ID A0A0L7RC51_9HYME Unreviewed; 710 AA.
AC A0A0L7RC51;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=WH47_06358 {ECO:0000313|EMBL:KOC68567.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC68567.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC68567.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC68567.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; KQ414615; KOC68567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7RC51; -.
DR STRING; 597456.A0A0L7RC51; -.
DR Proteomes; UP000053825; 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 GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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 DOMAIN 41..80
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 81755 MW; 8818892B7262CEF4 CRC64;
MEGPLEVKTS TAGAEEPIKS EPIKSEAPDR SEGAVSPPPN CSICLGKLVN TSFTDSCLHQ
FCFTCLLQWS KIKTECPLCK QTFKSIIHNV RSEEDYDQYH VSRELATLDP SFELLSHYRT
TMTGHHIRPH EVMFNPEQVA RRDQSPSLIP QVPMGERLRR RAKPAYDRRT IYRLGLWALP
QNVLRRFRVT SADFYRREPR ELSRLIPWLN RELLVLLNNN TTYVEYVLRV ILTALNNYDI
RSTSFRELLR PHFGTFTDHF VHELFNYARS NYDLLGYDQS VISVPREILN EYISDMNISP
ANTSTSSDDS DVRVLDEAIL DLRMNTEMPG VGPHTINMPG PSTVGQAFQS EEIDEPFNAP
DVYTISSDSL ASDNDCEVIA YVKPRHERTP EIIELVSSDP EEIDISHVSN DNAQSSSTVA
SYEDNAQPST SHSIKKNVNR SSSTSHSIKK RVLTSSSSES DSDSDSDYTS VRSKKYHSRS
RKRSKRSTTK RRNRSRETRV RNRSSRHLSS SGESDSRKKR KKRNTQRRVK KRLSNSNDSS
SHEIVEKKSR TSQYSTKGTV RVRKDLIKKE TRYSDEESFS SDSSTECDET AKNVKCRTVR
RSKRIYTTSS SDFDMGSRNE RVVRKRGKTK QALDVRESHR KESRYKDDRQ STSRSSSASS
YASQKEKRVS SKRRESQRPM SDEDSNWINR IVSRKREFKS KMRKTIRSSF
//
