ID A0A0D0DHY0_9AGAM Unreviewed; 721 AA.
AC A0A0D0DHY0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PAXRUDRAFT_831640 {ECO:0000313|EMBL:KIK90518.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK90518.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK90518.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK90518.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN825508; KIK90518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0DHY0; -.
DR STRING; 930991.A0A0D0DHY0; -.
DR HOGENOM; CLU_014026_0_0_1; -.
DR InParanoid; A0A0D0DHY0; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000054538};
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 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 655..715
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 80822 MW; F5AAE367232C049B CRC64;
MDRDEGNAIT NADVRMQQQQ QRSSIPSTLF IIFMLFMFTN HSGDEFLARN HYQDALQSMN
YQLSNFTAWM SGEASNFTMP DRTPAITPLA QSFMHPGTRL DPLHASYYPN TTGFIRGDLD
FYNITPSSLD PTNFPWKPYA ESYMSDTNMS ELLSNLGSWN WSAVDKISWS VIDRAPRSAD
GVSERIAMIH GRIDLTDTAR TDDMRLEFEG VHFLPNGSVY GFAEPNGRPI DIRHLPVIVP
NSVQNETARA IQPELLSRIN KVKVNIDAGI IDQEIPEGSD NQTGCGFLVY AQIEPSGVSE
DVMRDLEDEL QKPTGKWTID PPPLRMTGVL ISRECGLLYR LRDAEGLRSQ SFFRKVTSYA
GVSAIFYLLL LALLCRQTDR MHSPAGLSRV SLWSFLAQAI VDAVAFAGHI TFAILANGRP
SMSLVAPAFL ACILFALEAQ HAILINQVQA PEDAVSPLAQ PPQSPPLNGT AETADAPQPQ
LPLLTIVPPR PTAPSFVRLV IRHLLTDSQA RIWLGMFIFF TFIIRVIVSP SLTLFFVASM
YSMFWLPQII RSVKRGRSSS LSAEYLIGTS ICRLYFALYF LRCPKNVLDV EPRRWAYYLC
AFVLLQVVIV LLQQRLGPAF FLPKRFATTQ TYNYHPPLPL SGSDPESPDQ SLGDCSICME
PIHADDPRHF QQVASGLLQK VGGRKNYSMA PCHHLFHTDC LEKWLAIKNI CPQCRRPLPP
L
//
