ID   D2W397_NAEGR            Unreviewed;      1089 AA.
AC   D2W397;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC36477.1};
GN   ORFNames=NAEGRDRAFT_82220 {ECO:0000313|EMBL:EFC36477.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC36477.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC36477.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; GG738930; EFC36477.1; -; Genomic_DNA.
DR   RefSeq; XP_002669221.1; XM_002669175.1.
DR   AlphaFoldDB; D2W397; -.
DR   STRING; 5762.D2W397; -.
DR   EnsemblProtists; EFC36477; EFC36477; NAEGRDRAFT_82220.
DR   GeneID; 8862711; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_82220; -.
DR   eggNOG; ENOG502SUEM; Eukaryota.
DR   InParanoid; D2W397; -.
DR   OrthoDB; 5478504at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR12631; ALPHA-L-IDURONIDASE; 1.
DR   PANTHER; PTHR12631:SF10; GLYCO_HYDRO_42 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00989; PAS; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          543..589
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          48..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  120571 MW;  DADF98702363987B CRC64;
     MTNYDDDDDD KALQEFLAKK KTANLHSPSS NFNHQSSRNI FASFDASALS KSTSPKKPLT
     SPTKQNNKDD EDEDEKALQE FLQAKKSKPS PGAFNTQSSR NVLVGFSPVK PKVPTRIPNN
     DGVGGSDFLA PFTITETPAS ARKEKEDEDQ KALNEFMSKK QSMYEVSSKN TASSRNIFEG
     LDTSAMLKVG VSSSLRVAPK LTRENSTISQ KPRGMLRREG SSLLTNNDGT LSRPPPLLRG
     NSTMTTAPSA PRRGMLQREN SSFITRKNNE YELSDKPLSD VPTKRGPLQR ENSLMMREGS
     QSVPRARPPL ERGMSRNDQG YKQSINQRFL SKMKTKNEGF DDFPDTVSEV SVMSVRSTET
     ALLSDREINE EVGFTHQVEF VQLNHLVSQF MTCGFPVLVF DKLGSIEYLN KEAEDLFGVF
     SFSALGEHVS ELFLDDASVE LHQAIYEFLG PTENSTLKAD KIGSDQNYLD DIRPYNQISE
     EEKLERRRAL SQLRTLRAKA TTIKQFFSVS AKIIPISKLQ ETHFCIYMRF AQQAENGKYS
     QMTNSLNQAV TEMITIPVIT INDKGIIQVF NKAASSTFGF EAKEVVGRNV KIICNKKDRL
     KHDSYLEKCK TKDKNTLNMV KKVKGETKSG KIISVEIRVS HILKDGKSSY IAYIRDYKSL
     CCQAGGFSWI RMDLFWSSVE TTKQVYNFAS YDTLLTALKL RGLKALFILT YSNTLYTGSA
     STPPTTDIAI EAFANYSRAA AKHYANENVI FEVYNEADLQ GFTPVTYAAL SKAAVAAIRE
     GNPNAQVSTT GVAGFSYTFV RGFTSEGGAA SKNGSQLFSG IGLHPYGVGS PKSPFGRFPD
     LTRKFRSIIN DNINATLQGK ASTLTSAQKS LISTVPPVWD TEWGLTATDF DSNSNGLDEA
     ALRLHANNVV GRLLSSCAVG FPIYIYYDLR NDGVDPTNRE HNFGLLFNNY TDKPAMKAVK
     QLSSIVRNRL FDGYIQIEHP SVTAMRFKSS NDSVIVLLPT ETGASVNIKA NSASSVVDIF
     GRNVTVSKDN TFTVKETEGL VYVTFVTPMV TPTVSQPIIQ PANSTKVSSA EKLIGNWIIL
     ALLLILIIV
//