ID A0A0D2US04_CAPO3 Unreviewed; 508 AA.
AC A0A0D2US04;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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};
GN ORFNames=CAOG_007850 {ECO:0000313|EMBL:KJE97746.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE97746.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KE346375; KJE97746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2US04; -.
DR STRING; 595528.A0A0D2US04; -.
DR EnsemblProtists; KJE97746; KJE97746; CAOG_007850.
DR eggNOG; KOG0415; Eukaryota.
DR InParanoid; A0A0D2US04; -.
DR PhylomeDB; A0A0D2US04; -.
DR Proteomes; UP000008743; 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:UP000008743};
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..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 242..320
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 325..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 57365 MW; 71C4BAE9DBA7A9A1 CRC64;
MSVLVETSLG DIVIDLNVEH APIASLNFLK LCKLKYYNYC LFHNIQRDFI VQTGDPTNTG
RGGTSVFGIV DGPSRRLFRD EIVPTVKHVA VGTVAMAGSG KDGNGSQFYI TTAPALESLD
GKHTIFGQVV EDESLATLAR INDSFCDDKG QPYKDVRIKH TIILDDPFPD PPGLRVPDES
PLPSKEQLET GRLAEDEEIN VWQGRSDEEI EEAIKDREMY AGAQILEMVG DLPDANIRPP
ENVLFVCKLN PVTKDEDLHV IFSRFGDIRS CDIIRDPVTN ESLCYAFIEF EREADCEEAY
FKMDNVLIDD RRIKVDFSQS VARVGGQQQR FDSRRQERDM SLPSGIRLRN SSGSHGAHRD
MVFEHDHYAE NSSSSKRARM DTEPAARDRQ HSSHSGHDRY ENGGRDYRSD SRDRERSSRD
SRRDAPSGSS SSSSSSHRSS HDGDRDRRSS SDRDGDRDRR SSSDRDRYSS SSGRAGHERH
DRDRHYSSSS SSNDRHSSSR DSDDRRHR
//
