ID   A0A091P1Q1_HALAL        Unreviewed;       702 AA.
AC   A0A091P1Q1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Aspartyl/asparaginyl beta-hydroxylase {ECO:0000313|EMBL:KFQ00279.1};
DE   Flags: Fragment;
GN   ORFNames=N329_04750 {ECO:0000313|EMBL:KFQ00279.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ00279.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ00279.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ00279.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC       family. {ECO:0000256|ARBA:ARBA00007730}.
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; KK648283; KFQ00279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P1Q1; -.
DR   Proteomes; UP000054379; 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; 2.
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; PF13174; TPR_6; 1.
DR   Pfam; PF13181; TPR_8; 1.
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:UP000054379};
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..89
FT                   /note="Aspartyl beta-hydroxylase/Triadin"
FT                   /evidence="ECO:0000259|Pfam:PF05279"
FT   REPEAT          398..431
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          535..689
FT                   /note="Aspartyl/asparaginy/proline hydroxylase"
FT                   /evidence="ECO:0000259|Pfam:PF05118"
FT   REGION          147..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ00279.1"
FT   NON_TER         702
FT                   /evidence="ECO:0000313|EMBL:KFQ00279.1"
SQ   SEQUENCE   702 AA;  80804 MW;  D60BD9640825F0A0 CRC64;
     ETKHGGSKNG KKEGLSGSSF FTWFMVIALL GVWTSVAVVW FELVDYEEVL AKAKDFRYNL
     SEVLQGKLGI YDADGDGDFD VEDAKVLLGE YQHWWNNPYN SVVILIRLFG LAEDLLYPVL
     ENFVMFIEHH RYVHNLFPFC NKSGLKERSV PAQPTSPESE ETVQPAEKSY VESELEEEIQ
     SVLQEALHSQ PVSYEHDMDV EKTVSDPEAP GDSDLMLEDA MEHYTEPKHE KKTETQDTGR
     KVRLTKELHV YPNKKTSKVK VYRFFSLVAK KKKKPKLLNK FDKTIKAELD AAEKLRKKGK
     VEDALRAFEA LVNQYPQSPR ARYGKAQSED DLAEKMRSNE MLQKAINTYD EVVSLPNVPS
     DLIKLSLKRE ADRQQFLGRM RGSLVTLQKL VHLFPSDTSF KNDLGVGYLL IGDNSNAKKV
     YEEVLSLAPN DGFAKVHYGF ILKAENKIAE SIPYLKEGLE SGDPGTNDGR FYFHLGDALQ
     RMGDKEAYKW YELGYQRGHF ASVWQRSLYN VKGLKAQPWW TARETGYTEL VKSLEKNWKL
     IRDEGLAVMD KKRSLFLPED ENLREKGDWS QFTLWQQGRK NENACKSVPK TCALLERFPE
     ATGCRRGQIK YSIMHPGTHV WPHTGPTNCR LRMHLGLVIP KEGCRIRCAQ ENRTWEEGKV
     LIFDDSFEHE VWQDAENYRL IFIVDVWHPE LTAQQRRTLP AI
//