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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//