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Database: UniProt
Entry: A0A1V6XWA1_PENNA
LinkDB: A0A1V6XWA1_PENNA
Original site: A0A1V6XWA1_PENNA 
ID   A0A1V6XWA1_PENNA        Unreviewed;      1015 AA.
AC   A0A1V6XWA1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=MutL C-terminal dimerisation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENNAL_c0051G07214 {ECO:0000313|EMBL:OQE79432.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE79432.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(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:OQE79432.1}.
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DR   EMBL; MOOB01000051; OQE79432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6XWA1; -.
DR   STRING; 60175.A0A1V6XWA1; -.
DR   OMA; RMRIIGQ; -.
DR   OrthoDB; 4698638at2759; -.
DR   Proteomes; UP000191691; 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; 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.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT   DOMAIN          219..354
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          792..947
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          360..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..618
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  112366 MW;  478C94D47377E71A CRC64;
     MKMATIQAIE ARSVHQIQSG QVIVDLCSVA KELVENSLDA GATTIEVRFK NNGLDLIEVQ
     DNGSGISPEN YENVALKHYT SKLSSYDDLS SLHTFGFRGE AISSLCALAD FHIVTAQEKQ
     VPRANRLDFE QSGKLRKTQI VAGQKGTTAS AEGIFKRLPV RRRELEKNIK REYGKVLNLL
     HAYACISTGV RFSVRNTVGK TRNVVVFSTN GNKTTKENIA NVYGAKTLSA LISLDLELEF
     ETSAATKRVG DDQLSKIQVR GHISRPVFGE GRQTPDRQMF FVNSRPCGLP QIQKAFNEVY
     KSFNVSQSAF IFADFQMDTN AYDVNVSPDK RQILLHDAGA MIQSLKVSLA QLFEDADQTV
     PQSSVRSKPL PKQQPLAPLP GFVTARELSE SGEFRRPSQD RTKEGSVETP GASQQSALQR
     FTSSEAGMGS AQATPSPARS MRTPRAATNR SLMSTPAPSE LETPTAAISD DELFVQGGAQ
     EEPEPTAVSD EPSSQPPIPD ETPSRTRGDP EEIPNVVQNA FDRMRPRREP AELATITIGN
     RTITSMVGSG PPRKRVSADP PLMKEPPRRK RRIHTPSRPN IFGEHMKSFA APGSQPHEAA
     EEGEDDEDED EEASASEVGQ VEEDGSNLLS EIEDTQGAEQ EAEGEGSPPP EDVDYVPDQG
     ANQLETENTE AKDKDTAADE NLDEAQKKAQ EEATVQRLIH EAEETAMLTQ ENSAKRAKKM
     SKGAAHRDAT IQLVGTVDGS ISRLQSQFVT FQKTLQAGMK KTKEEATDLG QKTAEDKLSL
     TVSKNDFAQM RIIGQFNLGF IIAVRPGEDH DELFIIDQHA SDEKFNFERL QAETVVQNQR
     LVRPQRLDLT AVEEEVVLEN RAALEKNGFL VTVDESGDEP IGRRCQLVSL PLSKEVVFGV
     RDLEELIVLL SESISTSNEL SVPRPSKVRK MFAMRACRSS IMIGKTLTSR QMERVVQNMG
     TIDKPWNCPH GRPTMRHLMS LGQWDEWNEF EETEGLDPWK QYLEEEDEED EEDGE
//
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