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Database: UniProt
Entry: R7QFA0_CHOCR
LinkDB: R7QFA0_CHOCR
Original site: R7QFA0_CHOCR 
ID   R7QFA0_CHOCR            Unreviewed;       644 AA.
AC   R7QFA0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   ORFNames=CHC_T00008322001 {ECO:0000313|EMBL:CDF36438.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF36438.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
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DR   EMBL; HG001780; CDF36438.1; -; Genomic_DNA.
DR   RefSeq; XP_005716257.1; XM_005716200.1.
DR   AlphaFoldDB; R7QFA0; -.
DR   STRING; 2769.R7QFA0; -.
DR   EnsemblPlants; CDF36438; CDF36438; CHC_T00008322001.
DR   GeneID; 17323970; -.
DR   Gramene; CDF36438; CDF36438; CHC_T00008322001.
DR   KEGG; ccp:CHC_T00008322001; -.
DR   OMA; NECIRAC; -.
DR   OrthoDB; 25281at2759; -.
DR   PhylomeDB; R7QFA0; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 3.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR46512:SF9; TETRATRICOPEPTIDE REPEAT DOMAIN 9; 1.
DR   Pfam; PF00254; FKBP_C; 2.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF54534; FKBP-like; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 2.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   DOMAIN          100..188
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          332..434
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REPEAT          535..568
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  70661 MW;  BE355CF8E9137717 CRC64;
     MPAPSLSAPS LRPYHCFSSP SPTFEPPASP KPHPPTPSSP SPHSPYYLDP NISMDKPVAT
     TDADGEVEDF SKSGDLTGDG GVIKEILQQG VQGWEKPENG DDIQMHYRGT LLDGTTFDSS
     YDRGTPFSFK LGDGKVIRGW DVVGKTMAKG EKAKVTLKPE YAYGAAGSPP KIPENAILVF
     EMELLSWTSK RDVFGDGTVI KTEISPGTGW ERPGSLAEAT LAVSATHMNE NARDELAKLH
     EGEVIFTFGG KQVPEAWEKV VKDMKKDTEV SLICRPPHTT GPSVDYVPAD AKCVKFGLKL
     LSWRKIEDIH SDGKLVKKVL QEGDGWERPN EGSTVTVTAK YMLPDTTSSL LVPPPAGGDA
     VVVEDLEFKV GDGVVIDALD RVVQSMKVNE SAIVAVAPEH AFGSAVGLLT EEFTAKGFKA
     DSKILIDLKM TKFEKAKDVW SMSFEEKVEE MNIRKERGND LFKSGRYATA KKSYDRAVAF
     FDSPTSELSP ELKAKVNELL VKCHLNLAVC LNKLGDIQQV MVHCKKALEI QPSNDKALYR
     QGCAYLALDD YDNAKLSLKY ALELSPKNAD IQRKLRELKE KRSKQDAQDK KLYSNLFGRM
     RKLEEQEHQG AGSNGLPNPT EMKPEGIVSD AEMKEAPAEP VKAQ
//
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