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Database: UniProt
Entry: A0A0A2JEM3_PENEN
LinkDB: A0A0A2JEM3_PENEN
Original site: A0A0A2JEM3_PENEN 
ID   A0A0A2JEM3_PENEN        Unreviewed;       898 AA.
AC   A0A0A2JEM3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   SubName: Full=DNA mismatch repair protein {ECO:0000313|EMBL:KGO53201.1};
GN   ORFNames=PEX2_058440 {ECO:0000313|EMBL:KGO53201.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO53201.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO53201.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO53201.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO53201.1}.
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DR   EMBL; JQFZ01000252; KGO53201.1; -; Genomic_DNA.
DR   RefSeq; XP_016595840.1; XM_016743118.1.
DR   AlphaFoldDB; A0A0A2JEM3; -.
DR   STRING; 27334.A0A0A2JEM3; -.
DR   GeneID; 27678537; -.
DR   HOGENOM; CLU_005415_0_0_1; -.
DR   OrthoDB; 9570at2759; -.
DR   Proteomes; UP000030143; 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:0006298; P:mismatch repair; IEA:InterPro.
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   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF47; DNA MISMATCH REPAIR PROTEIN MLH3; 1.
DR   Pfam; PF13589; HATPase_c_3; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          604..823
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          333..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  99736 MW;  2994C62FAC5A2E62 CRC64;
     MPPPQSRIRA LPSDVIAKIK SSTSIVHLTG VILELVKNSL DANAHTVFVT VDFKRGGCIV
     EDDGDGIPPV EFEAAGGLGK PHRMSPNLLI GMFRVKSRAL TLQRPDELER EWDYLRNSLV
     SLLLANPQFS KLVFLDVERN KRMSIRLGTA SIPESCIAHV QREFDLKRIG SILTQSGLIT
     PQDLDNWHEI SASVSGLIIQ GAISLQPSPT RKIQFISLGK VPVLSHNSSN VLYNEVNRLF
     ASSDFSNAGA MSGRSSVTHP ASLVNQIDAP SNASTRSWAK PVNKWPMFYI RIDTNAIIQL
     DDDGSEHLPE SAKSVQRIVD VLGAMVYEFL RQHNLRPRNG KQQTSSSDQT QIIRSKVSKA
     AGSSRGPLKQ GRPVSSTEEA FSGHLKIPSF PRTQSVNSSQ SFANWSRVKT AKDIKGHSPT
     HRPPRRSHAA PDIMQGESSL PILPKNRPTR RDDGTTLPNS PNQSVSDGDR NRTEDLPGDS
     PSDKMINWID PHTKLAYMIN PRTGQTMNSR KSLATQRSPT ECVDTSSKHP TQTFWMENLL
     GAWDNPSFSR TETPIPNLGA ESAGQQNTTT SSHDCFKGIG SLDTAQVAKY RGKLRRRVLE
     TAEVIAQVDK KFILAKVHTA PVILNCVGPS NDVLLLIDQH AADERCRIEL LFREMFLSAG
     QGENLESGHR VRTVQVGSLA FEVSSTEGDL FQKYTGLFSD WGIEYVTQGQ TKSTVLITVH
     TLPILIAERC RLEPHVLTDL MRREIWSSEE DGRKPFQLKK TFETQDADQD LDLSDNDNVA
     HKETSTSYAS RSWVQKMNGC PQGIVDLLNS RACRTSIMFN DPLNIEECQA LVSRLARCAF
     PFQCAHGRPS MIPILDLRYL SETAVSLPLD LDTRASTYDY YDGMSLDFVE AFKTRYVT
//
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