ID A0A0K1ESD2_CHOCO Unreviewed; 536 AA.
AC A0A0K1ESD2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CMC5_079340 {ECO:0000313|EMBL:AKT43699.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT43699.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT43699.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT43699.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012159; AKT43699.1; -; Genomic_DNA.
DR RefSeq; WP_050435129.1; NZ_CP012159.1.
DR AlphaFoldDB; A0A0K1ESD2; -.
DR STRING; 52.CMC5_079340; -.
DR KEGG; ccro:CMC5_079340; -.
DR OrthoDB; 613638at2; -.
DR Proteomes; UP000067626; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..536
FT /note="AB hydrolase-1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005459912"
FT DOMAIN 103..244
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 414..507
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 56991 MW; 32635AF4D6D2A7BD CRC64;
MLSRSSTCAL LTCTLAFLPA CAGDPERLEA PLDAPTPTPQ PGPEPPAPLQ LTWSPCDLFS
GGAGDGTATC TELEVPLTWD DPAGRTLTLF VKRLQATAPR RGALLLLDGG PGGGSVGPEG
VAHDLAQRDP GLDVYLPHHR GTGLSTRLSC AGDAPGSESG VLITDAEWPA CIDELQQQWG
AGLSAFNTTE AARDLGALVA AIQAEHPEEQ TFVLGSSYGT YLANRYLTLH PDQPTAVIYD
SICPPDACHL DEFDVLYDQV ATEFLALCGA DATCSSHLGP DPRARLATLY DALDAGHCPA
LGDRGVDRSL LRKVLGILLN DWNLRLAIPA VIRRVERCSN DDLTALDHLL DLLSSDPQTP
SPFLTAWSFP LQNNILFSEL WSAPPPPVAD ILAAAEATLI SQGTTLQEAD LFTVWPRYER
DAHFGQWAST TVPLLMMNGD LDPATPITLA ERVADHHTAP GQTFVRLPRS PHGVLTGSPI
HPNGETCGTA LLLAFLADPH APLDTSCKDQ VLPLNFAGAP WLAQALFGTS DFYGLP
//
