ID R0M159_ANAPL Unreviewed; 726 AA.
AC R0M159;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Aspartyl/asparaginyl beta-hydroxylase {ECO:0000313|EMBL:EOB06383.1};
DE Flags: Fragment;
GN ORFNames=Anapl_13714 {ECO:0000313|EMBL:EOB06383.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB06383.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000256|ARBA:ARBA00007730}.
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DR EMBL; KB742618; EOB06383.1; -; Genomic_DNA.
DR AlphaFoldDB; R0M159; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
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; ASPARTYL/ASPARAGINYL BETA-HYDROXYLASE; 1.
DR PANTHER; PTHR12366:SF33; 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; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 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:UP000296049};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..74
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REPEAT 422..455
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 559..713
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 77..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB06383.1"
FT NON_TER 726
FT /evidence="ECO:0000313|EMBL:EOB06383.1"
SQ SEQUENCE 726 AA; 82985 MW; A514D3016DA212F4 CRC64;
ETKHGGSKNG KKEGLSGSSF FTWFMVIALL GVWTSVAVVW FELVDYEEVL GKLGIYDADG
DGDFDVEDAK VLLGNGLKER SVPEQSTSPE SEETIQPDEQ SFVKSEHKNV DDVELEEEIQ
PVLHEAVHSE PGVLKAEYLL VAEFTNDCVF SNNLYSQLGE GHEDVDESVN EQWQEKEETH
GETFEAPATD DLLKELENEV TEDYETPDSF QKAVEDLPEE VHEAAEQGIF CYCDLSVLVK
DADEEGEKEK NKHLIIHFYL FILTDEIIED LEIDKKMSGK GEKETEQDKT EKAKKKKKPK
LLNKFDKTIK AELDAAEKLR KKGKIEEALK AFEALVNQYP ESPRARYGKA QSEDDLAEKM
RSNEILQKAI NTYDEVVSLP NVPSDLIKLS LKREADRQQF LGRMRSSLVT LQKLVHLFPS
DTSFKNDLGV GYLLIGDNSN AKKVYEEVLR LAPNDGFAKV HYGFILKAEN KIAESIPYLK
EGLESGDPGT DDGRFYFHLG DALQRIGDKE AYKWYELGYQ RGHFASVWQR SLYNVKGLKA
QPWWTAKETG YTELVKSLEK NWKLIRDEGL AVMDKKQSLF LPEDENLREK GDWSQFTLWQ
QGRKNENACK GVPKTCALLE RFPEATGCRR GQIKYSVMHP GTHVWPHTGP TNCRLRMHLG
LVIPKEGCRI RCAQENRTWE EGKVLIFDDS FEHEVWQDAE NYRLIFIVDV WHPELSAQQR
RTLPAI
//
