ID A0A0V0S7T4_9BILA Unreviewed; 887 AA.
AC A0A0V0S7T4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=brat {ECO:0000313|EMBL:KRX22816.1};
GN ORFNames=T07_12613 {ECO:0000313|EMBL:KRX22816.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22816.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22816.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22816.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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};
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:KRX22816.1}.
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DR EMBL; JYDL01000029; KRX22816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S7T4; -.
DR Proteomes; UP000054630; 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; cd19813; Bbox1_BRAT-like; 1.
DR CDD; cd19798; Bbox2_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; 1.
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; 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; 4.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000054630};
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 226..266
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 333..376
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 385..424
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 683..709
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 710..751
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 752..794
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 795..838
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 37..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 56..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX22816.1"
SQ SEQUENCE 887 AA; 95816 MW; 17A1622DBEC67CFE CRC64;
LTCMPNNGLS VESNEAVDAL LSLVAWPRAA SLDLKPDRLS SLRKGKKRRK KPQTTNCNKG
GESRRRPGQS EMSSTESGGL DSDSCSTANR TFEPLVRSSP VRTDDSPPLF ASASSSSSLQ
QQFSTLNVIS NNSCTMSNNN NNNNDNNNNS MNSCCTTAVN TISSGCGVAG GGSSSLRYCS
VGVTAAGSGC LEMSLGGSIS CNGTVGAMTL KTTANAAVLS SHLTRCPLCS ELYDQPKVLA
CFHTFCRACL EKLVDTPGKV LCPQCNLETQ FSADQGVDSL FSDYALINLL EQLKVRAGSC
TEASSTVVSV DAASPSSSAS PSASSTSVLQ TNCTGCKSKD MSALAHCYDC TNYLCANCVM
AHKYMHCFEG HRVVDLCDVI PSEVERVVRC MQHRSEPLKY FCVSCSVPIC SECLNSDHPR
GMHHFELMSE VSGQQVMQQL LDEARNKQMK LMESLKATED ATQRLLLSYQ KAQQDIIETA
NLLQQVVEEQ RQQAMRDLEQ AYNCKQLGVN VVDKKLQHTM EKLSHTIEFT SRLLQYTNST
ETLVFKKLLE NRIGVVLNYS PDMNALSQSD LEFVPNVQGS RLAIMNTFGY VRQGQDLSYM
GKSGLAPISR PTLSVTAAQY CQPNGSAPGG PGLGLSIAAA HYLPVVNGSG GAVAGSAGSG
AQVTGVSSHL AGGSLLNGST GPVAVNRATG DIIVTERSPT HQIQVYNQYG QFIRKFGANI
LQHPRGVTVD YKGRIVVVEC KVMRVIIFDM VGNVLVKFGC SKYLEFPNGV VTNDRQEIFV
SDNRAHSVKV FNYEGAYLRQ IGGEGLTNYP IGVGINQLGE VVVADNHNNF NLTVFQQDGM
LINALESKVK HAQCFDVALL DDGSVVLASK DYRLYIYRYL QVSSLIM
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