GenomeNet

Database: UniProt
Entry: A0A3E2XPR9_9FIRM
LinkDB: A0A3E2XPR9_9FIRM
Original site: A0A3E2XPR9_9FIRM 
ID   A0A3E2XPR9_9FIRM        Unreviewed;       634 AA.
AC   A0A3E2XPR9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN   ORFNames=DW747_03785 {ECO:0000313|EMBL:RGC50502.1};
OS   Coprococcus catus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=116085 {ECO:0000313|EMBL:RGC50502.1, ECO:0000313|Proteomes:UP000261231};
RN   [1] {ECO:0000313|EMBL:RGC50502.1, ECO:0000313|Proteomes:UP000261231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM28-39 {ECO:0000313|EMBL:RGC50502.1,
RC   ECO:0000313|Proteomes:UP000261231};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RGC50502.1}.
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DR   EMBL; QVFD01000002; RGC50502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2XPR9; -.
DR   Proteomes; UP000261231; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000261231};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}.
FT   DOMAIN          404..542
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70431 MW;  BE856561E8325588 CRC64;
     MGIAAVDMSE KNNKSNSPAD NTKSEKKMTK YDLKMQRRQE EERKAKKEKK IIKTGCILAV
     IICVCIAAWK FYDNYQEKHG PYITVGDHEI QKAEFDYYYY SSLNSFASTY GSYLSYFGLD
     TSKPLDQQQY SDTMTWDDYF QQQAVNQLKN VYALTDEANE KGFEYDASSD YDDMVTSIKS
     YAQQQGVSED EYCKSVFGSD ATLEGIKPYV EMSGLASAYY NDVKDDIEVT DDEINTYYDE
     NKDNYDSVDY RVCKIEADMP EEETETETEA QTETAAESTS ETAVTETQTE TESETMSAEE
     SEAAAKAEEE AKKAAMAEAK AKADDMLSKI TDEASFEKVY GDYATDASTD SLNTGKKKSS
     ISPTDVANWL FDADRQAGDT TVIEDTANNA YYVVYFKDRY LDHIKTVDVR QILISADTSS
     SDAAETDETE TTAAGETETA ETESAEAQEQ AKEDAKAAAK IKAEQILDDW KNGDATEDSF
     AELANTYSDD SGSNTNGGLY EAVKEGQMVT NFNDWIFDAS RKPGDTGIVE SDYGYHIIYF
     VGDNKEEWYV NIKDTITSNK LNDYMSDLTA DIEVKDSRHH VAYLHETEAA TETTSDTAAS
     TESAAASESA AETAASETET VAETTTETAE TTAK
//
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