ID E2BIS0_HARSA Unreviewed; 837 AA.
AC E2BIS0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EAI_04176 {ECO:0000313|EMBL:EFN84410.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN84410.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN84410.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL448530; EFN84410.1; -; Genomic_DNA.
DR AlphaFoldDB; E2BIS0; -.
DR STRING; 610380.E2BIS0; -.
DR InParanoid; E2BIS0; -.
DR OMA; AYDQHAN; -.
DR Proteomes; UP000008237; 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:UP000008237};
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 43..82
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 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..829
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 95896 MW; C4022C8DB273D1B0 CRC64;
MEGSLEVKHS LAGVEEPIKS EAPVQNSDSN ERSDDIASPP PNCSICLGKL INTSFTDSCL
HQFCFDCLVK WSKIKTECPL CKQTFKSIIH SVRSEEDYDQ YHVPRELAQS QIPQPHVVST
LDLNLDVGVG RWEDVPRFVY RTTMTGNRRH GLLNPEQVAR REQLPSVAPQ VPREERRRRR
DNPTDYRRTV YRHGIWATLL PDIFGRFREC SAEYYRQVSL VTTVMRYPQE LDRLIPWLNR
ELQVLLANST HITYVMNIIL DALRQFDIRS TEFRNLVRPY FDVHTDHFAH ELLNFARTNF
DMVGYDQAVT YLPRGLSNEY APRIVSPTSS TSSSSSSSSS HISFLSDNSD VRILEDEAID
LRVNTVMPTV LPMSQPGPSA VGQLLRSLES SYDIPELLVL SSTSSESEGE CEIIGYVKPR
HERTPEIIEL VSSDNEMSPV RSNENIPSTT EETVPANLSL PSTSYATKEI SSDLSSSSTS
ADDNSDSDYN PGTSRRFRNH SKKLSSRKFV EKEHKKMNKT RSHNKRSRNS YSSEESDFKK
RSSRKIVKKR IYSSSDSSSS EGSSTKYDEK RSKKERCSVK EQMKLKKEET YPNADGDSDS
STETDSKTKT KKCDRQYVSK RKRSLSSSDY TAKSERTTRS KDRICTQEKS KSNNKDNKCR
QSRSRSTSLS SNVSEQDKVS GYRHHESRGR RPDDSASTNK VTKRQSESKS KSKTCYFSDS
DDDHLRSSSQ CSNRSNKSYL RWRRSKYKDR HKDKDRTNRS SSRTFNSSQE AASPIVTSST
SAKNDAHPTK HSDCVESHKS TRSEYKKSKH RKFHDEKKSR SRKRRRRLRS LSTSQSE
//
