ID   MMS19_SCHPO             Reviewed;        1018 AA.
AC   Q9UTR1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=DNA repair/transcription protein mms19;
GN   Name=mms19; ORFNames=SPAC1071.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC       (CIA) machinery that mediates the incorporation of iron-sulfur cluster
CC       into apoproteins specifically involved in DNA metabolism and genomic
CC       integrity. Acts as an adapter between early-acting CIA components and a
CC       subset of cellular target iron-sulfur proteins such as rad3/xpd and
CC       dna2, thereby playing a key role in nucleotide excision repair (NER)
CC       and RNA polymerase II (POL II) transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UTR1; O74560: raf2; NbExp=2; IntAct=EBI-15934093, EBI-904886;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB59878.1; -; Genomic_DNA.
DR   PIR; T37484; T37484.
DR   RefSeq; NP_594352.1; NM_001019773.2.
DR   AlphaFoldDB; Q9UTR1; -.
DR   SMR; Q9UTR1; -.
DR   BioGRID; 278036; 151.
DR   DIP; DIP-59170N; -.
DR   IntAct; Q9UTR1; 2.
DR   STRING; 4896.SPAC1071.02.1; -.
DR   MaxQB; Q9UTR1; -.
DR   PaxDb; Q9UTR1; -.
DR   PRIDE; Q9UTR1; -.
DR   EnsemblFungi; SPAC1071.02.1; SPAC1071.02.1:pep; SPAC1071.02.
DR   GeneID; 2541536; -.
DR   KEGG; spo:SPAC1071.02; -.
DR   PomBase; SPAC1071.02; mms19.
DR   VEuPathDB; FungiDB:SPAC1071.02; -.
DR   eggNOG; KOG1967; Eukaryota.
DR   HOGENOM; CLU_005943_1_0_1; -.
DR   InParanoid; Q9UTR1; -.
DR   OMA; FSFMPEF; -.
DR   PhylomeDB; Q9UTR1; -.
DR   PRO; PR:Q9UTR1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0097361; C:CIA complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; EXP:PomBase.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; ISO:PomBase.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; Nucleus; Reference proteome; Repeat;
KW   Transcription.
FT   CHAIN           1..1018
FT                   /note="DNA repair/transcription protein mms19"
FT                   /id="PRO_0000356171"
FT   REPEAT          857..895
FT                   /note="HEAT 1"
FT   REPEAT          899..937
FT                   /note="HEAT 2"
FT   REPEAT          940..981
FT                   /note="HEAT 3"
FT   REPEAT          984..1018
FT                   /note="HEAT 4"
SQ   SEQUENCE   1018 AA;  114670 MW;  92903717B942EAEB CRC64;
     MSSNLVALYL FSIDRSQDEA NDVVDRIVEE IVTDRMGIVD LVTSIGEYLT DNNISVRAKA
     VLLLSQTLGE LPKDRLPAKH VSVLLQFYLS RLDDEVTMKE NALGIGALLN MQNFPAQKIV
     DVCKALFSST DMPKYAQATR LNILKVFETI IDNYLFFISS QTRDAFFSGI CSTFAGEKDP
     RNLMLVFSML KKILSTFPID GFEQQFFDIT YCYFPITFRA PPDATNLAIT SDDLKIALRE
     TLVANDAFSK LLLPALFERL KASTVRIKID ALNIYIEACK TWRVGAYLWS AKDFWESIKQ
     EILNSTDAEL QNLALGALNT LASKFYKEEG FSSSFTEFVD MILIQLSQRL LEDVNVKSCG
     SCAAVFASLA SISVETFNYC SCNFLPSVLD LPMVNEPLEK QKGMLVFLEY VYKCLVLLYG
     KWRSKNQADI DNPLLVYKDK QLSFVSGSLM GTAKDETEIR MLALKVIFLM ASIKNFLTES
     ELTMVLQFLD DIAFDFSDPI KKKATECLKD LGLLKPDFLL LTSFPFAFSK LTDDVTAKSS
     SEETFKQYLS VLVSISEERS LFKALVIRLV EMLKDQFKSK EMSVDLVESI VQSLSVAFKE
     RNDRNEQEIP FFFEELLKQL FTLCFANCES MNVRCLIYVS QTINEIVRVN HFEFQEKFVG
     QLWKLYMENS NSDLIETEGC EKAAERFTLA ASLSDQKFLN LVVLLQGGLN GLSKKLHFIE
     KLNIELLNLL INVVFVTESP GVKISALRLI SSLINKCEKD EDISSFISSK GVTSLWDKVY
     TGTPKESEAA LDVLAWVDKA LVSRKHSEGI PLAFKLLDTL NLQNVGDSSV KALSIIIKDD
     PALSKENSYV EKLLYKQRFY ASVSPKILEH ISTATGGEKS LYLMLLSNVI GNVPKEIVIP
     DMPSILPLLL QCLSLSDISV KLSTLNVIHT SVKELTSLLT EYLDTLIPSL LAIPKDMNNP
     TVVRLLALKC LGSLPEFTPT TNLQLFRDKV IRGLIPCLDD PKRVVRTEAS RTRHKWYI