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Database: UniProt
Entry: A0A076H623_9SYNE
LinkDB: A0A076H623_9SYNE
Original site: A0A076H623_9SYNE 
ID   A0A076H623_9SYNE        Unreviewed;       146 AA.
AC   A0A076H623;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   ORFNames=KR49_01995 {ECO:0000313|EMBL:AII45235.1};
OS   Synechococcus sp. KORDI-49.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=585423 {ECO:0000313|EMBL:AII45235.1, ECO:0000313|Proteomes:UP000028589};
RN   [1] {ECO:0000313|EMBL:AII45235.1, ECO:0000313|Proteomes:UP000028589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-49 {ECO:0000313|EMBL:AII45235.1,
RC   ECO:0000313|Proteomes:UP000028589};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequences of Synechococcus sp. KORDI-49.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|ARBA:ARBA00002388,
CC       ECO:0000256|RuleBase:RU363019}.
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|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; CP006270; AII45235.1; -; Genomic_DNA.
DR   RefSeq; WP_043691074.1; NZ_CP006270.1.
DR   AlphaFoldDB; A0A076H623; -.
DR   STRING; 585423.KR49_01995; -.
DR   KEGG; synr:KR49_01995; -.
DR   PATRIC; fig|585423.3.peg.374; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_3; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000028589; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
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; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 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   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU363019};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          1..122
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   146 AA;  15452 MW;  CEEEB3FA32CCE710 CRC64;
     MTKALMETEA GPIELELFEA DAPNTVANFV KLAKDGFYDG LAFHRVIPGF MAQGGCPNSR
     EGSKGMPGTG GPGYQIDCEI NSKKHQAGTL AMAHAGKNTG GSQFYICHEA QPHLDGVHTV
     FGLTGNMDTV LKLGNGSRIT KVTIQD
//
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