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Database: UniProt
Entry: A0A2G5SXM4_9PELO
LinkDB: A0A2G5SXM4_9PELO
Original site: A0A2G5SXM4_9PELO 
ID   A0A2G5SXM4_9PELO        Unreviewed;       428 AA.
AC   A0A2G5SXM4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=PPIase cyclophilin-type domain-containing protein {ECO:0000259|PROSITE:PS50072};
GN   Name=Cnig_chr_X.g25198 {ECO:0000313|EMBL:PIC19780.1};
GN   ORFNames=B9Z55_025198 {ECO:0000313|EMBL:PIC19780.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC19780.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PIC19780.1}.
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DR   EMBL; PDUG01000006; PIC19780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5SXM4; -.
DR   STRING; 1611254.A0A2G5SXM4; -.
DR   Proteomes; UP000230233; Chromosome x.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
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; PS50072; CSA_PPIASE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT   DOMAIN          13..176
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          181..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  49439 MW;  B6E7E8B034683469 CRC64;
     MSSREGRGNK RTFFDITING EPAGRIVFAL YNHSCPSTAE NFRALCTGEL GQLYGHNASY
     QGSIFHRCIK GFMIQGGDLT HKNGQGGFSI YGRTFDDENL SLPHNKPFLL SMANRGPDTN
     GSQFFITTEK VPHLDGKHVV FGEVVKGFDV VKRIEKVETE EEDMPVQRVT IAHCGEMVRK
     SDVMASDKKE KQDEQVAEPE PVGCKMDNEP KTINWLMRRS RSRTPEDGKK SKKDRERRDD
     RGDRRRHDRQ RDRYGRERRS RSRSGSRDRH RDRDRNRVPD ERRSGKRPVI TNKDGIKVRG
     RGKLTFMGSR DRSTTPPHWK REESKKLTLE EHQKRQEEIE ERKQMRAKRE KEDAERKERE
     EKEAMERAAQ RELERQEEEE ARKRSRSDSP PSPVVKVEVM SPRQAESSSS RSSSSSSRSS
     SSSDSDSD
//
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