GTAA_ARTBC
ID GTAA_ARTBC Reviewed; 862 AA.
AC D4AMT2; D4AMT3;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Probable glutaminase ARB_05535/05536 {ECO:0000305};
DE EC=3.5.1.2 {ECO:0000250|UniProtKB:Q2U4L7};
DE Flags: Precursor;
GN ORFNames=ARB_05535/05536;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Glutaminase catalyzes the hydrolysis of glutamine to glutamic
CC acid and plays a key role in nitrogen metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q2U4L7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q2U4L7};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the fungal glutaminase gtaA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE35493.1; Type=Erroneous gene model prediction; Note=The predicted genes ARB_05535 and ARB_05536 have been merged into 1 gene: ARB_05535/05536.; Evidence={ECO:0000305};
CC Sequence=EFE35494.1; Type=Erroneous gene model prediction; Note=The predicted genes ARB_05535 and ARB_05536 have been merged into 1 gene: ARB_05535/05536.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000003; EFE35493.1; ALT_SEQ; Genomic_DNA.
DR EMBL; ABSU01000003; EFE35494.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003016138.1; XM_003016092.1.
DR RefSeq; XP_003016139.1; XM_003016093.1.
DR AlphaFoldDB; D4AMT2; -.
DR EnsemblFungi; EFE35493; EFE35493; ARB_05535.
DR EnsemblFungi; EFE35494; EFE35494; ARB_05536.
DR GeneID; 9524127; -.
DR GeneID; 9524128; -.
DR KEGG; abe:ARB_05535; -.
DR KEGG; abe:ARB_05536; -.
DR eggNOG; ENOG502QPQS; Eukaryota.
DR HOGENOM; CLU_008020_1_1_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR InterPro; IPR014870; DUF1793.
DR InterPro; IPR032514; DUF4965.
DR InterPro; IPR033433; DUF5127.
DR Pfam; PF08760; DUF1793; 1.
DR Pfam; PF16335; DUF4965; 2.
DR Pfam; PF17168; DUF5127; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..862
FT /note="Probable glutaminase ARB_05535/05536"
FT /id="PRO_0000434907"
FT REGION 798..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 862 AA; 97132 MW; CEBD87D448BD3963 CRC64;
MLSWVLLAWA VACSALAGAS RLTPSVLPLV VRNPYLSTWL ADARHEPWSS WPIFWTGQHM
GMSIMAHVPS TGNTYPLLGR PHDSLGPNNP NNGCFLGSKY DASTTNMTYL IQPEGKHLAG
ESVKITITFL SPITPTSTLR QSIPAGYVTI RVEGNMNVNI YMDMNGEWVT GDRGSSLIWK
MDNIVDTGKG ESLYQWQVSR KTEQLFTEFQ DRAEWGMLHF LAPQGVRYES GTSMLLRTRF
ARTGVLQNRN DERFRTVMDE EPVFAYSKAF NLNGTDDEPN IEAIHDEVTF TIAHTQDPVV
QFASARGLTL MKPLWESYFP DVKSLLNFHY FDLDKARILA HRYSNQLARD AQLSAAEDYV
DVVALTARQV LGATSFSGTS DNPLLFLKEI SSNGNCQTVD VIFPSFPFFL YTNPRWLAYL
LEPLIEHMLS GQYPNNYSMH DLGAHFPNMT GHPDGKDEYM PVEECGNMLI MGLSIVNSLR
FPPEANTTAP WYPGTLEARD AEPDVVGLFP LRDLQTVGGI DRLDSVWGVG PDATNLARKW
VEKSYRLWRQ WTGYLVEFSL EPHNQLSTDD FAGWLALQTN LALKGIVGIN AMSEMSRFVG
KTDDYKYFKN ISDTYITKWE GFGFSRDGTH AKLSYDWYGS WTTLYNMFAD ALLCFHLDGT
EYDTHPRTLD DQEPIAPPPG KTGFIPRRVY EKQSKWYANV RQKYGLPLDS RHLYTKSDWE
FFSMAVSSPS VRSEILQSYA KWVNETSTDH PLTDLYKTEE DGGYPGPNFF ARPVVGGHFA
FLALEKACNG KATDGLKFLD DKDNNSPEDI PEDNVHDGDA DNEDSQSPIQ DSDGSEVKAG
DQAQFPIQDM DDSQMTIVNE ND
