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Database: UniProt
Entry: A0A0L0FFQ5_9EUKA
LinkDB: A0A0L0FFQ5_9EUKA
Original site: A0A0L0FFQ5_9EUKA 
ID   A0A0L0FFQ5_9EUKA        Unreviewed;      1107 AA.
AC   A0A0L0FFQ5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SARC_11877 {ECO:0000313|EMBL:KNC75602.1};
OS   Sphaeroforma arctica JP610.
OC   Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX   NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC75602.1, ECO:0000313|Proteomes:UP000054560};
RN   [1] {ECO:0000313|EMBL:KNC75602.1, ECO:0000313|Proteomes:UP000054560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP610 {ECO:0000313|EMBL:KNC75602.1,
RC   ECO:0000313|Proteomes:UP000054560};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA   King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Sphaeroforma arctica JP610.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KQ243527; KNC75602.1; -; Genomic_DNA.
DR   RefSeq; XP_014149504.1; XM_014294029.1.
DR   AlphaFoldDB; A0A0L0FFQ5; -.
DR   STRING; 667725.A0A0L0FFQ5; -.
DR   EnsemblProtists; KNC75602; KNC75602; SARC_11877.
DR   GeneID; 25912381; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   OrthoDB; 101939at2759; -.
DR   Proteomes; UP000054560; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 4.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 5.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 7.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 8.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000054560}.
FT   DOMAIN          218..410
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          412..451
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          453..490
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          492..528
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          529..566
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          568..608
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          613..641
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          646..688
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          691..727
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        441..450
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        518..527
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        537..554
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        556..565
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        598..607
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        631..640
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        659..676
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        678..687
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        717..726
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1107 AA;  119385 MW;  32E8466AFDD0390E CRC64;
     MRVLQSATIS ALAMSRALGN VYDYDSNHVG SILNGYVTKD ISNDNRMIVE AELLGEVLSL
     ELEPRSVLAP DFELHIISEG MTKIRKHREN IVQYTYSISS AQNQNLNGMA TLSADGSIVD
     VLLNTKRRLL SGRRSGDGTI IFYDTSSQIE LQGNLNRQVG EDRKRARAER RNIKFAPVTK
     SANRVKEQLI EKPAGQVGDF GHHLNVLHRT LRQEEPLKQI DLVLDFDYDL FFALGSDEEV
     CQQKALSLVA AVNVIYESQL GLTHSLKSVN VRSVPNYSAS ERQSLLFEVE DQWQPLEPSR
     EYGALVLVTG KVFADGVLNA EANSVCQDLW KYGLASMMDS PTVASAIDTQ ALRLAHTLGH
     MWGAASHVAE SGFVMSTTEI ADQASFKDTS IADINAYIAE YGPLCLTEVQ PEVGPCSVSP
     CLNDGTCLDD PGAALGYRCE CGGGFAGANC DEVGNSCSSK PCKNGGVCTP TESEFSCTCA
     FTGFTGPTCE VDVDECASQN PCKNGECVNE EGTFSCTCDA GFSGRLCDSV ACVSGRCKNG
     GTCTPSTVAP YYACECASGF SGTVCSTNVN DCRNPALNLC DAEHSTCKDE VNGVSCICDA
     GYLPPYCIEY SCPCVNDGVC VKSGENTVCK CPAGHWGPNC QNTPSASNKC LVDGVKDACN
     GNGNCKETDN EQGFLCECVE NWEGTTCNKS TVDYCALRPC QFAGTCLSLD TGHRCYCLPG
     RGGDNCELDM KECDSNPCQN GGACVEKHNR ELGVNLMGKR VCIMGAGAIG GLLGVKLAVS
     GNQVTFVARG AHLKAMSENG FTLAMADGTI HNTKDLDCQY TDDLSTIHQE QDVIIICLKG
     HQIQNMLTDM NNSRILGEST MFVTTQNGIP WWLFQCCPEG SEICKYENTV VRAVDPDGSL
     FNGIDPKRII GCVSYPAARV SKHGTVEHLE SIRFPVGELN GSIDSARIKM LSNLLIAAGF
     KSPILPDIRS EIWLKLYGSV AFNPISALTH STLKEMCEYA STRQLIELVM GEIEEVGGRL
     GLTLRVSKDR RIGGAIAVGE HKTSMLMDVE NGKPMEIDGL VGSVVELAEL TGSDIPHTRT
     IFCLVNMLGY IIAKHSVAFP EQQLGTE
//
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