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Database: UniProt
Entry: A0A0P1BGU2_9BASI
LinkDB: A0A0P1BGU2_9BASI
Original site: A0A0P1BGU2_9BASI 
ID   A0A0P1BGU2_9BASI        Unreviewed;      1583 AA.
AC   A0A0P1BGU2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   SubName: Full=Dna mismatch repair protein msh6 {ECO:0000313|EMBL:CEH15177.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH15177.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH15177.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CCYA01000258; CEH15177.1; -; Genomic_DNA.
DR   STRING; 401625.A0A0P1BGU2; -.
DR   OrthoDB; 168255at2759; -.
DR   Proteomes; UP000054845; 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   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; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
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; PF00488; MutS_V; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054845};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1087..1103
FT                   /note="DNA mismatch repair proteins mutS family"
FT                   /evidence="ECO:0000259|PROSITE:PS00486"
FT   REGION          1..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1254..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          830..857
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1583 AA;  172532 MW;  950B731CC3ED23CA CRC64;
     MAGQKTLLSM WAKKPSAASS SASSSTPAPS LKGTNSATQR AVQVKDAAPS RPAKAASPSS
     ASTVRSAPLP NKRAAHSPVE STKKAKRDKE RESMDNALST PPVSVSPQQR PAKPAPAHSS
     PMTAPPSSRQ ASESPMKKSR SSLSKKAKAM VTSTQDDLDE DMEDIIGPTR RRTAQKRPAY
     FESDSEEQGN ASDSEDAFEP KRSVKPARNG KKRKSSGADD DWLVDDGAIE QESDAASVSD
     AAVESEDEPV PRKRNNTNAS SSKIAAASSS KGSGVQADAM QAFKMGSLGS ASPANGRPSG
     MQKSSSMSHL TKAERRVLDE RKKKAENEQA YSFLRDLRDK DGNRPGDAEY DPRTLYIPNG
     AWKDFTPFEK QFWEIKQKHW DTVLFFQKGK FYELYEEDAL IGHREFDLKL TDRVKMKMVG
     VPEGSFEQFA NKFLALGYKV GRVDQCETAV AKGMRVGEKS RGGGSEIVRR ELRHVLTGGT
     IVDSACLPDD MGSYCVAIKE TEAVPGQPIF GVCVLDAATA EFRLSEFEDD VSRTKLETML
     RSLRLRELLH EKAGLSQRTL RILRNTLPSS CQVTMLKSGT EYLDHDAAME RLEQLFGSSA
     DSHEAWPEAI TSMLDRDTAM SALGGMLWYL EQLNLDQDLC SSKNFDIFDP LKNNGCLVLD
     AQSLSHLNVL SNEQGNDVGT LHKLLNRCVT PFGKRLFKIW LVAPLCERRA LEARHDAVDD
     FLSSPDFQDV FDKAAKKLPD IERIMPRIHA GKCKPMDFTR VLTALSELDG LIERLLQETQ
     HFSSTTIGSL LRGIPQVSPI AQRLQDMFAL KDDGAFIPRT GVFQDFDDAQ DAESAILDQL
     ERELARAAKT VKLERRVVKW KHVGTNEIFQ VEVPAKTAVP KEWSIVSQTK DSKRWYPPAV
     RQLVQELKES RETLLASLKL FHAQLFEAFS EDTAVFTAAV KGLAELDCLL SLSKASYALG
     SPACRPQFID CETASVDFKD LRHPCMSTNT GLDFIANDVA LGDRHEEVVI LTGGNMAGKS
     TTARTAATAV ILAQLGCRVP ASSAVISPVD RIASRMGAND QIFRNNSTFM VEMLEASRII
     RECTPRSLVI MDELGRGTST FDGHAIAFAV LHHLVGRTRC LSFFLTHYTS LAHDFDAYPG
     VANKHMQVVV DDENREVVFT YRLVPGIAES SYGTQVAALA GVPHNICDRA MQVSKEFSEA
     SKALQAQRTH SRISVALLAD FAHLVKRISS DDTEDLSRQL GIIKAQARSL SLATASSSDL
     PKASEQSREV AAKAHDQRLH AQVPSSPNTP FQAGGWSSPQ SNENRPSSPA TSISGSSEPS
     SVAKVTSSPC HRTSSKKQPL AVRPQEQMVL DLGQRIQSTC RECEMSFDRS DVNDVALHTK
     YHERMTRGVE WSTKLVDAGE ECGSVNIPPA IAKKLKAGSN EVQLLSYSLA SNTNAMLNRK
     IEEVCKCVDE ALGAARLADQ ARKEGKLLVG VSKSGRVLGA AVVGPCPPND DPAEARSPPL
     AVHRIHVLHP ARRAGLGVAL LDAALAGAVY GMSTASIERM CGGRAGTTAF SQPTQAGRKL
     AEAWIKRGGS KASHLLICAE SPA
//
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