ID A7T106_NEMVE Unreviewed; 506 AA.
AC A7T106;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=NEMVEDRAFT_v1g248427 {ECO:0000313|EMBL:EDO30353.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO30353.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO30353.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS470064; EDO30353.1; -; Genomic_DNA.
DR RefSeq; XP_001622453.1; XM_001622403.1.
DR AlphaFoldDB; A7T106; -.
DR STRING; 45351.A7T106; -.
DR EnsemblMetazoa; EDO30353; EDO30353; NEMVEDRAFT_v1g248427.
DR KEGG; nve:5501116; -.
DR eggNOG; KOG0883; Eukaryota.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; A7T106; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 7846at2759; -.
DR PhylomeDB; A7T106; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 Pfam; PF04641; Rtf2; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 36..109
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 286..429
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 448..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 57437 MW; 82CF340E103F1370 CRC64;
MGKKQHQKDK LYITNKEWKE EWGGKRPDAG ERAAFRRLPF HCCSLSLQPF EHPLCTKEGV
IFDLVNIVPY LKKYGRNPVT GEPMQVKELI KLHFHKNADG KYHCPVTYKV FNQNTNIVAI
KTSGNVYCLD AVEQLNFKAK NFRDLLTDEA FTRKDVITLQ DPSKLDKFNM SNFHHLKNNL
KVLDKDEERA KQDPKYYLNK TNKETESILN ELDKTFKEPE KKKEEDREMV TDRNAAHFST
GAVAQSFTST AQDRVTEQEA AVVDKDVVRY REVKKKGYVR IQTTHGDLNL ELHCEMVPKT
CENFMKLCAK GYYENTVFHR SIKNFMIQGG DPTGTGRGGE SAWGGEFKDE FKPNLIHQGR
GILSMANSGP NTNKSQFFIT YRSCRHLDQK HSVFGRVVGG LETLNAMERI ECDEKDRPKE
TIKIKKAVVF VDPFAEVDEA EDAEKAKKRA AAADAGPTVH RPGATVGKYI PRAAGKTGAD
YESTTSQPVS KKLKKASSGF SDFSAW
//
