GenomeNet

Database: UniProt
Entry: A0A1V6PMD7_PENDC
LinkDB: A0A1V6PMD7_PENDC
Original site: A0A1V6PMD7_PENDC 
ID   A0A1V6PMD7_PENDC        Unreviewed;       564 AA.
AC   A0A1V6PMD7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENDEC_c002G05582 {ECO:0000313|EMBL:OQD77696.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD77696.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
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   -!- 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:OQD77696.1}.
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; MDYL01000002; OQD77696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PMD7; -.
DR   STRING; 69771.A0A1V6PMD7; -.
DR   OMA; DQVLMDH; -.
DR   OrthoDB; 23943at2759; -.
DR   Proteomes; UP000191522; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10232; ScSsz1p_like_NBD; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639:SF32; HEAT SHOCK PROTEIN PDR13; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191522}.
FT   REGION          479..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..507
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  60310 MW;  F522820B99029B99 CRC64;
     MGDSNGVSAE AERFAIGISF GNSSSSIARI SPEGKAEVIA NEEGDRQIPT VLSYIDGEEY
     HGTQAKAQLV RNSANTVAYF RDYLGKLFKD IDPTPCHQSA HPQQSDSTIA FSIRDTASET
     PNSVTVSEIA TRHLRRLKQS ASDFLGKDVN SAVITVPTDF TDAQREALVA AAKDAGIEVL
     QLIAEPVAAV LAYDGRPEAT VTDKLVVVAD LGGTRSDVAV VASRGGMYTI LATAHDYELG
     GASLDQIIID HFAKEFMKKH KTDPRENARG LAKLKLEGEG TRKALSLSPN AQLSIESLAD
     GIDYGSTINR TRFEMLSGKV FAQFTGLIEQ VVKKAGLDVL DIDEVIFSGG ASHTPKIAQL
     ARNIFSEKTT ILAPSTSTSA INPSELSARG AAFQASLVQE FDREDIEQSI HPMVTATPHL
     SKAIGVEFQS TTDTTFQALL GAETALPARR IAQYAAPKEG GDVLVRVCEG AREIKVTKPE
     AKAKEEKPAD DEDSDFDSDE EEEEDLREVV WKTEKPIAEL AVKGVKAGGK VEVMIHVNAD
     LGLQISVREV GGSTAVRGAI NGSA
//
DBGET integrated database retrieval system