ID A0A1I8IC80_9PLAT Unreviewed; 943 AA.
AC A0A1I8IC80;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0000313|WBParaSite:maker-uti_cns_0011433-snap-gene-0.5-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0011433-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0011433-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR AlphaFoldDB; A0A1I8IC80; -.
DR WBParaSite; maker-uti_cns_0011433-snap-gene-0.5-mRNA-1; maker-uti_cns_0011433-snap-gene-0.5-mRNA-1; maker-uti_cns_0011433-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00878; Arf_Arl; 1.
DR CDD; cd19773; Bbox2_TRIM23_C-IX_rpt1; 1.
DR CDD; cd19774; Bbox2_TRIM23_C-IX_rpt2; 1.
DR CDD; cd05301; GDH; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 322..375
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 444..490
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 407..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 101003 MW; D684BB55856EFFAC CRC64;
LQASAAAASR LRVLVTRQLP DKFTASLRRQ LQHLEIVTWP SATQPVERKF LLDEAAKIDG
LLCLLTDRVD AEFLGRVDPA RFRAVSTMSV GVDHIDVAAC RAAGVRIGYT PGVLTEGTAD
LALALLLATA RRLPAAVETV RQPGAWGPWC PFDRLCGRGI GGSTVGLVGF GRIGQAVARR
LSGFRPGRIV YTGPRPKPEL AGPLNAEYVK FEQLLAESDF VVICCPGTPD TRHLFNKEAF
KLMRPDSILI NVSRGTVVKQ SDLHEALSSG SIGAAGLNVT DPEPLPSDSP LLSLPNCVVL
PHIGSADVAT REAMAQLAAV ECRLCNEGFD MQGDLLPRLL ACGHSVCHRC LRQLPVLQHH
DGGGPGGCLL CPFDRQPTPL PEAGVWGLKK NFALLEQLER LAVSSDSAVG ASGGGDANSA
SAASGSGASS STAAASPPPQ PPSPPSVPCD ENDSHTAELH CLVCSSNLCP DCARTTHSSR
TLSQHSLVPV GQRPARIPRC RYHPMHAAEL VCLEEACWRN SLMCYICKDY GRHVGHRHAL
LESELESVRS GLSASLSSVR AFAADLNEAA RRLRACAEEI DRSETGTRAV AERQVEEYFE
VLAKRVQQQR QAARTALQAH VQQRLSCVNT QLEQLADLLN GVTSATEQLS GALALPDLEL
LAAKPELAAA ALTVAKQQAD CADTLARLAP DASVPLTFTR DHRLHIGPKL EMRAVLLGLD
GAGKTSILFR LKQNEFVSAV PTIGFNVETI ECDNVKLTYW DVGGSPKLRP LWRHYYLNTQ
CLVFVIDSCD SARLEEAFNE LTKLLQEPEL KEASFLILAN KQSSPGAITI EALMERFQLV
KLCSTRSWHI QSCDAMTGQG LPEAVDWLSH QLVAACPAAE ETADYSSHDG AVAPSADVVD
SAADRAAEAS ADGQQQQQQQ EDAIDSSNNG GGPLASPGLE SDA
//
