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Database: UniProt
Entry: A0A183NTU7_9TREM
LinkDB: A0A183NTU7_9TREM
Original site: A0A183NTU7_9TREM 
ID   A0A183NTU7_9TREM        Unreviewed;      1149 AA.
AC   A0A183NTU7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=SMTD_LOCUS5533 {ECO:0000313|EMBL:VDP29093.1};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0000553201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0000553201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP29093.1, ECO:0000313|Proteomes:UP000269396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Denwood {ECO:0000313|EMBL:VDP29093.1}, and Denwood, Zambia
RC   {ECO:0000313|Proteomes:UP000269396};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; UZAL01027087; VDP29093.1; -; Genomic_DNA.
DR   STRING; 31246.A0A183NTU7; -.
DR   WBParaSite; SMTD_0000553201-mRNA-1; SMTD_0000553201-mRNA-1; SMTD_0000553201.
DR   Proteomes; UP000269396; 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:UP000269396};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          1..146
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          209..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..666
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..976
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1036
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1099
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1131
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  128468 MW;  21B2639304C5874B CRC64;
     MGKHKFKTRC YLDIKIDSQP GVCGLGLKTG KPLTYQGSVF HRVIKGFMVQ GGDFSNKDGT
     GGESIYGGTF AEGLTLMALN SSCKAKQSLL SSFSTTAPAP HLNGKHVVFG HVISGEDVVR
     KIEAVPISDT KAHRPVKSIV IESCGELIPG KSPNESGMDN ECSVRKEEIP EVPPPKFLYR
     GNYEEDQLEL QKKVNLSPSI SARISNYSVE SRHDIDSRES ARSRYQEDRS GRVVKGRGRI
     CYQSPNSRSG SPGRSTTPPH WRQASSHTQR LDQDEWKQWN ERRNHEQINN LQRRVSSSRS
     SRGSRQDPLS PSIAASRNRN PSASPSSVVI ANTGVSGCLR DIDSSEKGFS MDQRDGHKQR
     SPSHSPSLDH RVLVNDSKVV ENGSSPTQNN LSPVSIGPKK LYTEFEGKPD DPSDRRYVRS
     PEDIRQASVS EDLFGKDRRA NQRLSEIDDE YMVDIDEDAK FKTLPTTTHE QSPKLSKFSE
     YSTIKSNDVS KRDLGDSPKV YHTNQSPRKC SGSPNLKSPQ QILISPVNSC ASGQQQKYQS
     KSPVLMLSPK PPTSFENHAP IDQPIIISPS RIPYPSPRSG SGSNNRMPSP PCENARISSP
     PDLSNRNQVS HELSRIPTPP QPDNKEQGKV FSEETDLHKL EEIPSPEKPR KQPSPSHSDK
     QLKVTRGSRS ASRSSTLGSR SNSSCESDSS RSCSRSHSQT SPKKRRRRTP RSPPPHLVEK
     WKMRREMLNQ KRRVVPPSVA AYAPSGSSED RLRGIERRHL SGRSTHIHSR SPSRSIPNRR
     RSRSSSSRSK SGSYTHSRTK LNVRRGSPEA ESLRSRRRSP SRDRKTSRSR SHSRSPPKSF
     GLKHRGTSPS KPIIVITKKS QTTQKPTKIV TEDPSTENAV TTSKWENSPQ ILEKNTNQHL
     GPWTNKHWET GDKVELDESV NKDEKKLATA KTQGPNSISI LQRLRVIQED SSKNEEKLEN
     SVAASNETTS IPTVPTMIKP QVPPISKNQV KKPAAIRGRS HSSSSSSASS SSSSGSSSRS
     SSRPKRSRKR CRSISSSARK MQRSDFSDSR SRGRGSRGRY SPVSRSYYTR SRSRSFSTRA
     STNWGTRTSY PSRNRSWSRS RSRSFSRDSR SHSSNARRHK RRHRRTRRGR NSSRSWSSSR
     SSSRSIRRR
//
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