ID A0A1C2GI85_9SPHI Unreviewed; 1034 AA.
AC A0A1C2GI85;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OCX51123.1};
GN ORFNames=BEL04_20650 {ECO:0000313|EMBL:OCX51123.1};
OS Mucilaginibacter sp. PPCGB 2223.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX51123.1, ECO:0000313|Proteomes:UP000095113};
RN [1] {ECO:0000313|EMBL:OCX51123.1, ECO:0000313|Proteomes:UP000095113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX51123.1,
RC ECO:0000313|Proteomes:UP000095113};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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:OCX51123.1}.
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DR EMBL; MDJS01000004; OCX51123.1; -; Genomic_DNA.
DR RefSeq; WP_066007057.1; NZ_MDJS01000004.1.
DR AlphaFoldDB; A0A1C2GI85; -.
DR STRING; 1886027.BEL04_20650; -.
DR OrthoDB; 9802793at2; -.
DR Proteomes; UP000095113; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OCX51123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095113};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1034
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008661975"
FT DOMAIN 341..426
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 870..950
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 993..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 112057 MW; 3B2582476BA2739A CRC64;
MKRTLLFCLA LLLFHLAQAQ ETFPVNGAWD VRPGLYAFTN ATIVVNADQT ITNGTLLVKD
RLIEAVGAGI AIPKGYITVD LKGKYIYPSL IDAYTTYGMP EAPRAQFGAG GAGGGGFGLR
STVMVSTKSG PYGWNEAIKP EMAAKAVFHV DATKAADLKK IGFGTVQSLI HDGIARGTSM
VVVLGDERDN EVVLNDVAAA HYSFSKGTAA TNYPSSLMGS IALLRQTYYD AAWYKNQKEE
YNISLDEFNK TQSLPQIFEV TDPLNVMRAS KIAKEFGKQY IFKTDGKEYQ RLNEMKATGS
SFIIPLTFPS AYDVEDPADA RNITYEQMKE WELDPTNPAT LEKAGVRFAI TTYGLDNNTT
FWANLQKAMD FGLTEKQALN ALTTIPAEML GVSDKVGTLT TGKLANFLIT SADLFKKDNV
IYENWVEGRK YVVGKMEVTD LRGAYNLTGA GLSNITLNLS GATPATVSLS AMHTGVDSTR
TQGTFTRTGD GVSFYFDLKG NPTGNIRLAG TITSVSPVTM KGFATLPDGT STPWVATYTG
PAQAGGPGGF GGRGGNNANA AKTPTNVGPV IYPFVAYGNA EIPKVETALF KNATVWTNEK
EGILKNTDVL IENGKIKAVG KNLSAPAGAR IIDATGKHIS PGIVDEHSHI AITGGVNEGT
HSVTAEVRTA DVINSEDINL YRQLAGGVTI SHILHGSANP IGGQLQVIKH RWGLAPEELK
MEGADGFIKF ALGENVKGSN NFGINTNPRF PQTRMGVEQV YVDAFQRAKE YKAARAVKGS
TVRRDLQLDA LVEILDNKRF ITCHSYVQSE INMLMHVADS MGFHINTFTH ILEGYKVADK
MKSRNIAGST FSDWWAYKNE VAEAIPYNGK LMHEVGLVTG FNSDDEEMAR RLNQEAGKSV
TYGKMSEEEA LKLVTLNPAK MLHIDNKVGS IKVGKDADIV LWSADPLSIY AICEKTYVDG
VPYWELDKDA AKQKALKADE ARLIQKMIEA KGSGATTQRA GFGGRRRPQY ECETTEDEQA
DFVSGLGNSQ GGSK
//
