ID A0A1S3NIU2_SALSA Unreviewed; 686 AA.
AC A0A1S3NIU2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Aspartyl/asparaginyl beta-hydroxylase-like isoform X5 {ECO:0000313|RefSeq:XP_014015106.1};
GN Name=LOC106579584 {ECO:0000313|RefSeq:XP_014015106.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014015106.1};
RN [1] {ECO:0000313|RefSeq:XP_014015106.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014015106.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000256|ARBA:ARBA00007730}.
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DR RefSeq; XP_014015106.1; XM_014159631.1.
DR AlphaFoldDB; A0A1S3NIU2; -.
DR Ensembl; ENSSSAT00000054115; ENSSSAP00000029210; ENSSSAG00000019881.
DR GeneID; 106579584; -.
DR OrthoDB; 37221at2759; -.
DR Proteomes; UP000087266; Chromosome ssa19.
DR Bgee; ENSSSAG00000019881; Expressed in liver and 14 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR039038; ASPH.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12366:SF29; ASPARTYL BETA-HYDROXYLASE, ISOFORM L; 1.
DR PANTHER; PTHR12366; ASPARTYL/ASPARAGINYL BETA-HYDROXYLASE; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..98
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT DOMAIN 519..673
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 111..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 77181 MW; FBDE1C698A349AF1 CRC64;
MAPRKNFRNQ AKKEVKPAAV VNKNGVKAEA TVAASGGGFS GTKIFTWFMV LALLGVWSSV
AVVWFDLVDY DNVIGKLSAY DADGDGDFDV EDAKVLLGLK ERPVSVLLRE AKEESAVKEP
DAVPPPDDDV DGSQNTDVES EIQAAVPLPP ISDDFIPDDS RDEATHPYED ENNAIDTKGE
LVEKAQPQQT VEESKQYNDQ PGSLETKETV QLRYNAEAES VPEPEADVEP EVESVPELKE
NAEDQPKDKL QEKPKKKKPK LLNKFEKTIK MEIDAAEKLR KKGKVEEAVR AFETLVLQYP
QSPRCRYGKA LAEDGLAEKM LSNDMLQKAI GTYKEASELP NATPDLIKAT LKKRAERQQF
LGRMRGALAT LEKLVQIFPE DVALKNDLGV AHLLIGDNKG AKRIYEEVLA TAPSDGFAKV
HYGFILKSEN KIAESIPFLR DGLESGHPGT DDGRFYFHLG DALQRMGDDS AYKWYERGHL
RGHFASVWQR SLYNVDGLKA QPWWTPKDTG YMDLVKTLER NWRIIRDEAQ SVMDKTTGLF
VPEEENLREK GEWGQFTLWQ QGKKAGEACR SVPKTCGLLE RYPEATGCKR GQIKFSVMQP
GTHVWPHTGP TNCRLRMHLG LVIPKTGCKI RCTNDTRAWE EGKVLIFDDS FEHEVWQDAD
SYRLIFIVDV WHPELTQYQR QTLSSI
//
