ID A0A1V6QI41_9EURO Unreviewed; 891 AA.
AC A0A1V6QI41;
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=DNA mismatch repair protein S5 domain-containing protein {ECO:0000259|SMART:SM01340};
GN ORFNames=PENANT_c003G06244 {ECO:0000313|EMBL:OQD88891.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88891.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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:OQD88891.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYN01000003; OQD88891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QI41; -.
DR STRING; 416450.A0A1V6QI41; -.
DR OrthoDB; 1369806at2759; -.
DR Proteomes; UP000191672; 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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR002099; MutL/Mlh/PMS.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
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:SF41; MISMATCH REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G05820)-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 229..362
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT REGION 367..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 98134 MW; F9A0B153872638BE CRC64;
MPIEALPQNT IQAIGSTSVI SDPCSVVKEL IDNALDASAT SLQIDISQNT IDVIQLKDNG
HGIPPEDQQY VCKRSFTSKI QTLDDLKNVG GSCLGFRGEA LASVAEMSGV IAVSTRVQSE
AVGSCHKYGR NGELIITQRT SHPRGTTVRI ENFLKHIPVR KQTALKAATR NLTRIKKLLQ
AYAIAQPSKK FSLKVLKAKN ENSNWTYAPG TSASLQDAAL KVAGTEVSSC CVLKLLSSQA
LAQIEGSPDQ ADYKVTAFLP KTPIDTSKIN NVGQYISVDG RPLSSSRGIG QDIVKLFKPY
IRLATSQAES FKTATDPFLC LQILCPRGSY DVNIEPAKDD LLFENRGLVL SLAESLFRDH
YGDIAETEKK PSTKGNTTSS DATASNGGFN LLMARKPPAE PSTQSHQAED PFGDAIIRPP
LLQRPSRPEN IISPHDNKAS SNGSPGQPNA NRPKRSSFVN PWSISRINTS FQTSQRDQNQ
LSQRSSVDLI VRSPEGSRRR SPELSSPQDS PESQDLPSPP ISRIASGSPV RRRHRNPQEP
IDSSPERPRV SSARRADRER DRERYGNGAL DTWFQRTTQV SLQRSAAEDE SIRETELPLS
SLAQERFGLH AGSSPNNLPI EGQNDGTLDE LSENGQTQQS FRRASSLPHD LNGINESLDS
GRGFPVLDRW AARLHDGVTV EETSDLEKAL DFERRKKRAI QDSRIRFREN ESLSSSQPRR
PISHSPHHSR YLAAKAALTS SQTSNTDPFF TTTLSPHDPR AYFMRNQTSN QSDEASTTGT
EPRKLPSSRL PLERIPDGYD LHDLGTTCLI DLSLISHING QHTQNEPYIE KDNEATAFSS
ANVEACTPLW DERLSLLMQQ KFKNDDQTSL PTGKIDLSEI ISKHLMEIDA S
//
