ID A0A3Q7TN00_VULVU Unreviewed; 795 AA.
AC A0A3Q7TN00;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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};
GN Name=TRIM9 {ECO:0000313|RefSeq:XP_025856490.1};
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_025856490.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025856490.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025856490.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025856490.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR RefSeq; XP_025856490.1; XM_026000705.1.
DR AlphaFoldDB; A0A3Q7TN00; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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; cd19843; Bbox1_TRIM9_C-I; 1.
DR CDD; cd19826; Bbox2_TRIM9_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR049582; TRIM9_Bbox1.
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; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF13; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 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; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
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 10..50
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 163..212
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 224..266
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 374..432
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 440..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 602..787
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 288..344
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 795 AA; 88781 MW; DA2E51EA59834301 CRC64;
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSR RASGSGVSDY
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
PLLQSIHQLD FVQMKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PAEGYILELD
DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARIKAFNKTG VSQYSKTLVL QTSEDTDSEE
QTLPFPVPSE RLPLRRMSPF SSTLNLQPSF PGRSYFDFRS SPHQLSLHSS LQSLNAPGCS
FEPQSAPYTQ LVDIKKLLAV AWFAFDPGSA HSDIIFSNDN LTVTCSSYDD RVVLGKTGFS
KGVHYWELTV DRYDNHPDPA FGVARIDVMK DVMLGKDDKA WAMYVDNNRS WFMHNNSHTN
RTEGGIAKGA TIGVLLDLNR KTLTFFINDE QQGPIAFENV EGLFFPAVSL NRNVQVTLHT
GLPVPDFYSS RASIA
//