ID E2C866_HARSA Unreviewed; 211 AA.
AC E2C866;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
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_02790 {ECO:0000313|EMBL:EFN75869.1};
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:EFN75869.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN75869.1,
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; GL453568; EFN75869.1; -; Genomic_DNA.
DR RefSeq; XP_011152390.1; XM_011154088.2.
DR AlphaFoldDB; E2C866; -.
DR STRING; 610380.E2C866; -.
DR EnsemblMetazoa; XM_011154088.3; XP_011152390.1; LOC105191011.
DR GeneID; 105191011; -.
DR KEGG; hst:105191011; -.
DR InParanoid; E2C866; -.
DR OMA; VGMLQHQ; -.
DR OrthoDB; 5474929at2759; -.
DR PhylomeDB; E2C866; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46661; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1-LIKE PROTEIN; 1.
DR PANTHER; PTHR46661:SF4; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 168..208
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22484 MW; D1AAEEF540BD76A6 CRC64;
MGAKASTVAQ SAGGNGQSST GANETMQGFS MLRSLPGGVG MLQHQHQQAN QSQSSRVSGD
SRQRARSLSS VPDLSSAEQA ALATSVGVGV GQALGLPQLD SDDADEDSGR VYAAHSLPSH
IWSLNGLKCP VCSKFILPDD IECHLVMCLT KPRLSYNEDV LADEKGECVI CLEELQSGDV
IARLPCLCIY HKNCIDKWFQ VNRSCPEHPG D
//
