ID A0A8H7SBM5_9FUNG Unreviewed; 533 AA.
AC A0A8H7SBM5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 16.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=INT45_003258 {ECO:0000313|EMBL:KAG2225058.1};
OS Circinella minor.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Circinella.
OX NCBI_TaxID=1195481 {ECO:0000313|EMBL:KAG2225058.1, ECO:0000313|Proteomes:UP000646827};
RN [1] {ECO:0000313|EMBL:KAG2225058.1, ECO:0000313|Proteomes:UP000646827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 142.35 {ECO:0000313|EMBL:KAG2225058.1,
RC ECO:0000313|Proteomes:UP000646827};
RA Muszewska A., Okrasinska A., Steczkiewicz K., Drgas O., Orlowska M.,
RA Perlinska-Lenart U., Aleksandrzak-Piekarczyk T., Szatraj K.,
RA Zielenkiewicz U., Pilsyk S., Malc E., Mieczkowski P., Kruszewska J.S.,
RA Biernat P., Pawlowska J.;
RT "Metabolic potential, ecology and presence of endohyphal bacteria is
RT reflected in genomic diversity of Mucoromycotina.";
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:KAG2225058.1}.
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DR EMBL; JAEPRB010000033; KAG2225058.1; -; Genomic_DNA.
DR OrthoDB; 10264956at2759; -.
DR Proteomes; UP000646827; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000646827};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..495
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 174..223
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 93..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..161
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 62020 MW; DA1F17DC9A67C22D CRC64;
MEVQQQQQPT LQLQSIQGQQ QQQQLEEEEK TTWLNQFKKY WEKFNLANLL FCYCLPFFYM
FYPTLLMPAI FLRTLSFFIG WLYQLVLSHH KDPTTTARRR RQQRKHRSAH HTNRNNTRKR
NMITSMASSS SSSSSSRPLL TSPSTSSLMI ETSSSGTSSG SDDNDGMEYW LQKCSICLSK
RYALCLESCR DQFCKPCFQR YIEEIVHASW GLGVTRIKCP VCQEPIKQSE WSRYVPSSMV
ELYEKYNQPY RPFSRYCSSC RVNQVAPCQS PRSQGLSRQK RIEKIAHLMN ELKKSIDIIQ
LSWLDPLLKP NMNNHPHHHH NNNTLSSLST STSFTIGRIQ TLYHQMTPVL RQAAQDPRLY
SMASELSKQL VALEIVPEAW KRAQFWHIAN FPIETCNICG HDMCLQCGEN AHLSNSCLDN
LKLKLSNEEN KQEETSTIQW KLENTRACPC CSVMINRDEG CNKVDCLFCG FQFCWSCRSG
WSQQTCGFYQ CRENSEQQHE GLNNSQKDIT NKVKKKKKKI IITSLLIIIY LKF
//
