ID A0A1S3HQU0_LINUN Unreviewed; 507 AA.
AC A0A1S3HQU0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cytokine-like nuclear factor N-PAC {ECO:0000256|ARBA:ARBA00034140};
DE AltName: Full=Glyoxylate reductase 1 homolog {ECO:0000256|ARBA:ARBA00030287};
GN Name=LOC106156613 {ECO:0000313|RefSeq:XP_013387404.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013387404.1};
RN [1] {ECO:0000313|RefSeq:XP_013387404.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013387404.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000256|ARBA:ARBA00007598}.
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DR RefSeq; XP_013387404.1; XM_013531950.1.
DR AlphaFoldDB; A0A1S3HQU0; -.
DR EnsemblMetazoa; XM_013531950.1; XP_013387404.1; LOC106156613.
DR GeneID; 106156613; -.
DR OrthoDB; 103196at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05836; PWWP_GLYR1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR035501; GLYR1_PWWP.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000313; PWWP_dom.
DR PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 7..66
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 94..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 55288 MW; EB44945596DABBB9 CRC64;
MASKFRVGDL VWAKMKGFPA WPGKVIEPKP EVKRPSNKKP MHFIFFYGSE NYAWVFEENT
FLYATNKDKF MPASRIPKGF KEAVEAIDEA LEAMPTQHER RSPSPVLVDG EEPPVETAAD
DAETPEGATE QKMPRVRKPT QKFAESVESG EMTAKNATAR KKNELVKKAI KHATASQSGP
SPKKIKLGTP RKSPKKPRMP SVRIPSELTT RKPQKNIIPT PCKIGFLGLG IMGSGMVRNL
LKSGHEVTVW NRTIEKCKDF AALGALPGET PCDVVQSCDI IFSSVANPAA LKDLVFGNCG
VLQGISPGKS FVDMSSVDVE TITDINEAIT MRNGRFLEAP VFGSKEASED GQLVVLAAGD
RDLYDDCLSC FEAIGRKTYY LGEIGNGARM RLVLSMVLGT VIAGLSEGMA LAGKVGLHQE
DLLEILSLSS LNCSLFRSKG YAMMENSYNP RALLQNQQKD MRLSLNLGDE VDQPLAVAAA
ANEMYKKAKA RGYGTSDVAA VFRAADI
//
