ID A0A091SYU6_NESNO Unreviewed; 479 AA.
AC A0A091SYU6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=N333_08431 {ECO:0000313|EMBL:KFQ48605.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ48605.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ48605.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ48605.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000256|ARBA:ARBA00007930}.
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DR EMBL; KK938243; KFQ48605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091SYU6; -.
DR Proteomes; UP000053840; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd01923; cyclophilin_RING; 1.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF1; RING-TYPE E3 UBIQUITIN-PROTEIN LIGASE PPIL2; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KFQ48605.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053840}.
FT DOMAIN 1..66
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 243..391
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 449..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ48605.1"
FT NON_TER 479
FT /evidence="ECO:0000313|EMBL:KFQ48605.1"
SQ SEQUENCE 479 AA; 53707 MW; 202CC8F1C3D921CC CRC64;
SLSLQPFEYP VCTPDGTVFD ILSIVPWIKK YGTNPITGEK LDAKSLIKLN FAKNSEGKYH
CPVLFTVFTN NSHIVAIKTT GNVFAYEVVE QLNIKPKSYK DLLTDEPFTR QDIVTLQDPT
NLDKFNVSNF FHVKNNIKVI DPDEEKAKLD PSYYLKNTNT ETRETLLELY KEFKGDDILA
ATMKAPEKKK VDKLNAAHYS TGAVSASFTS TAMVPETTHE AAAIEEDVVR YTYVKKKGYV
RLHTNKGDLN LELHCDMTPR TCENFIKLCK KNYYDGTIFH RSIRNFVIQG GDPTGTGTGG
ESYWGKPFKD EFKPNLSHTG RGVLSMANSG PNTNKSQFFI TFRSCAYLDK KHTVFGRVVG
GFETLTAMEN VESDPKTDRP KEEIRIETTT VFVDPYEEAD AQVAAEREKV QLEEAAAKAK
AEVVPPKKEV QTPKTYRQGI GKYINMAAAK RSMEDDGPST STAAKKEKKS TGFGDFSSW
//
