ID A0A395SNS5_FUSSP Unreviewed; 505 AA.
AC A0A395SNS5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=5-methylthioadenosine s-adenosylhomocysteine deaminase {ECO:0000313|EMBL:RGP74108.1};
GN ORFNames=FSPOR_1803 {ECO:0000313|EMBL:RGP74108.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP74108.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP74108.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP74108.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(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:RGP74108.1}.
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DR EMBL; PXOF01000023; RGP74108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SNS5; -.
DR STRING; 5514.A0A395SNS5; -.
DR Proteomes; UP000266152; 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; 1.
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; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 68..434
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 505 AA; 55040 MW; 360B4491EE4880B3 CRC64;
MPSSSARNGV SSTRRLLLRG GTVLIHDAED NVEALAKDIL IENNRIVKIA SNIEDVADAE
LIDCNLKIIS PGFIDTHHHL WQTQLKGRHA NELLLDYMAS GNLQSSNYTK ADIYWGQLGG
CLEAINAGTT TVLDHSHVNT FPGAAQTAIS ATVSSGLRGV YGYCPTARVA SYLPFEMNQE
MIASWTLEEL TMLGTQAPFG DGRVNMGLAF DLWFLPEPVV QELFQTARKA GINLATTHAV
RNHQLSMSDV IQQVKSQGLL DDRMLFSHAN GYPAESIQDL VDAGAHISST PSTEMQMALG
NPICLDDDYP MAQAQSSLGI DCHSNQASSI VYEMRLGLQA SRAKRNQRYI DQESAPRHIS
KTAQDAFNLG TIQGARAIGM QGQLGSIAEG KLADLVIFDA NTPELLCAAE QDPLAAIVLH
SSIGNIDTVI IDGIVRKRGG KLVDVEAEPE LRGITGKDLL SWSDVAKAMR TSRVEILERE
KKQDFAELKQ GVMRSLFVDE SKLRD
//
