ID A0A3F3QKR3_9EURO Unreviewed; 671 AA.
AC A0A3F3QKR3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 02-APR-2025, entry version 17.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=BDQ94DRAFT_165164 {ECO:0000313|EMBL:RDH39452.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH39452.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH39452.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH39452.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852032; RDH39452.1; -; Genomic_DNA.
DR RefSeq; XP_026632474.1; XM_026770221.1.
DR AlphaFoldDB; A0A3F3QKR3; -.
DR STRING; 1341132.A0A3F3QKR3; -.
DR GeneID; 38138577; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR052032; ATP-dep_AA_Ligase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR041472; BL00235/CARNS1_N.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR Pfam; PF18130; ATPgrasp_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 327..563
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 671 AA; 75061 MW; 47C5E04E370C6144 CRC64;
MAYSCFLALT TQDQIDHFTC EWNKTDPVKG FVGQRHESVN LTLYPTKTIV TKTYNNKVAA
SAACFDGYQN GDDKEFCTPW NLTPEITSFI TTTIFERNKG ADNKSPVIMK FILSRVDGYL
ARSDFLEQRL DGVKHIAKVV GLLRPLQQVT TAQVQIDGTA HDLSTLLSMS VGAVLLETGS
GSDLHDTLQS VEEALCNRIS YPWVVPTSIV PKRLAWVEGR KDADTSRRMY EAAAALGISL
VIIDKPGHWL QNDNGPYAHL REGFVAANID VDEGFVDRIV TAVRSYDKPI DGLMTVSDSR
MIGVARACEI LGYSTSPSSA YILAGDKYRT RMMEPDTHGA FRVFGTDELD KVLRSTEEVS
YPLIVKPCLG WGSQAVTKVS TEDELFQAVE KACDCHALGP QKRSDAVIEP YIDGPEVDAN
FILLNGEVIF CEISDDFPSP GDLDAQQSHN FVETMVHIPS ALPPHELKAI RNALHQSILR
QGFLTGTFHC EARLQYSSHE FRKDSENGVE NLYPRQGKTN DGKKSVRVYL LEINARPAGY
LETVGVNLVY GVDYFAQQML FAVNEELRYR ALCHPFLNGP RYNLSVLVLQ EDVAGIMKTE
DATAELLHQY PELKPHVPLY ATIKKKGDRL VGPKSSEVHF IAWMLVTAEK RRDCLRLVER
IRSNFRYEVE S
//
