ID A0A0V0SGH1_9BILA Unreviewed; 525 AA.
AC A0A0V0SGH1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=cyn-4 {ECO:0000313|EMBL:KRX25831.1};
GN ORFNames=T07_2175 {ECO:0000313|EMBL:KRX25831.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX25831.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX25831.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX25831.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX25831.1}.
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DR EMBL; JYDL01000010; KRX25831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SGH1; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; 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; 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 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.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KRX25831.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 290..433
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 525 AA; 59929 MW; 436AAFCAE91DCCBE CRC64;
MGKKQHQKDK MYLTTTEWKE LYGGHKDTKI FQASLAKFQR LPFGHCCVSL QPCDVPYCCL
DGYIFDLIHI LPFVRKFGKH PVTGNPLDVK SLIKLDLKKN SEGQYVCPIT KNAFTDNSHV
VMVRPTGIVY SYEAVEELNF KTKHFKDLIT DEPFVKADII TLQDPYKLEK FNISKFYHVK
NKLKVKEDEV EELPQDDPLY KLKSINTETR ETLSQLQKDY KAPEKQELPS TSKADALNAA
HYSTGMVAAG FTSTVMEPVT EQQPAVLDED ILKYRRVKSM GYVRLVTNKG LLNLELYCEK
VPRACENFIV HCRNGYYKQT KFHRLIRNFM VQGGDPTGTG TGGESIWGKP FRDEFVSLYS
HSGRGVLSMA NRGKHTNTSQ FFITFRSCKQ LDKKHTIFGR VVGGLDTLEK IEAIETDNND
RPVEDIVILD TVVFVNPFEK AEEQLKAERK AALEQSGKEE KKVVMVEKKS AEKKIFRSGV
GKYIDLKAVA KSNDQSDDEE QPLNSITVAK KKKVIRTELS DFSQW
//
