MMS19_DICDI
ID MMS19_DICDI Reviewed; 1115 AA.
AC Q54J88;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=MMS19 nucleotide excision repair protein homolog;
DE AltName: Full=MMS19-like protein;
GN Name=mms19; ORFNames=DDB_G0288217;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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). {ECO:0000250}.
CC -!- SUBUNIT: Component of the CIA complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR EMBL; AAFI02000109; EAL63339.2; -; Genomic_DNA.
DR RefSeq; XP_636848.2; XM_631756.2.
DR AlphaFoldDB; Q54J88; -.
DR SMR; Q54J88; -.
DR STRING; 44689.DDB0235234; -.
DR PaxDb; Q54J88; -.
DR PRIDE; Q54J88; -.
DR EnsemblProtists; EAL63339; EAL63339; DDB_G0288217.
DR GeneID; 8626516; -.
DR KEGG; ddi:DDB_G0288217; -.
DR dictyBase; DDB_G0288217; mms19.
DR eggNOG; KOG1967; Eukaryota.
DR HOGENOM; CLU_005943_0_0_1; -.
DR InParanoid; Q54J88; -.
DR OMA; FSFMPEF; -.
DR PhylomeDB; Q54J88; -.
DR PRO; PR:Q54J88; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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: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 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Nucleus; Reference proteome; Repeat;
KW Transcription.
FT CHAIN 1..1115
FT /note="MMS19 nucleotide excision repair protein homolog"
FT /id="PRO_0000356170"
FT REPEAT 944..986
FT /note="HEAT 1"
FT REPEAT 990..1032
FT /note="HEAT 2"
FT REPEAT 1035..1075
FT /note="HEAT 3"
FT REPEAT 1078..1115
FT /note="HEAT 4"
FT REGION 587..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 127373 MW; 2AE75FD6A079A34F CRC64;
MTSNITELNK WIEGYVNPQS EESVKTNAIN MVLLYMKSNK IDLQDVVQGL GDYLKSNDSI
LRARGTLLLS EVLCRLPDLP LNQDQVHFLA MFYCDRLQDY ACSSEVVKGI TGLITNHTPD
YPDNQKLLRN IFSEVHPTSL TQAHRKMVLQ VIDIMFNKCL SEIQELKNDF MVGYLQFIDN
EKDPRNLIFS FKLLPKVIYN IPEHKHFLES LFEIISCYFP ISFNPKGNDP NSITKDDLSN
SLLNCFSCTP LLAEHSIPFL IDKICSNLIE TKIEALQTLV YCCDRYGGFA VQPFLEEIWS
TLRTLILTHK NTTVIEESKK TIFYLTRSFT KERKVLESFL SIMIKECLHH IKSSQDSKIA
IYCASILYQS VSASLLSSKI ILIHIFPNLF NFLSELQKQD TVQKVNEQNS VIALFNDLLK
ANSIAFEMYS NENKEPNPLE PFVDQLFKLF SDLLLLNSSS SIRSNSIECL SNLYISKKVH
TTEQDDDDSE QITNEFLLDL EKRQFIIKSL VSLLNSSDNT LRHKSLDSLF TIASNEDPSV
LNLYVIPTLL QMINHSSCNI NTTNNKINNN NNNNNIVIKN NKCQDEHCNE DHSNKNENNN
NSNENSNGNS TSGSDDDLKH YLEAFTKLCT HQPLLESVIP QIQVLLQHNI KETYQSNEDF
EKSILILQSI SFILEKSTNI KSMTICSKSI LFPLIKGLYK QELISSSNDN NNNNNNNSNR
FNQILTPTLK MIHSIFENIS IESQKPLLEK LIKLFLNGDT LVINYQLPTT TTTIIKPFEK
SSPYKYLIPI FTTIISQSKL DLSENNELKQ SLYQMSLDVN VDDSIAISCS KAYSSIINKQ
QQQQQQDQIN FNFFNDNLLK VINDTTTPLP LKIRHLDLFT WCTKALLTNG NSINIKLGSC
LADIISNENV ELSYHASKSF GILLSETDVL NEKSGSIIKI LFEQKFFTLM FPILLESFKV
SKNKELQTIS SHYLIAISNL LKHVPKEILL AELNEILPIV MQSLKSSDNN DQVQLLDSSL
QTLTMLINET PSSFISYLDS LIPSLIKIST KSTKYNLKRS ALEILTLLSK SIPFVNLFPY
KTQVVTDIIP CLDDKKRIVR REAQKCRNSW YILQK