ID A0A158P6T4_ANGCA Unreviewed; 783 AA.
AC A0A158P6T4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000149501-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000149501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR AlphaFoldDB; A0A158P6T4; -.
DR STRING; 6313.A0A158P6T4; -.
DR WBParaSite; ACAC_0000149501-mRNA-1; ACAC_0000149501-mRNA-1; ACAC_0000149501.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14959; NHL_brat_like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF229; NHL (RING FINGER B-BOX COILED COIL) DOMAIN CONTAINING; 1.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 147..194
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 206..242
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 419..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..320
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 783 AA; 87228 MW; BC1A3BD2A1CC5333 CRC64;
MGDQNGRLES PLSCQELEKS TPYIFRSSTS SPLLNTEPLP LDDQSHCPYC HKNFRKPRVL
DCLHSMCEDC IIAQLDGRRD AQITTDLVSR NPTDCELELP KLKERPTPPG VIRCPICAQE
SHVGNDVRYV HTMLLDYVRL AENEEAVGER RCRACKSEQP AIAVCKQCQS DLCSNCLSAH
GVMRMFEGHE VMTYLEMEQL GQRGEVRPVQ CPTHSLPYKM LCATCETLCC KVCLEMEHLN
HKSEIEKLAD KVERKWRDSM AEWSAIPDRS ASLHEQYESA KIHIEMAFDD LLKALDEAKA
NKLEETRQKQ EVAIEDLYRK MNLNEARVSD ALRFSRNLLS KSNGMELLAS RRKVVQQLNN
LAHTMPALGI QVELEYQPLS KKQLDTHMNV CTSNVIFYFS LRHRSEHFCS TSSTWGSGIA
PSRLSGPGGD TFGWPPSSHP PDLPSPSPPI PLKDIVPPTF PSNATGLIGQ PSNTNSAVTT
SGGNVCNSFV FGTSQQGSSM RELHCPSGFC LSASDDILIA DTNNHRIVVC GPPHPWKIGR
PGTDDGQLCF PRKVIALKAD VTRYAVLDKG VDGKTRAQLF DQRGEFIKRI NMMPLVPRGG
IEVSAASCTS TGYLLLVDTS GVVYCIDVDV PRVVFWFDAS SHLGEASDVA IYEKNVYITD
FKHHCVQVFN TDGQFIRKLG EPSQTPYPIG IDVSKNGDIL VADTHGNHLH VVVFTADGTL
QQSFTHNEFR LSRCVGLRVA GSGHVVTLCK HNHTLFVFKP LYIRELVSAP SMHKISVFHL
SRL
//
