ID A0A368FRJ1_ANCCA Unreviewed; 502 AA.
AC A0A368FRJ1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase, cyclophilin-type {ECO:0000313|EMBL:RCN33450.1};
GN ORFNames=ANCCAN_20719 {ECO:0000313|EMBL:RCN33450.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN33450.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN33450.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN33450.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:RCN33450.1}.
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DR EMBL; JOJR01000921; RCN33450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368FRJ1; -.
DR STRING; 29170.A0A368FRJ1; -.
DR Proteomes; UP000252519; 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 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; 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 PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000313|EMBL:RCN33450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519}.
FT DOMAIN 274..420
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT COILED 425..454
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 502 AA; 56982 MW; 589049CB0A256FAF CRC64;
MGKKQHQKDK LYLTTTEWKE IGGHKDGVFL LLWGFSQQNL FQFINDTVLS FSNFRHIIPY
LKKNGVNPCT GKKMSSKDLI HLKFDKDDQG RFRCPVTFRQ FTDHTHVVAI ATTGNVFSYE
AVQELNLKAN HLKDLLTDTP FHRSDIIVLQ DPHHLEKFNM EKFFHVQFDP KTKEQIEKEK
KEMQDPKFYI RRMNNETKEA LDQLKKDYIP KKIEPVADET ADEINAAHYS QGHVAAGFTS
TTMAPVTKQK AAVLSDEAVR YSRVKKNGYV RIITNHGSLN IELFCPKAPK TCENFILLCS
RGYYNNTRFH RIIKNFMMQG GDPTGTGHGG ESAWGKPFDD EFAPGLSHDA RGILSMANKG
TNTNQSQFFI TFRPCKYLDK KHSIFGRVVG GQDTLIAIEK VETDGSDVPK DPVYFMRAEV
FVDPFEEAEA EVQKERATLL NKDAQKEADA KKEALAKPKA YGTGVGKYIN PQNKRPAGDA
LPSTIALKKR AVKTSLTDFS AW
//
