ID A0A2K6GRR8_PROCO Unreviewed; 1464 AA.
AC A0A2K6GRR8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSPCOP00000028927.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000028927.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000028927.1}
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 RefSeq; XP_012520957.1; XM_012665503.1.
DR STRING; 379532.ENSPCOP00000028927; -.
DR Ensembl; ENSPCOT00000039862.1; ENSPCOP00000028927.1; ENSPCOG00000027138.1.
DR GeneID; 105827380; -.
DR KEGG; pcoq:105827380; -.
DR CTD; 4820; -.
DR GeneTree; ENSGT00940000158548; -.
DR OMA; DSHHKKR; -.
DR OrthoDB; 5324361at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0016018; F:cyclosporin A binding; IEA:Ensembl.
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:UP000233160};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 183..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
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..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1012
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1387
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 166153 MW; FFF8022FE2D25EFF CRC64;
MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG KTTGKKLCYK
GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG
SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDA ASRPYADVRV IDCGVLATKS
TKDVFEKKRK KPTHSEDSDS SSNSSSSSES SSESEIEHER SRRRRHKRRP KVKRSKKRRK
EASSSEEPRN KHVMSPKGHS ERSDTNEKRS ADSNAKREKP VVRPEEIPPV PENRFLLRRD
MPVVTVDPEP KIPDVAPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC SESDDDDSSE
TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER SLSQRSRSWS YNGYYSDLST
ARHSDSHHKK RRKEKKVKHK KKGKKQKHCR RHKQTKKRRV VIPSDIESSK SSTRRMKSSC
DRERRSRSSS LSSHHSSKRD WSKSDKDVHS SSTRSSRYSY RSKSHSRSYS RGSSRSRTAS
KSSSRSRSRS KSRSSSKSEH QRTASKSPRI ASQLSESKPI KTEPLRATVP QNENVVVQPV
VAENIPVIPL SDSPPPSRWK PGQKPWKPSY ERIQEMKAKT THLLPIQSTY SLANVKETDS
SSSYHKRGKN SESDRSAYSK YSDRSSESSA RSRSRSSRSR SYSRSYTRSH SLASSHSRSR
SPSSRSHSRN KYSDHSQCSR SSSYTSVSSD DGRRAKRKLR SSGKRNSTSN KRHSSSSEKT
LRNKYVKGRD RSSHQRKYSE SRSSLDYSSD SEQSSVQITQ SAPEKEKQGQ LEIKTNKQEK
NRDEEKSKPE RECPPSKKRT LKENLSDHCR NGSKPKRKNY AGSKWDSESN SERDVPKNSK
NDSRPSSDKE EGEATSDSES EVSEIHIKAK PTTKSSANTS LPVDNSTWKT SKQRSSTSDS
EGPYSNSENN RGKPQKHKHG SKENLKREHT KKVKEKLKGK KDKKHKAPKR KQAFHWQPPL
EFGEEEEEEI NEKQVTQESK EKKVSENSET IKDNIPKIEK SCEEGNLSSK HNTVTVSSDL
DQLTKDDNKL RISPTALNTE ENVASSPQNI QRIEESVPSG VEDVLQTDDN MEICTPDRSS
PAKVEGASPL GKSQLDTQDI SVVLKQDVQT ENPETEVVKQ ESSVSESKAL GEVEKQESSS
ASFASAGEST EKKEVAEKSQ VNLMDKKWKP LQGVGNLAAP TAITSSAVEV KALTTVPEMK
PQGLRIEIKS KNKVRPGSLF DEVRKTARLN RRPRNQESSS DEQTPSRDGD SQSRSPSRSR
SQSETKSRHR TRSVSYSHSR SRSRSSTSSY RSRSYSRSRS RGWYSRGRSR SRSSSYRSYK
SHRTSSRSRS RSSSYDPHSR SRSYTYDSYY SRSRSQSRSQ RSDSYHRGRS YNRRSRSCRS
YGSDSESDRS YSHHRSPSES SRYS
//
