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Database: UniProt
Entry: A4AF63_9ACTN
LinkDB: A4AF63_9ACTN
Original site: A4AF63_9ACTN 
ID   A4AF63_9ACTN            Unreviewed;       556 AA.
AC   A4AF63;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Amidohydrolase-like protein {ECO:0000313|EMBL:EAR26264.1};
GN   ORFNames=A20C1_10294 {ECO:0000313|EMBL:EAR26264.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR26264.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR26264.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR26264.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR26264.1}.
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DR   EMBL; AAOB01000001; EAR26264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4AF63; -.
DR   STRING; 312284.A20C1_10294; -.
DR   eggNOG; COG1574; Bacteria.
DR   HOGENOM; CLU_009942_6_1_11; -.
DR   OrthoDB; 3238066at2; -.
DR   Proteomes; UP000003868; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EAR26264.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT   DOMAIN          55..550
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          166..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  59193 MW;  A3EA6D7039861398 CRC64;
     MTTVDLVFTG GAVFTATGSE PTVGSVAVSA GRIVAVSTDP SSESAVLELI GPSTEVIDLN
     GKLLSPGFQD AHVHAVWGGL DMIRCDLSDD STRDQYVARL SAYATAHPEL EWILGGGWNM
     AAFPGGTPTA ADLDLAVTDR PAFIPNRDGH GAWVNSRALE LAEITADTPD PSDGRIERDS
     EGKPTGTLHE GAMSLVNRLL PETSPADYAR ALAIGQEYLH SLGITAWQDA ILGGYGDAGD
     ATPAYMEAAT SGALTARVVG ALWWDRTRGP EQIVDLVTRR ESNAAGRFAA TSVKIMQDGV
     AENFTAAMLE PYLDGCGHHT DNSGISFVDA AQLASNVVEL DRLGFQVHFH AIGDRAVREC
     LDAVAAARAA NGPNDNRHHI AHLQVVHPDD IPRFAELGVT ANMQSYWAAL EPQMVDLTLP
     FLGDPRSSWQ YPWGDLHRAG THLASGSDWS VSSPDPMAAI HVAVNRISAP GHEEGDYEAF
     LPEQSLDLLT AMTAYTAGSA YTNHLDTTGT IEVGKLADLV VLDRNPFDGP VSEIGLTRTE
     QTFVEGERVY LAPVKP
//
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