ID A0A199VYT1_ANACO Unreviewed; 1172 AA.
AC A0A199VYT1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072};
DE Flags: Fragment;
GN ORFNames=ACMD2_03723 {ECO:0000313|EMBL:OAY82164.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY82164.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY82164.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY82164.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
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|ARBA:ARBA00009340, ECO:0000256|RuleBase:RU367072}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAY82164.1}.
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DR EMBL; LSRQ01000543; OAY82164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199VYT1; -.
DR STRING; 4615.A0A199VYT1; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR GO; GO:0097361; C:CIA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
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; 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; 2.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU367072};
KW DNA repair {ECO:0000256|RuleBase:RU367072};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367072};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..79
FT /note="MMS19 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14500"
FT DOMAIN 117..264
FT /note="MMS19 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14500"
FT DOMAIN 656..1050
FT /note="MMS19 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAY82164.1"
SQ SEQUENCE 1172 AA; 130732 MW; 495602F6E8FD2902 CRC64;
VASIEATTKL VNNDLLSLLD LVKEMEMYLT TSDHVIRSRG ILFLAEVLAR ITSKPLDSVS
VSCLAEFFTS RLLSFEVLHC LLEEYPDAVV VLVLYLFQFY TFHILLYTFI IENSLFLVKG
DELLYGICEA VDEEKDPDCL MLSFQLVEIV IRLFPDPSDL VTRFAGDIFE ILSKYFPVYF
THGGGDELHA TRDDLSRALM NAFCSTPNFE PFAIPLLLDK LSSSLQSAKL DSLKYLTNCL
RCYGADRMLK HSKAIWLNLK DVIFSFPPQR PLVLTTESSQ DTERVEHQIG KEALSCLQTA
MLCLTSPDKD VFINLILEDE DVVKRFGFVL NEGYSVGTSV DIHGQLNALG SIFSTISKSS
TYFCTRVFQK YFPCLLDFLG VSRSGASYSI EMNNVNFPGR VNNAALYLCN DILSACKELT
LDSLVFSQDI LEQDTWWHVL KRFSDSLSYF AGSLVTTCNE AANSQIQQAV THSKIQQESI
LYSMKVLQTL ATFPEHYSPI SESVYHDILL MLISVVTCKY DDVYLWNLSL KTLGQIGSSI
EDIHDSAKGT IYSRTVVERA ISLLQVDDTA LPLSLKLDVV SEIGAIALDP MSRVLKALEE
AIVFHISKAC VDGRTESAET AICLLECYSC KLLPRFCTLQ DFDEVLVLFA IRLWEQMESL
VASKNEIKVQ GLLDSLMMTM KLLVASCSEE QQSLIVKRAY TIVSAVKCLP LQPFSPSSKL
EELRISPGFS IHNWLVSLFA SVVIALRPQT TLPDVDILLN MFIVFLLEGQ LPAAQALASI
LNKWPSNGNI SELSSVYTFD QAIDLVLEKC FTVLSSSSFL ANFYSSNDSK INAIAGLAWV
GKGLLMRGHE KVKEITMFFL KCLLSSQNSE IMQLNQKELD ARSLLATSAA DAFQLIMSDS
DVCLSKKFHA TTKPLYKQRF FSSLIPVLLS SVKEYATMNT KYTSVIPDYR TVLYRAFGHL
ISNTPLAAVV AESHKIVPTL VDCLGILSLN TQNKDLIYSL LLVLSGILMD KNGKEHITEN
IHLVINLLAK LVLYPHMMLV RETALQCLVA MSGLPHSRIY PMRLQVLRAV TKALDDKKWA
VRQEAVRCRQ AWSGIILPSF NTFVANKLWH QLLKEASIIE AIGAAGSGLN LSELLMNLTD
FSLEGAQSSF ESVLIGEARA TAVDVNSLCT KC
//
