ID A0A0V0S837_9BILA Unreviewed; 1258 AA.
AC A0A0V0S837;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KRX22815.1};
GN ORFNames=T07_12613 {ECO:0000313|EMBL:KRX22815.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22815.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22815.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22815.1};
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:KRX22815.1}.
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DR EMBL; JYDL01000029; KRX22815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S837; -.
DR STRING; 6336.A0A0V0S837; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
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 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; 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; 5.
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 278..318
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 483..526
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 535..574
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 988..1031
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 1035..1080
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 1081..1122
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 1123..1165
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 1166..1209
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..639
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 108..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 135816 MW; 6A27EA124E85B117 CRC64;
MRSLAHFGPL ASTDAFGWCS ASKQDKNAHT HTERRNQSHQ PHTQPPLITA FIATGCPDLQ
RIEREKETVD ALLSLVAWPR AASLDLKPDR LSSLRKGKKR RKKPQTTNCN KGGESRRRPG
QSEMSSTESG GLDSDSCSTA NRTFEPLVRS SPVRTDDSPP LFASASSSSS LQQQFSTLNV
ISNNSCTMSN NNNNNNDNNN NSMNSCCTTA VNTISSGCGV AGGGSSSLRY CSVGVTAAGS
GCLEMSLGGS ISCNGTVGAM TLKTTANAAV LSSHLTRCPL CSELYDQPKV LACFHTFCRA
CLEKLVDTPG KVLCPQCNLE TQFSADQGVD SLFSDYALIN LLEQLKVRAG SCTEASSTTP
TPITTNTTIA SSSSSTLSNT TTSPVGGGGS SSSSSLPGSC CTDESASLSS VHNSNNTTTT
TTAVATTTTT ASTSATNNMA VNNSSTANNI NTSSSTVVSV 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 GPSTAGGALS
TPPHAFSDSN LLQSKQYGDS SQSLGPYSAL GDTYGGYEKW STGAPTVADV AYHHQQQQQQ
HHQQQHHQQQ QQQQQQQQQQ QQHHSGSLGS LHQHVTGFLS DSGLYTPSPL GDQNGSHPVM
ELNSKLMNTP LSFFPPKSQI KRHKMIYHCK FGEFGVAEGQ FTEPSGVTVN SLNDIIVADT
NNHRIQIFDK DGRFKFQFGE CGKRDGQLLY PNRVAVNRAT GDIIVTERSP THQIQVYNQY
GQFIRKFGAN ILQHPRGVTV DYKGRIVVVE CKVMRVIIFD MVGNVLVKFG CSKYLEFPNG
VVTNDRQEIF VSDNRAHSVK VFNYEGAYLR QIGGEGLTNY PIGVGINQLG EVVVADNHNN
FNLTVFQQDG MLINALESKV KHAQCFDVAL LDDGSVVLAS KDYRLYIYRY LQVSSLIM
//
