ID   A0A0J8UBB5_COCIT        Unreviewed;       874 AA.
AC   A0A0J8UBB5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=FLU1-I {ECO:0000313|EMBL:KMU84398.1};
GN   ORFNames=CIHG_02183 {ECO:0000313|EMBL:KMU84398.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU84398.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; DS016985; KMU84398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8UBB5; -.
DR   STRING; 396776.A0A0J8UBB5; -.
DR   VEuPathDB; FungiDB:CIHG_02183; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   Proteomes; UP000054563; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR   Pfam; PF04909; Amidohydro_2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT   DOMAIN          551..874
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   874 AA;  98434 MW;  FA28B103ECBE247F CRC64;
     MADLQDLRYL IYSHPIIDNH AHNILRKDTA TDYARYPLEA VTSEAQGEAL IDHATKTLAH
     HRAVNQLAGL YGCEPEWESI KAARQKIVEN EYNGLVKRCL EGTHTLLIDD GLTDGREVEV
     FSWHDAFTSS PTKTLVRIEA VAAKQMEKHV QDLRNRVPPI TIQTVQIDHF FSYPDFREGF
     VKAIQDSLDD PNVAGFKSVI CYRTGLKDIK WPSQGELQTS FFRILSATLE NGESRICDKP
     LNDWILRMTL RCIQRKWAGT GSKKPIQFHT GLGDTDIDLS LSNPAHLQSL IEEFRDVDFV
     LLHSSYPYTR EAGYLASMYS NAYLDIGEVF PMISRDGQLS ILRQSLELVP TCKILWSTDG
     HFHPETYLLA NKQFREIMDT VLVECVEKQD FTFSQAMDAA KNIMFNNSNL LYKLNQTPKF
     SLSDTAQCNS GSLVTSKKAS SILDTFLRSN PHVEFIWAIF IDYTATIRVR MFSIREFMKL
     AGGKRRAGIT LAVFNILQTD AIVPPHPLIA GQFYLKPDLD TLSVNIGLSS NSATVMTFWE
     TEDGGPQDGC PRLTLENIVN RCETQFNLKL LCGFEVEVVF MEKSTSDEGL TVYKPWLMNH
     SWSNMTSDTR RALPLIEEIV RELAQIDIHV EQFHAESSPG QFEFILPPDS PLAAVDTLLK
     ARQTIVHLAE RHGLRATLYP RPYSSAAGTA AHVHISINPP TKQASFLAGL LNHLPAILPF
     TFPQDASYER VKEGIWAGGV WVAWGRQNRE TPVRAIRGGH WEIKSMDGLA NPYLGVAAII
     AGGYLGMRSE LELKMEDCSV DTASLSLAQR EALGIQARMP TSLDQALAAL EADTDLQSIL
     GKWFEKYIGV RRGEHNMLSK MGKKERKTWL IERY
//