ID A0A183CK63_GLOPA Unreviewed; 1144 AA.
AC A0A183CK63;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001326900};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_001326900}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) 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 AlphaFoldDB; A0A183CK63; -.
DR WBParaSite; GPLIN_001326900; GPLIN_001326900; GPLIN_001326900.
DR Proteomes; UP000050741; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 30..167
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 170..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..348
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 171..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1117
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 129763 MW; A01F6C3BEDAC103A CRC64;
MTIEKTSKVE RRRCFFDIQI EWRRSGLGTN FVMLCTGQAG IGKVTNKPLH FKGSVFHRVI
KNFMIQGGDF SAGNGTGGES IYGGVFEDEA FMAKHEQPFM LSMANRGKDT NGSQFFITTK
PAPHLDDVHV VFGKLISGQE VATKIENLKV NTKSRPISDV VIVNSGQLIK KRSAHDSEME
EEEEIKDSTK KRHHKKGRKR VKRATDDEGE EEEENAEPTA LPILKNEPEN ISSVKPEDLP
EVPSTNKFLM RRSKTPEGKE STRHNLAASS TSVRQSRGSM RVKGRGAIRF RPEDEAFGGG
RSRSATPPHW RREERRLITL KELDQRIKDK LEREEEAQKR AQLKQQERYA TGEVVNETIE
TFGYRNIFAQ QPLLPTEAAA AAAQQQPPTA RREEHQKREE RKERDKRHHH RDGSAERRWP
SDRYRTDAHH AAREQPHDRQ RWRSGARDGS RSPLRNGRAA RDEQSRARGG ASGRGGGDSS
RTPPPRDVER RGEHHRQAPR AAAVEVELQR QHPRHHRAEN SGRDAAAMAG TELEQQKDVG
DEHHHQEKVT AADETENRRG ERYRDRDTYY RDGGRRDTER MPAAERRGDR DRDSRREHRG
GDVRERSRDR QQDGRARHRF YDDEHQQRRD SRDRDRGRRG DEQRRRSRED QRRHSSNSRR
MEAEQGEGVE HGQPKDVAGL VKREALDDHS MRSKWEHEEE PVEENGGEQL PHATSVKLEG
LDVNLQHDIE RSKQHVRGYS DAKEADNEKG IADQQESDQK GQLQRPLKQE IGETGDGGVG
LVAQQQRHKL DVDQNGMGQQ QQDGEKQQKR TNVIAKEKND AKEEVIKQQK SPLSKPKLVS
NDGGVSPVKV APAVVALDQQ AAQTGPVHGG HADDAVAALP TVAPAKERSK AQESDVHADS
ERNHSPRASL ASTNVAEKSV EKPERVVRID EDEFESVGDE AELSKDDKVP AVKEKKKTQS
RSRSSTKSSS SSKSSSSRSS SRPTSKRSPT KKSSAVRSSA SSSSSSSSSS TSRESSSSSA
SSDGKPSREV SRHRSRSRSR SGVRRAARRS PVDERRRSKE LTSRRRSRSR SRRRGGGTDR
SHSSGRRRHL SPRQRRSSRD RSRSRRRRSR SRRRSPSRSP RAGSDRRRRS SQSRDDNRYG
GRRR
//
