ID A0A1V6R320_9EURO Unreviewed; 702 AA.
AC A0A1V6R320;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PENVUL_c102G05190 {ECO:0000313|EMBL:OQD95781.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQD95781.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
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:OQD95781.1}.
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; MDYP01000102; OQD95781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R320; -.
DR STRING; 29845.A0A1V6R320; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd16536; RING-HC_RNF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 182..232
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77811 MW; 35E9D1EE1C3224D8 CRC64;
MSSNAGQNPP PSKAVNIPNT ASSAPFHSAV PAENGSQRRL GGAGSSRPGV SSKTSATPRN
NQARKSQHNR QRKPRLLDDD EYNESAAMKS TTSRKGQTSI THLMNFSLPP RPQYQAPPRN
IRRYTSWGAS AVDKSRYVHA NYRFIVMPNQ NFHAQAANAD VHIDWASVLQ VLVSAQTQAA
SCPICLSTPV APRMARCGHI FCLPCLIRYM HSSDDDNMVP EKRHRWKKCP ICWDSVYISE
TRPVRWFRGQ EGDLPVEGGD VVLRLVKRES GSTLALPRDG SEALGPGEDV PWYHVAEVAD
YARIMKGGEE YMTAQYDAEI EDLRKQEVED ELLFGDENTW TRKAIGSIMD AKEKLKGIGN
PPEVRPVKER NIVPTLTKSS SEPCTVMPST LDEANHLSKT LDGVDLDPEF STKAKEKGRS
KQTPASSGPD QPYHFYQALP HFYLSSLDIR ILKAAFGEYS LFPATILPRV EHISTGHIVD
DELRKRVKYL GHLPQGCEVS FLECDWRDVV VPEVLGRFRA ETDRRRKRNR EKEAREEKDR
VRAEREEDDK RWAAARRKRP SIGSASVSEA PFSAHDFQPL PHNADSTLFD TTASSASPPR
PSSGFGALAT PSTSPPGIRT VWGTTAVGSL SPSLEAQRAI HSDGWRQGWE DELFAHQESD
LLAQTASGDQ NLNTGPSSSG GKKKKKNKTK ITLMATSSQR GA
//
