ID A0A3Q7TDP3_VULVU Unreviewed; 771 AA.
AC A0A3Q7TDP3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM56 {ECO:0000313|RefSeq:XP_025875459.1,
GN ECO:0000313|RefSeq:XP_025875460.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025875459.1};
RN [1]
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025875460.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025875460.1};
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025875459.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025875459.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025875459.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_025875459.1; XM_026019674.1.
DR RefSeq; XP_025875460.1; XM_026019675.1.
DR STRING; 9627.ENSVVUP00000032563; -.
DR KEGG; vvp:112935775; -.
DR OrthoDB; 207577at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19789; Bbox2_TRIM56_C-V; 1.
DR CDD; cd16584; RING-HC_TRIM56_C-V; 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; 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:SF304; E3 UBIQUITIN-PROTEIN LIGASE TRIM56; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
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; PS50119; ZF_BBOX; 1.
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:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 21..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 164..205
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 371..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 374..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 83198 MW; 70DF6E2E641C7882 CRC64;
MVSQGSSPSL LEALSSDFLA CKICLEQLRA PKTLPCLHTY CQDCLAQLAE GGHLRCPECR
ETVPVPPAGV AAFKTNFFVN GLLDLVRARA GGDLRAGKPA CALCPLMGGA GTGGPATARC
LDCADDLCQA CADGHRCTRQ THTHRVVDLV GYRAGWYDEE ARERQAAQCP QHPGEALRFL
CQPCSQLLCR ECRLDPHLDH PCLPLAEAVR ARRPGLEELL AGVDNNLAEL ESARMVEKEA
LARLREQAAK VGTQVEEVAE GVLRALLAQK QEVLGQLRAH VEAAEEAARE RLGELESREQ
VARAAAAFAR RVLSLGREAE ILSLEGAIAQ RLRQLQGCPW MPGSAPCLLP QLELHPGLLD
KNCRLLRLSF EEQQPQKDSG KDEAESQGGD ETQSWREDGA KSERQGAVQP QSRDGAYAPK
ENRAQTPQED GAQTPKEDRA KTPQEDGAQT PKEGRAQTPL EDEGAQTPRG GRSNKKRKFK
GRLKSISREP SPAPGLNLEG SGLLPRPIFS CSFPTRMPGD KRSPRITGLC PFGPREILVA
DEQNRALKRF SLSGDYRGAV PVPEGCSPCS VAALQGAVAF SAGARLYLIS PDGEVQWRRA
LSLSQASHAV AAMPSGDRVA VSVSGHVEVY NMEGSLATRF IPGGKANRGL RALVFLTTSP
QGNFVGSDWQ QNSVVVCDGL GQVIGEYRGP GLHGCQPGSV SVDKKGYIFL TLREVNKVVI
LDPKGSLLGD FLTAYHGLEK PRVTTMVDGR HLVVSLSNGT IHVFRVRSPD S
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