ID A0A452GZF7_9SAUR Unreviewed; 631 AA.
AC A0A452GZF7;
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=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
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:ENSGAGP00000007567.1, 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:ENSGAGP00000007567.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSGAGT00000008736.1; ENSGAGP00000007567.1; ENSGAGG00000006049.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19815; Bbox1_HOIP; 1.
DR Gene3D; 1.20.58.2190; -; 1.
DR Gene3D; 6.10.140.1100; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR047543; Bbox1_RNF31-like.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR032065; RNF31-UBA.
DR InterPro; IPR040641; RNF31_PUB.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF31; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF16678; HOIP-UBA; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF18486; PUB_1; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 211..257
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 296..326
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 339..368
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 250..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 68588 MW; 2608C3358E7BEF34 CRC64;
MAQAVPPLGE PQFLQLREEL VQALARSPVD LHPETVQQLV EAPLPPHIKY REIDAQGILR
ANMQGQSPAC LRTISTALNI LEKYGRNLLN PLKPRYWRGV KFNNPVFRST VDAIQGGRDV
LRLYGYTEQQ PDGLSFAEGL EEPDARRVAS VTVDVVLLRA ELNLLLSNNH PNPDTLQRML
AVGTGSRGAL ARGHEGLGCG VIPLSHPPGP PPRATCLLCG LEPASLHCPE CNQSLCPECD
RLFHKHPARA QHQRLPVGEP GLGAGPPAQS PPFPQGLGLS MVPSEPPVAR PALPPKPRLP
WRCGACHAPN EARAVLCVGC DRPRGCPTPP NPPPDGDPLR GAWACQTCTF LNTGPTVLCA
VCERPRLAGR PGAPDPQHPP DGPPVPMQGA PGWQCEHCTF WNQLPGRVCE VCNRTXGAPG
WQTSQLAGPP QEEKGPRRPG KPHPLSPEEV ERRRQEKLRE DGMKLVAMIR EAELVGVPPE
EVGAALRYSG TELPLPWLRS ELPAVLDAVV EQATERGAGA ELGAITQQEA HAAWTQSQGD
LDEAVSRCLS TRRCKVRELA ALGFAERGPV LQALYQNGGD MWGALTELQR LQLEPFHRRM
WDLAEPEIDF HAPDRQVRAR GRGTWGKSGG G
//
