ID A0A3L8SXX3_CHLGU Unreviewed; 1454 AA.
AC A0A3L8SXX3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=DV515_00001273 {ECO:0000313|EMBL:RLW11351.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW11351.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW11351.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW11351.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW11351.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW11351.1}.
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DR EMBL; QUSF01000003; RLW11351.1; -; Genomic_DNA.
DR STRING; 44316.ENSEGOP00005004006; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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:UP000276834};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 187..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..455
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..548
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1014
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1351
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 164405 MW; 35B200594AEF7E89 CRC64;
MGVQDRPQCF FEIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGIG KTTGKKLCYK
GTTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG
SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDT ASRPYADVRV IDCGVLVTTS
AKDALEKKKK VCSDSEASES SSSVSSSSES SSESEAENER SRRKKRKRRA KTKQSRKRRK
EERKKEDPRC KRTSSQRCLS DKSDVADKVD LSAKRDKPVV RPEEIPPVPE NRFLLRRDVP
VVNIEPEPKL LDAAPVLTDQ KPSVSKSGRK IKGRGTIRYH TPPRSRSCSE SDDEESSETP
PHWKEEMQRL RTYRAPSGEK WSKGDKLSDP CTSRWDERSA SRRSRSWSHN GYADLSTVRY
SSHHKKHRKE KKKVKHKKKS KKQKHFKKHK QTKKKKTSAS SDVESSHSFH RRTKPSCGRE
RKSRSSSLSS RRSSRRDWSK SDKEDQSLSS LSSRGSRSYY RSRSRSRSKS RSYSRRSSRS
RSASKSSRSR SRSRSSSNPR QQKTVPNSPR NISARLNDTK LTKTAEPVRA AILPSDKVIV
PPVVPENLPV IPLSDSPPPS RWKPGQKPWK PSYERIQEMK AKTTHLIPTQ TNYNLVVVKE
ANTSSSYRKQ ERSSESDRSG YSKGRSDRSS GSWPRSRSRS SRSRSYSRSY SRSRSPSSSR
TKSPSSGRSP SPSKYRSDRS GYSESTSDYS LSDEDRHRNK RKSTSSDPKA RGLKVRQETS
SESTLPYTHP KDYDESSQGL KESDSLSSSD FSSDSERSAK ARAVQEKEGR FPLEGDAEKQ
DKNSLSCERG EEKAKGEQDS DHSKKKAAKE KCSEQPRGGA KTKRKSYSGS KWDSESNSER
GEAKHNRGDS RPSSGKEEGE ATSGSDTELS VTKRMKKQSS SSEGFLGSDC AWKTSKQLSS
SESESSCSSS ADTRGKLKKH KHGWKKTPKK SHSKKTKEKS KGKKEKKHKV QKRKEMFHWQ
PPLEFGEEED DEINEKPVTK DDKKEKQLSR DIKDKKQVYE KDETVTDKMG NGEKSCVNEN
LLDKSTTCGA SPDRSNPNKE PIETSTSTGI LNSGINVAAC KSEIKQAEEN NQNGLEDVIQ
TDDNMEICTP DRNSPGKVDV DVLSPVILTA KPLSAGVKKE LQVETPEQDA VKLGNNIRDF
INIKEEKETG RQENNSASVS GAKDCSLKSE NSDNTPSNMI DNKWKPLQGV GNLKPATISM
TMEVKNVASA PEPKPAGLRI EIKAKNKVRP GSLFDEVRKT ARLNRRPRNQ ESSSEEESPS
RDDNSPSRSL SRSRSKSESK SRHRTRSMSY SHSRSRSRSS TYSYRSRSYS RSRSRGWYSR
DRSRSRSSSY HSYKSRRSYS YDSYYSRSRS RSKRSDSYRR SRSYDRRSRS YGSDSDSDRS
YSNNRSPSES SRYS
//
