ID A0A0F4YTR7_TALEM Unreviewed; 1693 AA.
AC A0A0F4YTR7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=T310_4319 {ECO:0000313|EMBL:KKA21662.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA21662.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA21662.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA21662.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:KKA21662.1}.
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DR EMBL; LASV01000175; KKA21662.1; -; Genomic_DNA.
DR RefSeq; XP_013328274.1; XM_013472820.1.
DR STRING; 1408163.A0A0F4YTR7; -.
DR GeneID; 25316667; -.
DR OrthoDB; 1355382at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR13789:SF306; HYDROXYLASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..364
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 1177..1273
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 377..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1693 AA; 185996 MW; D2EDA840349F43C1 CRC64;
MSQSKASFNI VIVGAGLGGL GAAVCLARKG HRVTVLEAAS QLAEVGAGIQ IPPNSTRILD
AYGLTSQFEK KVVWPKNITF RRYATGADIG STPLHPDMTE KYGYPYWLIH RADYQAILYE
AAKEAGATVL LGTPVDRVDA RAPAVILQDG RRMTADLIVG ADGIRSRTRR AVIPDREIEA
TDSPHCAYRA TVPASLMNAD AEVKHLMTDV NANCWIGPDR HIMAYPIRQG AMYNMVLCHP
GKASVGRWNE PGDLDEMKAH YASFDPVMRK VLTKVSGCLK WKLADLPPLT TWVSRSGKVV
LIGDAAHAML PFLAQMLKTR KGAAMAIEDG AALGECLDRA ATKRDLPRVL QAFQTIRKPR
CERVQLGSRA NGDIWHLHDG KEQEQRDRAM KQRAAQREDG SSNPNQWSDE DFQPWLFGHD
VFAYRPVYPC LPVAPRGFRC PSSDALQARA PRRADMARLK NGVHSWEDVL AQRYQSNKPS
ALPRYRKRTV VGRGPVPKGL DISIEPKCQP GCPLLSKLAP EIRLMIWEYV LGGLRLHIIQ
RSQRRLGYVV CPQHDACEIC RGGLHQPVKD GEHLSDWSLL SLPITCKQIY CETIHILYAS
NVFEFSNTWS LTYLRPTIPQ DQWNDIRVLD LKWAFPGHWL PSKDSVKSVY VWAGRQQWID
TCNAILRMKG LEDFTLHLTS NWFGEPVEKI PIFLAPLREL RLRRRWKILL PPQPYYKNEI
SRLNTMLQKE GIDLQVQFGE AVFSLFVDMG SPNLPEIRPR RSYRLRPGRL LLPAAIVLGF
VLLILYPPRL AHYIVEFRSS DSTLLQSQWD ALDAGLRRCA ELTAPSPVYS LPPPADRSNP
RWNPISGQNK TVVLRNATLF DGDAILPEPV DIVFDKGVVR SISSTGARDY ATSSDPDISV
FELDGRFVTP GLVDMHSHHL VGAWPDLKGY QDINEVNDAT GPLTPFVRAL DSIKPYDVAA
TIIASGGVTS SLILPGSANI IGGEAVIVKN LLRSGENGEE TVEELLLEHG IPKENRRRYM
KMACGENPRR VYHHTRMGNA WIFRHHLARA KDLRDRQDAW CASAAAARRS GDSATAAALL
AVGPDGKGGL PEELELDSTV AILRGKIGVN IHCYEQEDFE DMLLHSEEFG FRIQAFHHAL
SAWKVPELIK SSGQNITIAT FADFSLYKKE GYDASLRAGK ILAEHGVPVA YKSDHFEENT
NAKYLLSQAA TAHSFGLPEI KALQSVTSVP ARALEVHHRI GFVKPGYDAD IVVWDSHPLS
VGATPLQVYI DGKATLEAVD LRKNKDDSVK RVQEKPKMRA ETPARDIKEF CSRSPTGSEN
IVITGISNSY LQLPHVKASG NNLTMVISSG KITCLGGHEE CVTSMSDADV ISLQDGYVLP
GLTAISTTLG LTEIESEDST SDGRGNPDAD PLDPDNAIYA KYGVHTEGRA FQRAQIGGVT
RAITAPVGRS FLGGVSVGIK TSEGSNPING GIFKDDVALH FVVGQDVKGS SHTPTVSSSI
AKLRKILDNN RGKDSLFGKA ADGKLPVVVH ADNKVKNDYA KVRLVIFGGA EAPAVADELA
ASGVPVIFNA VHSAPTAWEK KDVLVGPPLT PSPVRVLADA NVTFALALPY DTDWHLHNLG
IEASWAAKDA GLSPQHAVDL VSGKIDAILG LSGRESNRDY VIYEGNPLEY GANVVLAIDG
DDGTVRSCWP EAD
//
