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Database: UniProt
Entry: A0A364L172_9EURO
LinkDB: A0A364L172_9EURO
Original site: A0A364L172_9EURO 
ID   A0A364L172_9EURO        Unreviewed;      1006 AA.
AC   A0A364L172;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BHQ10_005552 {ECO:0000313|EMBL:RAO69540.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69540.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO69540.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO69540.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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:RAO69540.1}.
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DR   EMBL; MIKG01000010; RAO69540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364L172; -.
DR   STRING; 1196081.A0A364L172; -.
DR   OrthoDB; 4698638at2759; -.
DR   Proteomes; UP000249363; 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:UP000249363}.
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          353..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          695..722
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        353..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..594
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1006 AA;  112685 MW;  67AA2D947EE2B709 CRC64;
     MATIKPIEGR SVHQIQSGQV IVDLCSVVKE LVENSLDAGA TSIEVRFKND GLDSIEVQDN
     GSGIDPQNYE SIALKHYTSK LASYDDLTSL TTFGFRGEAL SSLCAVSNFH IITAQAHQAP
     KANKLEFEHS GRLKGTQIVA GRKGTTVSIS NLFSRLPVRR KELEKNIKRE LGKVVNLLNE
     YACISTGVRF SVKNTDSKKR QLVLLTTKPN ASIRDNIANV YGAKTLSTLI PLELELEFEP
     SATGKRLNRD LNKIHVRGYV SRPVVGEGRG TRDRQMYYVN SRPCGIPQVA KAFNEVYKTY
     NISQAPFVLA DFQMDTNAYD VNVSPDKRTI LLHDSAALIE SLKEALDQMF QEAEQTVPQS
     QFTSNKQQTD IQQRLKSSPM RAPPERTRAE QATPGEESRT DISEHVQVTS QHAQEDKAAE
     GTDIESVMQG VTNSQVTIVD TAADAGESDH GEDVDEAVKR IRARAAEVSP QLDERRILTF
     QSQSPPKQSS VIQNAFDRMR PRRPPAEVAT ITIGDKVTTS IVGHGALRKR DSFTAGHTES
     KRQSKRRIHT PSKPNIFGQN LRSFIAPGAQ TQAQEEEDEE EIDEIDDSSD EEVLEDTQLS
     AGSVESPDET EPADEPVDER ADEQAKDLQP DATSTESDKD VMDEQENKAR EDTKVQDLIR
     KAEEKGATHS ENHIKRGNYI EKERQTNKHS TARLVGTLES SFAKIQAQIE TLQRQLGSYK
     RLDEAKEDEE LFVQQQKTGE ERLSLTVSKD DFAKMRIVGQ FNLGFILATR SHGADEPTAP
     AEDELFIIDQ HASDEKYNFE RLQAETVVQN QRLVHPKTLD LTAVEEEIIR ENKEALEKNG
     FVIEVDDSGN EPVGRRCKLI SLPLSKEVVF DIRDLEELIV LLSEAPTGAM RNVAASDSYV
     PRPSKVRKMF AMRACRSSIM IGKTLTVKQM VKAVRNMGTI DKPWNCPHGR PTMRHLMTLG
     SWDEYDEYSL SNERHIVMED SSSPWRRFCD LQNQEEEYEE GEAGEE
//
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