ID A0A3D8R4H8_9EURO Unreviewed; 976 AA.
AC A0A3D8R4H8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN ORFNames=DSM5745_08732 {ECO:0000313|EMBL:RDW68972.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW68972.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW68972.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW68972.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW68972.1}.
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DR EMBL; PVWQ01000011; RDW68972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8R4H8; -.
DR OrthoDB; 1355382at2759; -.
DR Proteomes; UP000256690; 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 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; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000256690};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 439..525
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 976 AA; 105655 MW; 35894227787AC3D8 CRC64;
MLGLPYGMMD GKSDFYAHSA RRFETSGHRR ARHALRRWRV LIWTALCAGI LFLINGVPLS
SNFTLSTDLT AERVLYEGLQ QCYETVNHPK GETAPSADRH NPRWNAVSGQ KTPIAIQNAT
LFDGETTLPY SVDIVFDAGV VRSVTPTNSN NSLPEDAEII NVHGKHVTPG LVDLHSHHAL
LPFPSLSATS DANERPLLGP ITPFVRATDG FTPSDPAIKL IASGGVTSSL VLPGSANIVG
GQAYPVKNLP YPGAAAEPVI DELLLEDGIQ ESQRQRYLKM ACGENPRRVY GHTRMGLAWL
LRKELNKAKE LLEKQEAWCA AASKLQGEGS EFRFRLRQRD QVSAFVEREG PRPDSFDLET
FLALLRGEIN LNVHCYTPED LETMLSVLHE FGVHPRAFHH ALEAWQVPEL LKRLEPNVTI
ATFADSALYK AEAYDASLQA PKILHEHGVR VALKSDHTGE SDYAKYLLDQ ASVAHSYGLL
TDAALQSVTS IPAESMQQGH RIGYMRLGYD ADLVIWDSHP LQVGATAVEV FIDGRPLLRK
DLKEISKQLE PTYREPQGSL DIRQQAPATR PLMKAEERGE VCKRIQEGAA KGTVVFTGIK
EALLDVPGLD PNNEHSELVL VLEANKVPCL GSKLTCLSQS NLQSSNNDTE IPLQNGYITP
GLIAFGNNLG IQDIPSEPST GDGTSKSGIE AVHFAKYGVH LHGKGKAFGR ARIGGATKAV
TPPHGSGVLQ GVSVGIRTGP GETLLDGGVW RDEVALHFSI GQGAKVGSGI ETIRRVLEQG
NKGEGDDVFI RAANESLPVV VQAYNPDDIA QLILIKRDFP RVNLVIYGGH GAALLAKPLA
DADIPVILTG NRGAPDTWEK KDTLPGPPLS DSPAKILLDA GVLLGLAAKD DSKIHGLARE
ARWAGKFAGL DDTEAIRLVS TNFDEILGLS SKAEGDGEGY KGDFVLWEGN PLSGEGSVVI
SVKEDGSISD CWPEVD
//
