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
//