ID A0A0B2V9B5_TOXCA Unreviewed; 1175 AA.
AC A0A0B2V9B5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=brat {ECO:0000313|EMBL:KHN80016.1};
GN ORFNames=Tcan_16190 {ECO:0000313|EMBL:KHN80016.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN80016.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN80016.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN80016.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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};
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}.
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:KHN80016.1}.
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DR EMBL; JPKZ01001799; KHN80016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V9B5; -.
DR STRING; 6265.A0A0B2V9B5; -.
DR OMA; CDVNYQL; -.
DR Proteomes; UP000031036; 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; 4.10.830.40; -; 2.
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; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 3.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 1.
DR PROSITE; PS50119; ZF_BBOX; 3.
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:UP000031036};
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 169..216
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 243..290
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 302..345
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 900..940
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..441
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 469..511
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 127468 MW; 39B8FECDF1C01DFC CRC64;
MDEGGGGEHS PNLERPRVLF TTHEDKTGSP SSMKEEKGDA GSASHSCTSS PLLDTAPLPN
DDDAVCPYCG QQFRKPRVLD CLHSMCEDCI IAQLDGRRDG EPTRPHANPV ATDFELEQNS
MQMRPTPPGV IRCPICHQES HVGNDVRFVN HLVLDFVRIH EAENASAGGG VRACRACKSE
QPAMAVCKQC ASDLCKNCVQ AHRDMKLFDG HTESHVGNDV RFVNHLVLDF VRIHEAENAS
AGGGVRACRA CKSEQPAMAV CKQCASDLCK NCVQAHRDMK LFDGHTVLTY SEVAESDLEL
PHEPVMCITH PTVPYTTLCT SCEALVCAQC QPEHSDSRHH NIVQVDDRVA QLINTELREI
AAHADAKARF GILAKATENA CGCIPERQRL LADQYEAAHS QIEEAFADYQ HTLEEAKRRL
LTELERVRDE QDSQLNNLSH RISAKATENA CGCIPERQRL LADQYEAAHS QIEEAFADYQ
HTLEEAKRRL LTELERVRDE QDSQLNNLSH RISVTVVKIA DALAFTERLL AKGSPFELLA
SRKKVRQQLT SLAHSIPDMS STVELSFSRS PHAQFAKQLN AIVGTVSCRL IAEAVKNEAL
LPNVRSSDMS SLKQLTRAFP SDPSLAPVTS SGAPTATSTP SIGNTQTSAF STYSSGPGTI
GMERRQKSTS ISAHNSMADF NDGWPPSSVP PEPPSPSPPS DFTPMRGVAT SESSFYNWPP
SSNPPPVNES RSGGGHAVPQ PAPNSTLPSS IHAVNAQQMS AAMNSLLGMQ KPNNLWMAQQ
AAVAVAAAGQ LPNAFAMPAV RHRTAPSIFD PPLVDPSTLR LALNSLGAGV VDATSLAALQ
SALPQIPPPL GRQSQCGTPS EQIAASAASL LSDRQFLGLT RGVAPKNIVG ASDLILRWHI
GGIGVGPGQF NSPHGFCLGC DDEILIADTN NHRVQILSKQ GKVIMQFGVA GTDDGHLFYP
KKVIAVKPRP SLPDGGYIVV DKGDNKARLQ LYSKIGEFIH KIVATYIEYV SALTVNDAGH
LVVFNSTSAM FVLDIEQGPT AKILKWADCG KVLCEASDVS VFEGLYYVTD YKQHCVVVLT
IDGDLVRRFG AFEHTPYPIG VDVSKAGDVL VADSHGNHFH ILVCSKTGQR LQDFECTQLK
VSRCVGLRIT SEGNIVSISK HNHNVLMFNT LYVNH
//
