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Database: UniProt
Entry: A0A3L8S4K5_CHLGU
LinkDB: A0A3L8S4K5_CHLGU
Original site: A0A3L8S4K5_CHLGU 
ID   A0A3L8S4K5_CHLGU        Unreviewed;       725 AA.
AC   A0A3L8S4K5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=DV515_00012056 {ECO:0000313|EMBL:RLV97148.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV97148.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV97148.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV97148.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV97148.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(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:RLV97148.1}.
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DR   EMBL; QUSF01000061; RLV97148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8S4K5; -.
DR   STRING; 44316.ENSEGOP00005019168; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0047730; F:carnosine synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0035499; P:carnosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR031046; CARNS1.
DR   PANTHER; PTHR48066; CARNOSINE SYNTHASE 1; 1.
DR   PANTHER; PTHR48066:SF1; CARNOSINE SYNTHASE 1; 1.
DR   Pfam; PF15632; ATPgrasp_Ter; 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|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT   DOMAIN          416..617
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   725 AA;  77629 MW;  90B1B2E34264A3C9 CRC64;
     MPSETSPGAW SLLLSRGVSF KVGGHSALET FEPPRRANYV TGTFAPGDPE GGWVGELARD
     LDCPTGGSVP LAHRLEDTLV TRWVLAARAN LPVPPTLAFV LGARGDLPAE PAAPGVRLVR
     LEDPQGQQSL VQEEVGAFLG GTAMEPYSQV ACTVGRAESP VRHGAALPQG LDSSLQQWGV
     VGPSQRQALA TRLRKATEAA AAALLATEAE LSPRQRGGSR AHTDILGVDF LLACVDDALE
     LVALATNGQR CLETCELAEA MGHGVGEPRG DLPHLLAEAM LHRAQCHLVE GKDILLIGAG
     GVSKSFVWEA ARDYGLRIHL VESDPEHFAA GLVQTFLPYD SREHRRDEEH AERVLELLRS
     RGLQPHACLS YWDDCVVLAA LVCQGLGLRG PAPAAVRVAK QKSRTHWHLQ RCRRGRPPPA
     AFAVPCRRLR SHGDVERAAG AVPFPAVAKL EFGAGGVGVR LVENAGQCHA HAARLWRDLR
     DDADHPGIGL GWGNAMLLME YVPGTEHDVD LVVFEGRLLG AWVSDNGPTR VPAFLETAAC
     LPSCLPADRQ AQLVRAALEC CRACGLRDGV FNVELKLGPA GPRLLEINPR MGGFYLRDWI
     REVYGPDLLL AAVLVALGVP PVLPARPAPR THLAGVMCLG SEHGETLAGG GGMEALRELH
     DRGLVRLNRL FEEPEGAGEY EEPLLSVACA GATLAEACER LLGLCQGLGI DSPRYPVEHF
     LSHFK
//
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