ID A0A452IHM3_9SAUR Unreviewed; 602 AA.
AC A0A452IHM3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-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};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000027442.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000027442.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452IHM3; -.
DR Ensembl; ENSGAGT00000031172.1; ENSGAGP00000027442.1; ENSGAGG00000019947.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19848; Bbox1_TRIM36_C-I; 1.
DR CDD; cd19778; Bbox2_TRIM36_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16756; RING-HC_TRIM36_C-I; 1.
DR Gene3D; 1.20.5.170; -; 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; 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; IPR040859; Midline-1_COS.
DR InterPro; IPR047066; TRIM36_Bbox1_Zfn.
DR InterPro; IPR047065; TRIM36_Bbox2_Zfn.
DR InterPro; IPR027726; Trim36_HC-RING.
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:SF18; E3 UBIQUITIN-PROTEIN LIGASE TRIM36; 1.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR Pfam; PF18568; COS; 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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
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 21..73
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 196..238
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 345..402
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 408..501
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 602 AA; 68743 MW; CEFA624590DDE9DB CRC64;
MEGDRLEPGV TIKNIERELI CPACKELFTH PLILPCQHSI CHKCVKEILF FTLEDSFTDL
GSESSNQSSP RIRIHSPSLD RIDRVNRSGW KRNSLTPRTT IFPCPGCRHD VDLGERGING
LFRNFTLETI VERYRQAARA ATAIMCDVCK PPPQESTKSC MDCSASYCNE CFKIHHPWGT
VKAQHEYVGP TTNFRPKILM CPEHEMERVN MYCEICRRPV CHLCKLGGSH ANHRVTTMST
AYKTLKEKLS KDIEYLISKE SQVKGQISEL GLLMKETECN GERAKEEASN NFDKLFDVLE
ERRSAALRAI EASKNLRLEK LQTQIEEYQG LLENSGLVGY AQEVLKETDQ SCFVQTAKQL
HVRIQKATES LKSFRPAAQT SFEDYVIDIT KQEEVLGDLS FYSSGLDVPE INEEKSRMYN
KALICWEHLV KEDSADTYIL EYRKLNREEE NATWQEIEAC SKSKVISDLE NNSSYAFRVR
GYKGSICSPW SREVILHTPA APVFSFLFDD KCGYNSERLM LNPRRTSVES RAGFPLLLGA
ERIQVGCYTT LDYIIGDTGI TKGKHFWAFH VESYSYLVKV GVASNTKLKE WLHNPRDVTS
PR
//
