ID A0A0C9LS33_9FUNG Unreviewed; 980 AA.
AC A0A0C9LS33;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Composite domain of metallo-dependent hydrolase {ECO:0000313|EMBL:GAN02515.1};
GN ORFNames=MAM1_0023d01959 {ECO:0000313|EMBL:GAN02515.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02515.1};
RN [1] {ECO:0000313|EMBL:GAN02515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02515.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF836312; GAN02515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LS33; -.
DR STRING; 91626.A0A0C9LS33; -.
DR OrthoDB; 1355382at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF5; AMIDOHYDRO_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01979; Amidohydro_1; 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:GAN02515.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 453..545
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 106432 MW; 0AEF26C4BCA11E97 CRC64;
MTSIGNQPSY ASIVRDGEDA RGRDGEGSSS SPLLSSRKGK ELNWHDRMRR AQHFARRNIY
HILTLFTIAI LLVVLLVYTL LPDSSVFPAK EVHAVPHPIQ AGVSELTMEK GRMQCEAIQT
RKREKNTPNE SRKNPRAEVT QQPILLKNAV VWDGQGHVLK HVDVYVENGI IQKVEKDIKA
AGSHVKVIDV AGHVVGPGLV DMHSHMGVDS WPELDATQDT NEMTQPLTPF VRTLDAFNPS
DKAIRIVSSG GVTTALVLPG SGNLMGGEAF AFKLRPKSTL SNEDMLVQAN INPEQDTKWR
WMKMACGENP KRVYGSQNRM PSTRLGEAYL FRKELARAQA LKQQQDDWCQ AASLNDPLAR
FDTAFPQDLS LESLVSLLRG EVLLNVHCYE THDIEAMVRH SLEFNFTISA FHHALDAYRI
PAILRRAPNN ITVATFADHW GYKKEAFQAI PEAPKILYDA GIPVALKSDH PVLNSQHLIF
EAAKTTHYGL PAQEAFKAVT SVPANAIGLG HRIGSLKVGY DADMVIWDRE PLALGATPLQ
VFVDGVPLFE EKAIESATAA VEEEEEDKKQ ASTATANSQP PRKMHGAKSF VLKNAGYSFL
GQLPTQGPVD IVVQDGSIVC SAVDCTSTIA SIQTTKAVPE YDLQGGYILP GLIGVGSSLG
LIEIQGEAGT GDGRAPSSKS QDAKDIIQTV DGIKLSTRHL EEAYKGGILT AITAPMSNNV
VVGVSAAFKT GADSLLTDGA LLSSAVALHL QIGDDYKSSS FPTISSQISF IRQLFKDNLK
SDNYYGKAAR GEIPTIIIAH NKDEIASLVV LKRDHFPQAR LVIQGGTEAY LVASHLAALD
IPVVLQPVLC TPSRFDSIHC LTGAPLTNGT AAHALHRHGV KLGVGIYDDG LARNLAWDSG
WLAATSPSAS ELEHGAITEL EAIQFVTSHL RDIYGLNQAA AALDLDDEFI VYSGNPFDVK
HRLMFIHSSS NGLEALQHDA
//
