ID A0A084Q9Z6_STAC4 Unreviewed; 522 AA.
AC A0A084Q9Z6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=S40285_06330 {ECO:0000313|EMBL:KFA60781.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60781.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA60781.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60781.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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DR EMBL; KL660890; KFA60781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084Q9Z6; -.
DR STRING; 1283841.A0A084Q9Z6; -.
DR HOGENOM; CLU_548804_0_0_1; -.
DR InParanoid; A0A084Q9Z6; -.
DR OrthoDB; 5539564at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 211..420
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 46..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57825 MW; FDC521EB755F1426 CRC64;
MTCLDSLHYP LQLGRAAISW ASTIESSNID TATIADVLQQ TITPLQQSTQ PVTNTANMDY
APISPPESSD SSLPSQADPQ TAPRKPIIGI LGGGHFCRML RQSAKGLPVE LVILDRPGCP
AKRGVSSSTP DNFDGSHETE AWVRELAAKV DIITVKHEHV NSKVLREIEK NGVAITVDGK
SRMKKVEVHP SPDTISITQD KYALKSHLTE HGFYSRDEIQ TLILSMGQLS TAVEAMSSYW
GYPLFLKSQR PSLYNSSSFK IKNKEDIDKA LAALRGQPRY LEKWLPVAKE LAVSVERTTY
DSEGLTYGSH VVETVYEDGI CTQVFNPARI ALDLRARALV LACNVVETFT GRGLYTVKMF
VLENGNHVSG LWTFDALPRA LNQFRAHLCL VANVLETEPV DLNNPPPGWD ITETITLNIV
ASPSTIDLPE FAVPEGVEVI YAEYDNKPTA HERTKEPLMR RYTWGMIPGR KIGHVTFAHA
SNDMNLEEKI GESIELANKI RREAVQALSE GNEKPRVRFG KH
//
