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Database: UniProt
Entry: A0A1U8DGF8_ALLSI
LinkDB: A0A1U8DGF8_ALLSI
Original site: A0A1U8DGF8_ALLSI 
ID   A0A1U8DGF8_ALLSI        Unreviewed;       755 AA.
AC   A0A1U8DGF8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   Name=PPIG {ECO:0000313|RefSeq:XP_006025671.1,
GN   ECO:0000313|RefSeq:XP_006025673.1, ECO:0000313|RefSeq:XP_014376304.1,
GN   ECO:0000313|RefSeq:XP_025062249.1, ECO:0000313|RefSeq:XP_025062251.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025062249.1};
RN   [1] {ECO:0000313|RefSeq:XP_006025671.1, ECO:0000313|RefSeq:XP_006025673.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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_006025670.1; XM_006025608.2.
DR   RefSeq; XP_006025671.1; XM_006025609.3.
DR   RefSeq; XP_006025673.1; XM_006025611.3.
DR   RefSeq; XP_014376304.1; XM_014520818.2.
DR   RefSeq; XP_014376305.1; XM_014520819.1.
DR   RefSeq; XP_025062249.1; XM_025206464.1.
DR   RefSeq; XP_025062251.1; XM_025206466.1.
DR   STRING; 38654.A0A1U8DGF8; -.
DR   GeneID; 102381809; -.
DR   KEGG; asn:102381809; -.
DR   CTD; 9360; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   OrthoDB; 5324361at2759; -.
DR   Proteomes; UP000189705; Unplaced.
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   ECO:0000313|RefSeq:XP_006025671.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          11..176
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          182..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..249
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..345
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  88435 MW;  18054C29DD2C1BF1 CRC64;
     MGVKVQRPRC FFDIAINNVP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY
     KSCLFHRVVK DFMIQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN
     GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD ASSKPYAEVR ILSCGELIPK
     SKVKKEERKR HKSSSSSSDS DSSSDSDSSS DSSSDSETAS EEKPKKRKKK HKKNSRKHKK
     EKKKRKKSKK SSSSESEVEN PEAQPLSTVR PEEIPPVPEN RFLMRKSPPK VDEKDKERKS
     REKERESNPA NSQSTYQRRL LVTRSGRKIK GRGPRRYRTP SRSRSRDRFR RSETPPHWRQ
     EMQRAQRMRV SSGERWIKGD KSEINENKKD NQKSPGRGKE RKISDHRQAS ESPNRRGEKE
     KKIKDHKSSS KDRETRRNSE KDDKYNKSKA KKRAKSRSHS KSREKSKSKE RDSKHNRHEE
     KRLRSRSKER EYEKGKEKDK HHDSRGREKE RSRSKERCKR AGSKSNEQDH SKSKDREKYA
     KSRSRERDQA KGKYSSNSRT RERSRSRDRG RRARAXXXXS RSKEYSRNRD SRRRGRSRSR
     ERRGTPEKYR GRDNRRRRES RSSEREESQS RHRERYSNRE SRSSYRKNDA ENQRKKRSRS
     YESSSPETNK EKRGSKDQDS KDQDRSPDSK KRQSSKDREM KTSLSRRSKE KEKSRSSLEK
     EINQKSKSQE RDHAHSKDKK SDHESSPGTD EDRHG
//
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