ID B6Q769_TALMQ Unreviewed; 1011 AA.
AC B6Q769;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 08-NOV-2023, entry version 73.
DE SubName: Full=DNA mismatch repair protein (Pms1), putative {ECO:0000313|EMBL:EEA28734.1};
GN ORFNames=PMAA_035290 {ECO:0000313|EMBL:EEA28734.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28734.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; DS995899; EEA28734.1; -; Genomic_DNA.
DR RefSeq; XP_002145249.1; XM_002145213.1.
DR AlphaFoldDB; B6Q769; -.
DR STRING; 441960.B6Q769; -.
DR VEuPathDB; FungiDB:PMAA_035290; -.
DR HOGENOM; CLU_004131_0_0_1; -.
DR OrthoDB; 4698638at2759; -.
DR PhylomeDB; B6Q769; -.
DR Proteomes; UP000001294; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 217..351
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 757..925
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 367..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 695..722
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1011
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113336 MW; 1A13FC0000648785 CRC64;
MATIKPIEGR SVHQIQSGQV IVDLCSVVKE LVENSLDAGA TSIEVRFKND GLDSIEVQDN
GSGIDPQNYE SIALKHYTSK LASYDDLTSL TTFGFRGEAL SSLCAVSNFH IITAQAHQAP
KANKLEFEHS GKLKGSQIVA GQKGTTVSIS NLFSRLPVRR KELEKNIKRE LGKVINLLNE
YACISTGVRF SVKNTDSKKR QLVLLTTKAN ASIRDNIANV YGAKTLLTLI PLELELEFEP
SATGKRLNRD LNKIHVRGYV SRPVVGEGRG TRDRQMYYVN SRPCGIPQIA KAFNEVYKTY
NISQAPFVLA DFQMDTNAYD VNVSPDKRTI LLHDSAALIE SLKEALDQMF QDAEQTVPQS
QFTINKQQTD IQQRLKPSPM RAPLDRSRTE QATPTEESQT DRSEPVQVTH QHAQEDKTAE
VADNENITQE TTDSQVTAIS EDAAADESDH AEDADEAVKR IRARAAELSP QPGERRILTL
QSQSPPKQNN VIQNAFDRMR PRRPPAEIAT ITIGDKVTTS IVGHGTLRKR DSFTAGNTEG
KRQSKRRIYT PSKPNIFGQN LRSFIAPGIQ TQAQEDEVEE DMDEDDGSND EEMLEDTHSS
VHSEESPDET EPVDEPVGET FNERAESLPL DDASTEPAKG VIDEQEKKAR EDAKVQDLIR
KAEEKGATHG ENHIKRGKYI EKEQQTNKHS TAQIVGTLES SFAKIQAQME TLQRQLGSYK
ALDESKDDDE LFVNQQKTGE ERLSLTVSKD DFAKMRIVGQ FNLGFILAIR SHGADEPTAS
AEDELFIIDQ HASDEKYNFE RLQAETVVQN QRLVHPKTLD LTAVEEEIIR ENKLALEKNG
FVIEVDDSGN EPIGRRCKLV SLPLSKEVVF DIRDLEELIV LLSEAPTSAT RNATTSDTYI
PRPSKVRKMF AMRACRSSIM IGKTLTVKQM EKAVRNMGTI DKPWNCPHGR PTMRHLMSLG
SWDEYDEYNL SNERYIGEGD SRGPWQRYSD LQNQEEEEEE EESDEGEEGE E
//
