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Database: UniProt
Entry: A0A1Y2F1M9_PROLT
LinkDB: A0A1Y2F1M9_PROLT
Original site: A0A1Y2F1M9_PROLT 
ID   A0A1Y2F1M9_PROLT        Unreviewed;       689 AA.
AC   A0A1Y2F1M9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0000259|SMART:SM01340};
GN   ORFNames=BCR37DRAFT_382691 {ECO:0000313|EMBL:ORY77791.1};
OS   Protomyces lactucae-debilis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Protomycetaceae; Protomyces.
OX   NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY77791.1, ECO:0000313|Proteomes:UP000193685};
RN   [1] {ECO:0000313|EMBL:ORY77791.1, ECO:0000313|Proteomes:UP000193685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-1054 {ECO:0000313|EMBL:ORY77791.1,
RC   ECO:0000313|Proteomes:UP000193685};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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:ORY77791.1}.
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DR   EMBL; MCFI01000019; ORY77791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2F1M9; -.
DR   STRING; 56484.A0A1Y2F1M9; -.
DR   OMA; KDDVMFE; -.
DR   OrthoDB; 1369806at2759; -.
DR   Proteomes; UP000193685; Unassembled WGS sequence.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF41; MISMATCH REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G05820)-RELATED; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193685}.
FT   DOMAIN          217..341
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   REGION          344..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..397
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  74556 MW;  06E3366DA4C253A7 CRC64;
     MPITKLPDTD IKLLSAAQVC TDPAAALKEL LENSLDAHAT SISILIDGHG LDLLTVRDNG
     HGIPSADRNK LACRHYTSKL TSLEDLSHVA TYGFRGEALA SLADIAATFV VTTRTAQDAV
     ATSYERNSRG TCKPTKTSGE PVGTTVTATK LFKNVPVRRE KLKRDGNKSV AAIKELVLSY
     ALVHPNVRFH VSIKSGKRGE TPIVVVHAPA TSLEAALSRS FGATTMSACL IKHARLPLMD
     VTLVMPRRDA PAAAVANKGH FIYIDHRPLT TIRGLPKQLL SLLNTYATKA TSASKPLILL
     SLTNLTGEYD VNVEPSKNMV YAANADAILT ALTELLDSVY ADTNDDQAST CQPSSTDLQP
     SSSMPPPRSQ RRSSWLTSMD DVPSDSDDQE ELQTQEADGE EQGANQQEDY VPDRPALTSP
     WTIAALSAKS TSSNPQAQRT QSSQTPATRS ISPTAPHLQP PAKRQRTTEP RTTIERPTNT
     KQKKQTNDLY TYWRPQPTQS LIHDDADLAD RRGQVSASSP VRASRTVYPP ASPIISPAAE
     ANSKSNPFSG ASPTRASLVR ASRGSEDRMR KRVMLERSEP EDQCHDRELV LSTTGMLVTR
     TTVKDNGLND GLFLGIAAMG DAVDNMTDLS PLAKLDGGLC LLVASSHVST LGLFVTPLSE
     VSSTIPKLQE TRFTELKRMG DADRVVRVW
//
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