ID M9M7A0_PSEA3 Unreviewed; 915 AA.
AC M9M7A0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 44.
DE SubName: Full=DNA mismatch repair protein-MLH2/PMS1/Pms2 family {ECO:0000313|EMBL:GAC76910.1};
GN ORFNames=PANT_22d00250 {ECO:0000313|EMBL:GAC76910.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC76910.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; DF196788; GAC76910.1; -; Genomic_DNA.
DR AlphaFoldDB; M9M7A0; -.
DR STRING; 1151754.M9M7A0; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000011976; 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 CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 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; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
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:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF118116; DNA mismatch repair protein MutL; 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:UP000011976}.
FT DOMAIN 232..383
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 696..855
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 418..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 99999 MW; 98AA4868609D6D05 CRC64;
MAEARTDPQE GGSVIRAIPT SDVHRITSGQ VVLDLQTAVK ELIENALDAS ASNIAINFRD
YGADSFEVVD NGSGIDPSNY ASVALKHYTS KLASFSDLAH VRTFGFRGEA LSSLCALASV
TIHTATSQQA PMGTVLRLDR SGRVADDSGR AARQRGTTIT IEGLFKSLPV RRKEFEKNLK
REYAKAQNLL QAYALITKGV RWTTTNQPSG GRKTPQFSVN SSSADNYLAA NVSALFGAKV
APSLMPLSLE LTFCTARKGL TAVQKRGERD DDEGDEEETA DAASTVTVVG LISKPVYGSG
RTSSDRQFFY INGRPWEAGR VSRAFNEVYK SFNSNHFPFI IADFRLPTDS YDVNVSPDKR
TIFLHEESRL IEKVKQALEE LFAPSRATFL VNGASHSLRS RGSSVAVQAK LAQYARSGAA
ASTQEMEREM SEEEQDELLP SQRSIATVQD LEYREDVAIA SESASPNEVP VAEEAEDSET
EAPLPHAPEV YASPSVGEKR KEPTTTELPT KRRRSSQSSP EPETEEASPA LDSPPRSSKG
IRRNLRDFAL PGSQVDALSP VSSAAEPHSE QGETEVMEED DLTVGALHEE ASDIPSPEPS
DAFDSPPSQP VLAEARAKTD EMEGGETVSL DLALLKNRTR QWREHKAAST LPARTTTLSG
EELLLQGAGV ENADEEQVER TLSRVIHKQD FASMDVIGQF NLGFIIARRR TEPSGSADEM
DDLFIVDQHA SDEKYNFETL QLTTQIRSQK LICPRALELS ASDELVAIEH QSTLLANGFE
IAVSESGLPG TRVKLVAQPI SKTTVFGVKD LEELLYLLRD MSAGTEATRA VRCSKARSMF
ASRACRKSVM IGTALNKARM GSILANMGTI EQPWNCPHGR PTMRHLACLQ TLADMNPRGC
TDDEPDWTEI QRCFE
//
