ID A0A1L9PEX1_ASPVE Unreviewed; 1133 AA.
AC A0A1L9PEX1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN ORFNames=ASPVEDRAFT_26852 {ECO:0000313|EMBL:OJJ00097.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ00097.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
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; KV878127; OJJ00097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9PEX1; -.
DR STRING; 1036611.A0A1L9PEX1; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_26852; -.
DR OrthoDB; 251172at2759; -.
DR Proteomes; UP000184073; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073};
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 166..352
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 595..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..910
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 127922 MW; DBDB78344E1CDDF3 CRC64;
MLLWNMDEAS RNLILQLLTQ DALEESNRHK GKQRAGVFTD GELAMQEWSG QLNQSSTLIQ
DHQMALSIAN AVSEDGVAIT LAAQEEDRAF ADRRLAFQLA GKTPPANEQP SAHEQPLRLV
GTVFSEGVAS QIDAQDNFLR ENRPNKRRCV AESSKTAEGR QCIAGLQAEC AACNDRKPAC
DMIQAHCPHL FCKDCMIHLI KGALKDQSLF PPRCCCIPIP PSELKKHLDP GLARSFEEKE
IESNDPYRTY CSNAHCAKYI PPPQVDGYVG TCHTCHAKTC TLCKRLAHDG PCIDEDNEIM
ELAKQSGWQQ CPHCHHLIEL NTGCNHITCR CRHEFCYLCT AKWKTCGCAR WDEDRLYDRA
RVVAARNAER PPAQEDVREV VERIREGPCQ NQHARVWRRI EALENDDDED RDDEDADDYG
FDCDICGDVL PDFIMECPNC EMQWDAGRTL KTVTCEGIQA DWESLESEQS NDAIYTYDYG
FYLWMARLHL VLGPMFYTIL DLHYHPAHII AAIYLLLKCQ STTVFGFMIV ADEKRFLSWL
SQLHEAEPVI PQSDNRPSAR SIFDGVPIEK QIPDPNLNPQ RLPPQARRWQ QTHLELKDSG
KPCLSRPTTK GTESGMSRIE RNGYKRIPRA KTKEDRYEYK GKSSVKNNGN STVRTRKSSR
QKRKHTINED FQASNVPSSR LTVLTCKLHP ATNLGIFNRG KRSSPIKTHV LDQGFSETEF
LSKTPIGAQA NYVIQHEKAN LLEYDIGIEN SGQSHRETEP QPPSESIALN FDDTAIRHAP
DEQAETSDSL LFCYGKEKKG PSEEPMIYSP MKQESRSAAD IIAEPKTMGL LDFKMHSPKE
NVTENPAKVY WTLEDLKSIM QQRISSWKSE DEDSTTTSGS WLQTGSRKRK HTSSQDKKNT
HGKLSKRRRT QGYGQRSEID PSDRSTSPRT AALDPCSFTG SGIDFPFGKP LPTHAQIDYA
VEGNSFQPQR PCPYRGVGFV HDEDASFIHE ALDAAYEAIM RSEPDAPPNA LECVPTIKTI
TSSNDGNVPL HAPWEWGLKD EETLSLSHIG QETLLAGQQA SEMAIYTAAS GHYERHRSYF
GEPCASQEAL LPMEKVSSMD SGQVQEWKGL EANKLDFVTI DQMKNFWRQN KLY
//
