ID A0A2T3AW94_AMORE Unreviewed; 859 AA.
AC A0A2T3AW94;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=M430DRAFT_36156 {ECO:0000313|EMBL:PSS12945.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS12945.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS12945.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS12945.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KZ679014; PSS12945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AW94; -.
DR STRING; 857342.A0A2T3AW94; -.
DR InParanoid; A0A2T3AW94; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000241818; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
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 InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF12678; zf-rbx1; 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:UP000241818};
KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..859
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015612939"
FT TRANSMEM 407..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 792..853
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 514..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94880 MW; 4DE3B77F89877472 CRC64;
MPPQAPAAQE YARFVLVVIL LFFLSSSSDN GPPPGFAGSP RDYAAAKVAR QRRNLDVLNT
TQWEDFAPRA ADEPRFLNLT GFRAEDDLLW DRLGAFRERA ALFTDEAGGK WRLDRETQLR
AGVLGEVYEN VTGIVVGRWV RYTGDLEGGE ERHRRYNLSQ VTPEVEWSGN EELWDRNITG
TEGKLMLRVD ERDVEAVDVE GLSLGSGWVR EVAATMTIQD ESSSGDGWDM RIHGVHWPRQ
GVMLMTTTSD KFAGLFGLPH LTMDMNHFTS SKMLLNKTLE KTVEKMEKAY WTEVNNPWSS
SSDGQGDSAL STPHCEYVVY VQVYPLDLGL ALNDDYMDTA SIVQQIEQEL RFPNGAPTPP
APKMRMSTVI FSPDCGFMLE SKGPPAFPSE DGDHLVGRKQ EVFLHQVQSW LLVYAAVIFG
QVLLLKMQSK EASTPSTVGR ISIYTIAMML MADALLFSSL SLLSATAPNI FPSALLASFA
ALMSVALGVR FITAVYNVQE PERRERLRVQ LAAQAANTPQ PSPAPTPSSA PIITAAGADT
APPPGTASAP TAQATANNTP IIIPSDQDID AEIAEVANAA SAVPRPTLPT TNQGATTPTQ
QVPRASNFGA VYVQFVLALT FILFVSLSAL SWPVTFRTFY IHFLSVAYLS FWVPQIRRNI
IRNCRKALLW KFIIGQSILR LLPFAYFYLR EENVLFSEPD WKAFTALAGW VWIQIWVLAA
QEILGPRWGI PKGWTEEGWD YHPILREDNV EAGGLPIGLV RAPGSPTLER VRTGDEGKKS
DGPARNIRTV DCAICMQVLE VPVVAAGTDA SAAGGVVGML GRRLYMVTPC RHVFHSACLE
GWMRFRLQCP ICRENLPPL
//
