ID A0A094GPY5_9PEZI Unreviewed; 1204 AA.
AC A0A094GPY5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V498_01626 {ECO:0000313|EMBL:KFY98160.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY98160.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY98160.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:KFY98160.1}.
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; JPKA01000221; KFY98160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094GPY5; -.
DR HOGENOM; CLU_270413_0_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 863..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..100
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 983..1025
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1032..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 584..636
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1204 AA; 133149 MW; F79C1ECAB964F2C2 CRC64;
MPVTQSGNKL TEIMAHNLKG EQSAGHHPVM PSIFCCKVPP RPSNVSIMSI DTPELTRLET
LPTEILYSVI DHLPVRQIKN LSCASKRLRQ ACLSTLFRHV KFEFSPAGIE GLNDLLKSNI
CGSIASFTYE ITELLKPEIL DFDRFRSDIL TADSHVDQAK DLYDAGYEAD EFHSYMAIYK
TVHGICREQR SIVDEGADLI LSSVFCALPL LQEVRLSFSE VLEDDGWLLI PDMVINYEFY
KHHLQVVSSA IQRARSTGVA IHTISLLHFD LPFYDSGEEP NLGPLSESLR QLLKDVKVLR
VRGVSKRVLE LLSHCAFDLH QFDMCGVAAP EKVIKDFFET NKKSIRSIGF HDVGILGISG
LNCLYSKTPL SASMLCRVEM LTFRNEKQRL RYLRCTSSGP IILQDPRNGN ISGTSTSDLE
SLEKEMERLR LQAQVTPKAT ATTMAHRRML LSHRECTYSM YYNGEKLASH IHSQLGLTIL
LTNVKLITKP GDLYQWSIST ARKAALFNKQ LTKHSTGSYI DLCNGVGVHF KAVLGKGAAD
YEPETRLVTK ITAFDAPEKS REHPSSNTIA KEWREKFNAE VAIREALEIK MMEIKGENAE
LLTEMEALRE EEAMRIQELE KAREVLLITS RILQERALKA SEDSQKITHA ATSDLKGTAG
EAKTVRLSRL GRLKVLLVWI IQSPEHLEWM RPWMTSTKEI QSPSATVQMF PGRPNMDTLI
DMEIESQIGA MGVSVCGSGS LSDDVRNVCA GGRLEMHLIL RYSYRAIVLR TRETEMGRDR
RAGIGWKDPK PGPGRSWMVL GSTPPDPKAR RSLFVAYSIA CVVAQLGNMS NVLGVSAVGT
IGGLNSNNQT SAGASAPSAS TGAVIAIVAG GIGALFFSIV MVGVIIAVQR HGHPVRRNPQ
QVRPGRPKGP KRLALAMLES IPIVKFGHSN EDIELADTDR ANRNQWTTTD AIDTSTIHPA
RTVNPVPALM CGSLQARSSG HECSICLNVF IEDEDIRILL CNHKFHAVCI DPWLLNISGT
CPLCRVDLRH TTDNSDTGTN AASDSLLPPL PNEVGDAAPH RSHRPSFDEL RSAARSGPEE
CIAALRRLYH ENHHASHASI HTEATAPRES RLRLGTDGFT RQVYLINGQQ PAPLIDISEG
DDLEVFVQND LPVASTIHWH GLLQRGTPYM DGVLGVSQYP IPPVATLPTS SALTTTMQSA
CLKH
//
