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Database: UniProt
Entry: A0A2K6PCR8_RHIRO
LinkDB: A0A2K6PCR8_RHIRO
Original site: A0A2K6PCR8_RHIRO 
ID   A0A2K6PCR8_RHIRO        Unreviewed;      1418 AA.
AC   A0A2K6PCR8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   Name=NKTR {ECO:0000313|Ensembl:ENSRROP00000014352.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000014352.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000014352.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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};
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DR   Ensembl; ENSRROT00000038480.1; ENSRROP00000014352.1; ENSRROG00000031389.1.
DR   GeneTree; ENSGT00940000158548; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0016018; F:cyclosporin A binding; IEA:UniProt.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          10..175
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          185..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1139..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..238
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..458
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..568
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..914
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..1013
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1296..1310
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1368..1384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1418 AA;  160823 MW;  1274CDA63B176517 CRC64;
     MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG KTTGKKLCYK
     GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG
     SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDA ASRPYADVRV IDCGVLATKS
     VKDVFEKKRK KPTHSEDSDS SSNSSSSSES SSESEIEHER SRRRKHKRRP KVKRSKKRRK
     EASSSEEPRN KHVMNPKGHS ERSDTNEKRS VDSSAKREKP VVRPEEIPPV PENRFLLRRD
     MPVVTAEPEP KIPDVTPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC SESDDDDSSE
     TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER SLSQRSRSWS YNGYYSDLST
     TRHSDGHHKK RRKEKKVKHK KKGKKQKHCR RHKQTKKRRI LIPSDIESSK SSTRRMKSSC
     DRERSSRSSS LSSHHSSKRD WSKSDKDVQS SLTHSSRDSY RSKSHSRSYS RGSSRSRTAS
     KSSSQSRSRS KSRSSSKSGH RKRTSKSPRK PASQLSENKP VKTEPLRATM AQNENVVVQP
     VVAENIPVIP LSDSPPPSRW KPGQKPWKPS YERIQEMKAK TTHLLPIQST YSLANIKETG
     SSSSYHKREK NSESDQSTYS KYSDRSSESS PRSRSRSSRS RSYSRSYTRS RSLASSHSRS
     RSPSSRSHSR NKYSDHSQCS RSSSYSSVSS DDGRRGKRRL RSSGKKNSVS HKKHSSSSEK
     TLHSKYVKGR DRSSCLRKYS ESRSSLDYSS DSEQSSVQAT QSTQEKEKQG QMERTHNKQE
     KNRGEEKSKP ERECPHSKKR TLKENLSDHL RNGSKPKRKN YAGSKWDSES NSERDVTKNS
     KNDSRPSSDK EEGEATSDSE SEVSEIHIKV KPTTKSSANT SLPDDNGAWK SSKQRTSTSE
     SEGSCSNSEN NRGKPQKHKH GSKENLKREH TKKVKEKLKG KKDKKHKAPK RKQAFHWQPP
     LEFGEEEEEE IDDKQVTQES KEKKVSENSE TIKDNIPKPE KSCEEGSLSA LNTEENVTCS
     QNIQHVEESV TNGVEDVLQT DDNMEICTPD RSSPAKVEEA SPLGNARLDA PDINIVLKQD
     MATEHPEAEV VKQESSMSES KVLSEVGKQD SSSASLASAG ESTGKKDVAE KSQINLIDKK
     WKPLQGVGNL AAPTAATSSA VEVKALTTVP EMKPQGLRIE IKSKNKVRPG SLFDEVRKTA
     RLNRRPRNQE SSSDEQTPSR DDDSQSRSPS RSRSKSETKS RHRTRSVSYS HSRSRSRSST
     SSYRSRSYSR SRSRGWYSRG RTRSRSSSYR SYKSHRSYTY DSYYSRSRSR SRSQRSDSYH
     RGRSYNRRSR SCRSYGSDSE SDRSYSHHRS PSESSRYS
//
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