ID A0A136MVN9_9BACT Unreviewed; 303 AA.
AC A0A136MVN9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cyclophilin type peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:KXK37955.1};
GN ORFNames=UZ09_BCD002001709 {ECO:0000313|EMBL:KXK37955.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK37955.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK37955.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK37955.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK37955.1}.
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DR EMBL; LNBW01000055; KXK37955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MVN9; -.
DR STRING; 1617420.UZ09_BCD002001709; -.
DR PATRIC; fig|1617420.3.peg.1814; -.
DR Proteomes; UP000070267; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR CDD; cd00317; cyclophilin; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KXK37955.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..303
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007476143"
FT DOMAIN 57..106
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 114..301
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 303 AA; 33796 MW; 8CC3D89D4FCE9511 CRC64;
MIISTRFSTL SLLLGIFYVI STASCSSPKA SFSIENQEYR APATIVFNNT SQNADQYEWY
FDDEQMSEQK QPQHTYFASG RYSVTLKAKS GSKSSTAKRD LFIAAPEDCL VAIHTSAGNM
IARLYDDTPL HRDNFLKLAE ENFYNGILFH RVIKGFMIQA GDPESKTAAS GRALGQGGPG
YTIQHEINDT LFHIRGALAA ARLSDDVNPQ KMSSGSQFYI VHGRPVSATN LENNELEKNI
QYDDETKDIY INEGGTPDLD MHYTVFGQII EGLNVIDKIA ASETDRRDRP IDDIKIISIQ
VIK
//