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
//