ID A0A1L9U008_9EURO Unreviewed; 732 AA.
AC A0A1L9U008;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN ORFNames=ASPSYDRAFT_139568 {ECO:0000313|EMBL:OJJ65011.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ65011.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KV878582; OJJ65011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9U008; -.
DR STRING; 1036612.A0A1L9U008; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_139568; -.
DR OrthoDB; 3354811at2759; -.
DR Proteomes; UP000184356; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd20339; BRcat_RBR_RNF216; 1.
DR CDD; cd20353; Rcat_RBR_RNF216; 1.
DR CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR047545; BRcat_RBR_RNF216.
DR InterPro; IPR047546; Rcat_RBR_RNF216.
DR InterPro; IPR047544; RING-HC_RBR_RNF216.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 319..535
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..314
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 82792 MW; 4692AA476B371BE8 CRC64;
MNNWGLQREP PFEADDTTYI SLSSADESDG GISLPSDNNF PEQDDTWVPD FDGEIPKEGV
IGRLQKKQRV GGSSDTSLSQ DSFSLGHVAS QIPPMSKTDL IPSVEPADDE TDPLLLQVLD
TFPGISHKYV TDLITRHRDF LALDSGVSAN GIDLAFYRDA VYEEILAQES YPKQDSENGK
RKREESHSSE NDWESDETHQ TNARTYSEAA AAVLANEFPY IPIHYVKKIL RQKKRLYHAY
LTLQLDETLV EKQTNPYVKL KNRRNAGSSK RLESLPGIIT REFNAAKEEA QKQLGDIQKK
KEKEEAEKAN EEEHTRIGNL IECQCCYSDV PANRCLPCDG IEIHFFCFTC IRRSADTQIG
LMRYTLQCFD VSGCQAPFAR SELREVLGSL IMDKLDSLEQ EDEIQKAGLE GLEDCPFCSF
KAVLPPVEED REFRCENSSC KVTSCRLCKE KSHIPRTCEE FRKDKGLSKR HQVEEAMSKA
LIRNCPKCQV QIVKDFGCNK MTCTKCHTFM CYICQKDITQ DSYRHFKPGG CPQDDMRTQD
SDIQKAERTA IDKILAENPE ITEEQLRVGH VKPKRSQRRY TARAPMYPAD YFLHPPGLPD
IFGLYHGQIA QNVAQNAAQL GQYGQPGQEG MVGRRAAPAF AINQEGGQVG NPSPQHTRGT
QYEPFQDLYQ GLYLQPNAAV HAPVPVHGRE NPPLARFDGR NPQNAGLFQL EPLQRQLEDH
GPLAPRYMYD FF
//
