ID A0A366SCK3_9HYPO Unreviewed; 1005 AA.
AC A0A366SCK3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=FIESC28_00546 {ECO:0000313|EMBL:RBR26638.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR26638.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR26638.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR26638.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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:RBR26638.1}.
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DR EMBL; QKXC01000013; RBR26638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366SCK3; -.
DR OrthoDB; 20951at2759; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000253153; Unassembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd01319; AMPD; 1.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 112512 MW; ED430DF87B0C62EC CRC64;
MPETGKSADQ ANVTGAPIFE ESESTALDVR ARESDEEVDE TRDAGATGHG ASHKEAASDA
GSQVGDDAEE LEDGMLLRDL PKRTTFYDPV AERQMSQTDA KYFYHRNKAD VRSGGGAGNQ
SIPQSPFLAS GSRPATEYGA DSLILDSSGR RVDSLPPGLE MPNPAIDSSG FTQSPTKVET
QHAPFPSNDS SAIPHASQVA QDPRLPDGSS NGLPSGGLFD TEPHITSELS AISKNIQRIL
DLRRKYIALS HQGPDDNPRD GPDWEIYPPP PEPAWQQASR QATNAAEHVP GQENTGANGA
KTGTESASKD APQDHHESKR STRRRKPGQD IGEDFDMADV LPLPGTDGRS YKLDDSGVYQ
VFENDDAHAP AIKVPTIREF YMDLDDILDV SSDGPSKSFA FRRLQYLEGK FNLYVLLNEY
QETADSKKVP HRDFYNVRKV DTHVHHSACM NQKHLLRFIK SKMKKFPNEV VLFRDGRHLT
LAEVFASINL TAYDLSIDTL DMHAHTDSFH RFDKFNLKYN PVGESRLRTI FLKTDNFIHG
RYLAEITKEV ISDLESSKYQ MVEWRISIYG KSIDEWDKLA AWVVDNKLFS HNVRWLIQIP
RLYDVYKASG LMETFEQVVK NVFQPLFEVT KDPSSHPKLH IFLQRVIGFD SVDDESKVER
RLFKKFPVPK VWDTKQNPPY SYWIYYLYSN LVSLNYWRRK RGFNTLVLRP HCGEAGDSEH
LAVAALCCHS ISHGLLLRKV PLLQYIFYLD QIGIAMSPLS NNALFLAYER NPFHHYFKRG
LNVSLSTDDP LQFAFTKEPL IEEYAVAAQI YKLNSVDMCE LAKNSVKQSG YELAIKEHWL
GRGCNKPGKE GNAMVKTNVP DRREEFRYFT LMQERDVLSK YVTYNAASEP SAQTGGNENK
MSESVASMTS QAAATGLSTG KEPANPEMSP PAGHQITKVA SQIGLSASRD QVWPSDAMAD
HHLSGSDPRM FPGIFTRGHR TGSMRNLAQA GDDRDIADDV FGPET
//
