ID A0A0K0CUU9_ANGCA Unreviewed; 354 AA.
AC A0A0K0CUU9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU365081};
DE Short=PPIase {ECO:0000256|RuleBase:RU365081};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU365081};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000103101-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000103101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU365081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU365081};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily. {ECO:0000256|RuleBase:RU365081}.
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DR AlphaFoldDB; A0A0K0CUU9; -.
DR STRING; 6313.A0A0K0CUU9; -.
DR WBParaSite; ACAC_0000103101-mRNA-1; ACAC_0000103101-mRNA-1; ACAC_0000103101.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR CDD; cd12235; RRM_PPIL4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45843; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR PANTHER; PTHR45843:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365081};
KW Nucleus {ECO:0000256|RuleBase:RU365081};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU365081};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU365081}.
FT DOMAIN 6..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 241..319
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 354 AA; 41048 MW; D2BE25E1C6971829 CRC64;
MAVLLETTLG DVVIDVYVKE RPKSSLNFIK LCKMKYYNLC QFHTIEQNYI AQTGDPTGTG
RGGESIFMKL YGEQARYFEK EDLPKMKHTR MGVVSFVNNG SNMLGSQFFI TLGEELDYLD
DKHTIFGQVT EGLDTLEKLN EQLCDDEHRP YKDIRIAHTI VLDDPFEDHP RLEYPRKSPS
PTFEMLVKTN QIALDENVDD TEGKTAEELA EEIKKREMAE QAQILEMIGD LREADEAPPD
NVLFVCKLNP VTTDEDLEII FSRFGKIIKC EIIRDRRTKQ SLQYAFIEFE DPKSCEQAFF
KMDNVLIDDR RIHVDFSQSV AKLHQWNRSV AEKAHPENRH EVKNDKASVM RFLF
//
