ID A0A316UDI1_9BASI Unreviewed; 1743 AA.
AC A0A316UDI1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA mismatch repair proteins mutS family domain-containing protein {ECO:0000259|PROSITE:PS00486};
GN ORFNames=BCV69DRAFT_280915 {ECO:0000313|EMBL:PWN23307.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN23307.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN23307.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN23307.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ819322; PWN23307.1; -; Genomic_DNA.
DR STRING; 1684307.A0A316UDI1; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1069..1085
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1743 AA; 186357 MW; 5B7E8E2831CBAB9C CRC64;
MSTPRGSSGA GKASSPAGGK GTLLGFFRKV DGPAPARGQA SSTADAGKNT ASRVAPVMDK
VTQAPTVKKP PQTVASSSKT SAASSSTKTA FPSPPSSTSG RSVSPVAPRI SNDTPFNKKI
GTPSASTGGT SSPFKSPTQP ASASRPSREG SKSASRGLVG VNAGSGQPTP PSSSPATAQL
LEDEGLDEED VMPSSSRRVA KKRPAYFESG SEGDGESDFE ADDDDDDDEA FSDASMSPAP
PSRSRHSAAP VAKKPKAAAS RPSAVASSSK PPPVSRPPFA RASTSATSNS RASPGEDGTP
KPAGGSTEFA FLNDRRDMDK NRPGDADYDP RTLYIPNNAW STMSKFEKQY FEIKQWNMDT
ILMCQKGKFY EMFLEDAYIV HRELDLKLSD RGRMPMVGVP EASFDMFASK LLALGYKIGR
VDQMETAVGL GMRKDKDKAK GVGTDIVRRE LRHVMTTGTM IEGLEDDLAN YCLALTETVT
EGEDGREVVA FGVCMLDAAT SEFSLSEWAD DQARSELETL LRSLRVKEII HKKGQLSKST
SRIIRNCVGA DCRITMLRDG KEWFDAEATD AQLEDLFGEG KAELPQAISA MLDKAEAMNA
LGGMFAYLTQ LSLLGDVASS KNFNVLDARR SAAGQPMKLD ANTLSHLCVL QNEDGSDTGT
LHRLLNRCIT PCGKRLFKIW LTHPLSEAKA IEERLDAVDD LLGNSDFEDA FSRMRGFPDF
ERLIPKVHSG KIRPGEFTRL LSSFKKLTPE IENLLQMAEG HDFRSKLLRG LLSSVPDVAT
LANEIDSMFI AEEDGSFQPQ PGVDEAFDEA QTLVEGVHEQ LEDELRSARK KLKLGATKKG
GCNWKHKGTN EIYQIEVPRN TRVPNDWLEI SSTNDAKGYY PPEVKSLVLT LKESRETRLA
ALKEFHARLF EMFNANAKTY LSAVRAVGEV DCLLSLAQTS YAMGEPTCRP TFVESERAVV
AFEELRHPCI AGSTDFIAND VKMGGDSAEV ILLTGGNMAG KSTTARTTAT GVILAQLGCR
VPAASATLAP VDRICTRMGA NDQIFKGSST FMVEMQEASR IIKDCTPRSL VIMDELGRGT
STFDGHAIAH AVLHHIIART RCLSFFLTHY LQLAYDFEGY PRCANKHMEV LVDDERREVV
FTYRLVNGVA ESSYGTQVAG LAGVPREICD RASDISREFA EATKQHQAER TTSALPVSTL
GDFAYLFRLG QGALPHIADH LGDRGNDGQV ASQLEVIRAQ LQRIGSRNQS NGGDGDVEMH
DAEKQPSGIS DGNGIDSTPK KATAAAEPTA PSAALSSSSK RSASYGGSNA RYQKRRLAEG
GDSSLQTGEE GSEDFLGGAS SPLRTHSSPL ASKSRKQQAR LPFGSASTSS ANSHSNGAGE
QLILDLGQKL QVTCTACQMS YDRSSPEDMA LHVRHHDRVT RGVEWTGKNL LRAGEVVDVG
SLPEASLVRA LGKGVLTVAA RRDNQSTPQM GGAGGAMDEL DALLAASPTS SGKKKNNGAT
VPLRILRYSF TGTAGGAIST DAGQADHLVA KKLQEVSTTV DEALGAAPLD EETRRRRGPK
MFLAIVAGRV VGAAVTGAVP PGSARRVVDI AEGTDNGSKS SAEGKDVDSN STATSTSQAF
ASSGDAIFLS SQPLPKYQPA PILGVHRIYV LPSLRRLGVG SRLLDAVLEH SVYGQNAEAL
LRQFGGRKGN VVAFSQPTEA GRRLAERWLM QGSGQRREAG GGGGATTNGG GERASGLIVF
QEE
//
