FVLMAAPVIT HIKENLRHPK APVHTQDLLK
     VLHIILETRF LLVDTNMAAE DREDFAAIDG FFKSLYQDTF KNPVSLGSKP DASYDDIKVA
     TQAVPGAGVL VCQRPSKSLD LSNNGASDIS QRLLPDSTCS EICSSLFAIL KKSGPGYPRS
     SGGDELINDA AQALQRAIRY FPRGFDGLVD ESLSIIRSSR QNGKVPDTVE TIKTLGGLVA
     YLGSSELPFT PRDGFDHFIY SIRAFLSELF DSLESKSDPE IWCALVATIQ STIRYFNDAC
     LAKNPDKEFS IEDEPLQKIG SAYPALSLLG GETVTESSPE YHSQVPQSAS VAEIRSQFLL
     VTLFIARQLY RRATKVVDTH PQTGKQALSL SDDFANVDEV SGHQYLHLIS TLAGFVIHEF
     SETQQTSLKA ESFAISLFRD ESIRVPQTAP ETQSSLENGS SWSWLASEAP NVLAFGILQA
     LQPSAVSRLF DIGVAQELIL SGFAADTNFS RPVTLSILTI LANKFKVETV PSLITTLEQR
     SSSLSPASTS GNDASRLEQI TSIYALVAGM VRRYSGKEAK TLLDVVKESP KDPKLGTELA
     RRLEMIVAPQ QPLTKECYAI VKPLWTQKVY FQLVSPMLQA ATGKETEVQD QQVKANYSTA
     VLLMVKHMNF PIYEADADSI LRISIAVAQN SGIGPETKAA LDVIKNTLAE APEKGKGHIR
     SIIKICSSAF SHKPSPASAD VETEGACGKL ALEIVGSLPQ TYDSQHLIPH APQVQRQLTL
     VCGHRVREVR KTARLARAAW ADLK
//
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