ID V5EGC2_KALBG Unreviewed; 1332 AA.
AC V5EGC2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072};
GN ORFNames=PSEUBRA_SCAF10g05567 {ECO:0000313|EMBL:EST09581.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09581.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(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. {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; KI545852; EST09581.1; -; Genomic_DNA.
DR RefSeq; XP_016294570.1; XM_016434137.1.
DR STRING; 1365824.V5EGC2; -.
DR GeneID; 27416733; -.
DR eggNOG; KOG1967; Eukaryota.
DR HOGENOM; CLU_005943_1_0_1; -.
DR OMA; LCAIEVI; -.
DR OrthoDB; 38995at2759; -.
DR Proteomes; UP000019377; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 38..218
FT /note="MMS19 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14500"
FT DOMAIN 260..402
FT /note="MMS19 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14500"
FT DOMAIN 711..1267
FT /note="MMS19 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12460"
FT REGION 218..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 143083 MW; A73D03455F70E1D9 CRC64;
MSDPAQAIRA FIVGSFQELP PSIVDDIGSG SVSLLGVVRL LGEYLTSEEE EIRTRAVQLL
SDITCHFLES PSQTKEPLAS IFTIQAVRTL TAFFADKIAD GVIISDNFVR SAKAPEVLPD
SASRARKNEV EQKTLQGSAM LVSSLKALTV LSACRAPTET TPAAQPPVKG FGQEQAHAVA
HALFTNVVAT NHPQSLRFII YRLLDSLVAH HRAALKAYRS SASDTTDEQP SEATPSATTP
MEVDTSSDEA AAASQSETCQ GKDFLRGYVK MVQGEKDPRN LMVLFGVDKV LLTEWVMDRE
MTGKFFDITF CYFPITFRPP PDDPYGITSD DLKVALRAAI CASPAMAPLG YPLLLEKLSA
AGGPAKLDTL RTLIAAMPVY GRAAALANAL KLWEGLKIEI FHATDDETGD LAVDTLTVLL
HVLYHGVDPP EGVAPKMVHD CLVELEEPGK SLAKASIKVL SCLIRASAST AYLAVYGFMD
QMIKMFADPE DLAQRTPILA GIGELLEALA KVYRHAELAR AEDETKAKPA EIGSGQLLPM
TASERSYTGD NRPLDPFLAD LLNCLSNGLR STSYRRSAML VYSSVVSISI LSSGPTSEPG
TTEQKALLDF DELSFLTREV SSLLTSSIGD DVREEALCAI EVISNERTST SVAATNPTAQ
VIEEVVLPVL LEKLPDRIEP LTDPESRTTG NAMDDTEAEL DLVKANIRRS LGALSRLCVA
PFLFEAVVVK LFTKLELCCR PSRFGVTESS EEGEAESTVR EQLAALQEAN VGYARGLILT
LQTMVDLKRQ NGHRDLVKYA QTLPSRLVGL TLSGLGTGEG GREVSIAARP AVVADTAALL
GTFVKLLDVN RQKDLLASLN TTFVRGQSTF VTEGGEEGVS LIPAKSPLAQ TFEPFTTTSE
TPFATASRNT VALLSAAVVA SAPAAGVVVL TPSTPTSAHD AALSSISLLL SFSLSVPSSS
SPSSALQLNS TYWLVCALTN KFIDETSPAF LDTLDVFWTT HVKPPSSSSP RRRIAVQMWM
WLTRALVVKS SKLAEAMLNR VLIEVFDDVA GKIVGASDPS QLVPSGAAKG EVEWAFARAV
ARDLSAIVGV ADDGVATKEN GFTVRLLWKQ KVFSFLVPRL LESYDNAVKL TRRHAHTHVH
SSTCDHEEKE GGEVEGQTIY LVTLAGLLPS LPSSMLVERL PGLFPLLIQA LELPDARARS
AAANAITVAC EVGKKLPSSN EGEFDPTTLI AGHLQSITAK LLVNIRASKF TPVSTRVAAL
RTLTSLAAKP DEEDETGVKK DIGGLAHHHL HPLRGSVLKE LGRDGRGIDD KVRAVRSVAV
DARDAWFAVS ET
//