ID A0A0J1B3X7_RHOIS Unreviewed; 1211 AA.
AC A0A0J1B3X7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Secreted enzyme, contains two amidohydrolase-likedomain protein {ECO:0000313|EMBL:KLU01313.1};
GN ORFNames=RISK_006469 {ECO:0000313|EMBL:KLU01313.1};
OS Rhodopirellula islandica.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU01313.1, ECO:0000313|Proteomes:UP000036367};
RN [1] {ECO:0000313|EMBL:KLU01313.1, ECO:0000313|Proteomes:UP000036367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA Kizina J., Richter M., Glockner F.O., Harder J.;
RT "Permanent draft genome of Rhodopirellula islandicus K833.";
RL Submitted (MAY-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:KLU01313.1}.
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DR EMBL; LECT01000054; KLU01313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1B3X7; -.
DR STRING; 595434.RISK_006469; -.
DR PATRIC; fig|595434.4.peg.6154; -.
DR Proteomes; UP000036367; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 1.
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; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
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:KLU01313.1}.
FT DOMAIN 350..443
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 1024..1098
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 171..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 133146 MW; EEF5C03AF6FA7D89 CRC64;
MGRLMLTISV ACLAVVAHGQ DIRGVAPVVG LRTHSPTDVL LTGATLVANP DHYLKDLGSE
DSAKDSDENA STGDVLIRAG RIVAVSDSIE PPPGCRVVDC SGKTIYAGWI NAWQEVPSDS
LTSGDDYWNA NIVANREVRD LSSVPDAGKL RSQGFTTTVL APKGRILGGQ PSVWSLNESK
DDPDNSHAGP QRIADLKWMT AALSVPRGND SGERYPNSPM GAVALLRQSL YDAQWYRDAS
AAHDANPSLP QPDHSETLQT LHQALVGSTF VFDCPNERMA LRAQKIANEF SLRSIVRGSG
REYREAAAIA ALDRVLLLPL DFPEAPDVAT PESAREVDLV NLMDWKFAPT NPAEMVRQGA
TICLTTDRLD DPGKFLARLR TAVKRGLSRR DAIAALTTTP AGMLGLERSH GRIAAGMSAN
LIVASGDLFE KDTKVWKVLV DGQEFVVNEE PETKVASLVG SWKLRMPADS ATQVKLAITQ
KDGRLSAELI GTTPKEETDE EVLEGEKENL KESSDESVDG DTASSKTDDE ESDTESESDA
SDETKSEEEG SKENKDEEPK EQTSKQKLKK IVQRLDQFAG QITCEDSEDA LCQALGLPEG
THRVVIRSGA KSLEKVSESE PLSIEFYPIG KPARRFETSW VEPETDSDKT PEEESTDEKA
SEDEAPEDKD VESDDSDDSK DADGEQPPEV EVASAEPEQA PEESAADEPV VEELQVVRPL
GVYGRSEPVA PVTRVLFQGA LVWTCEDRDD LRVPETPMDV LVENGRIVAV DEHITVPTGE
DCTIIDASGK HITPGLIDCH SHAATDGGIN ESGQVVTSEV RVGDFIDNTD ITIYRQLAGG
VTTANILHGS ANPIGGQNQV VKFRWGDSMD DFRFQDAPLG IKFALGENVK RNTSRYPNTR
MGVEQLLRDQ FLAAREYAGA HRRWSSGQRD TLPPRVDLQL QTLVEIQDGK RWIHCHSYRQ
DEIMATLDVL DEFGIRIGSL QHILEGYKVA DRMVEHGAMA SSFADWWAYK FEVYDAIPYN
GVLMHNKGIV VSYNSDDAEM GRHLNTEAGK AIKYGGVPPT EALKFVTLNP AKQLRIEDRV
GSIEVGKEAD LVVWSGPPMS TTSRCEQTWI DGRPMFRLQD EAKLRARDEA WRNELIQELL
DGKPKTDSEE PSKDDDEKAL ADHQTMELKE EERWLRYDEF CNSRGAQQSV QQNARQAAQQ
AAKSQRSEEV Q
//
