ID   MMS19_DANRE             Reviewed;        1043 AA.
AC   E7FBU4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=MMS19 nucleotide excision repair protein homolog;
DE   AltName: Full=MMS19-like protein;
GN   Name=mms19;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96T76}.
CC   -!- SUBUNIT: Component of the CIA complex. {ECO:0000250|UniProtKB:Q96T76}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96T76}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96T76}.
CC   -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR   EMBL; CU459170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU459184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7FBU4; -.
DR   SMR; E7FBU4; -.
DR   STRING; 7955.ENSDARP00000098600; -.
DR   PaxDb; E7FBU4; -.
DR   PeptideAtlas; E7FBU4; -.
DR   ZFIN; ZDB-GENE-120316-2; mms19.
DR   eggNOG; KOG1967; Eukaryota.
DR   InParanoid; E7FBU4; -.
DR   PhylomeDB; E7FBU4; -.
DR   TreeFam; TF314469; -.
DR   PRO; PR:E7FBU4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0071817; C:MMXD complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006259; P:DNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 2.
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; PTHR12891; 1.
DR   Pfam; PF12460; MMS19_C; 1.
DR   Pfam; PF14500; MMS19_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1043
FT                   /note="MMS19 nucleotide excision repair protein homolog"
FT                   /id="PRO_0000419481"
FT   REPEAT          879..917
FT                   /note="HEAT 1"
FT   REPEAT          921..959
FT                   /note="HEAT 2"
FT   REPEAT          962..1000
FT                   /note="HEAT 3"
FT   REPEAT          1003..1041
FT                   /note="HEAT 4"
SQ   SEQUENCE   1043 AA;  113550 MW;  0F148742402985B8 CRC64;
     MAADNNVLLG LVEEFVSGQV DSKAADTSTG VKNGQFTVLQ LVEALGVSLT SSQPQTRGRG
     VQLLSQVLQE CYSGLSEREV EVLIAFYENR LKDHYVITPH VLRGLKALAK CSVLPPGSAV
     SILKSIFQDV HVQQQSLMVT ERSCVYNILI SLMESREEEL KGLGADFIFG FVQSVDGERD
     PRNLLLAFQV AKNIIYRGYD LGKFVEELFE VTSCYFPIDF SPPPNDPHGI TQEELILSLR
     AVLTGTPRFA EFLLPLIIEK MDSDVQSAKV DSMHTLAACG QTYSHKELAE FLPGLWSSIR
     REVFQTASER VESAGLSALS SLVSCLSRSV LNSDSEDSLQ VFLNLVLKSD CQHHLCEPDL
     KLVWPSAKLL QAAAGASYRA SLIGTQAVIP ALLDQYNNRT QCAQRRTLLE VLQGFVQPTP
     LSRPADGVSC ISTHTHEEES VLVAFQQSLC TVVFSALSET SAGLQVTATR VLTALSQQPG
     LLSQTDVENA VDHLTRLILE EEEAQVSLAV VECSGSLAHL HPHAFVSRMI PQLKEKILSG
     RVHTVMEKTL SGSLYECSGA VRRRCVAALA SVSSQPSVVQ ESSPVLLQVL TSAHTGCCGF
     SVEEVIAVCI SLQRIAVHAR DNEAIGQFFH DIIIPRLLGL TLQAALQSKD SGHISPLTDE
     AVLSAIVPVI STACAALKPE SASRMAAQAV SLFLDGDTSF LPENAFPSQI QPLQSQADSR
     GPSQLVCLLM ACVCSLPRSV EIPDMDRLLV QLEDLSCTSP HLFSYTFASK CIAGLVNKRP
     AGAALNAVLD RVLKRVSLEL EETSSTHRTQ AFTLLIWVAK ALLLRYHPLS TALTDKLFSL
     LSDSALGSLV ADGFCVLMND SPDVLNRDCH ADVRIMYRQR FFTENSSKLV QGFNSAEQAK
     KSCYLKALSH IVNNLPREVQ LTELPALLPL LLEALSCVDQ GVQLSTLSCL QPVLLESPAA
     LNTQLEALFT RLLALTTSPA MKVRMASLRC VHALSRLPEH MVMPFRARVL KALAAPLDDK
     KRLVRKEAVA ARGEWFLLGS PGG