ID F6RBK4_XENTR Unreviewed; 1026 AA.
AC F6RBK4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Aspartate beta-hydroxylase {ECO:0000313|Ensembl:ENSXETP00000046782};
DE SubName: Full=Aspartyl/asparaginyl beta-hydroxylase isoform X4 {ECO:0000313|RefSeq:XP_031759213.1};
GN Name=asph {ECO:0000313|Ensembl:ENSXETP00000046782,
GN ECO:0000313|RefSeq:XP_031759213.1,
GN ECO:0000313|Xenbase:XB-GENE-987977};
GN Synonyms=aah {ECO:0000313|RefSeq:XP_031759213.1}, bah
GN {ECO:0000313|RefSeq:XP_031759213.1}, jctn
GN {ECO:0000313|RefSeq:XP_031759213.1}, junctin
GN {ECO:0000313|RefSeq:XP_031759213.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000046782};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000046782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000046782};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000046782}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_031759213.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031759213.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031759213.1};
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_031759213.1; XM_031903353.1.
DR DNASU; 100124792; -.
DR Ensembl; ENSXETT00000046782; ENSXETP00000046782; ENSXETG00000021644.
DR AGR; Xenbase:XB-GENE-988623; -.
DR Xenbase; XB-GENE-987977; asph.
DR eggNOG; KOG3696; Eukaryota.
DR HOGENOM; CLU_023717_0_0_1; -.
DR OrthoDB; 2884005at2759; -.
DR TreeFam; TF312799; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Bgee; ENSXETG00000021644; Expressed in skeletal muscle tissue and 13 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; 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 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:UP000008143};
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 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..92
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REPEAT 722..755
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 859..1013
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 100..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..304
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 116718 MW; 16FE2B8921AB6E1D CRC64;
MMAEDSVNGG KNGKKEGLSG SSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLAKAQDFR
YNLSEALQGK LGVYDTDGDG DFDVDDAKIL LGLKERSVLV PPAEDSEDDH PATQATAEPD
DVEEEDIQDV FQPQDEADDL DKDLEEIVQD SLHESADDLD KDLQEVVEEI HEEAVDDLGK
AFDEEVQDSP HESTDDLDQD LKEIVEDSYT EAAAADDLDK DLEEIVQESL HAEEDASETH
EEADQVAEEE AHDEEPEVEK EVEAVETANV EAVFVEEQLE LEVQDDEQAE TTEEVPETEE
ADDNTVVEEA KVEIETESDD QELDQDVKAE PEIEEIYKEE LLEEDAEEQP EPEVIEETEP
EEEREEQVAL DDNQETEHEP ETHRDEEAPS ESQVTEDLQE VIVDEHVTYE QEEEHHTEDE
PQHTEHLEVE ESQTPDEEFE PEMLEAPAVI ENEDEDSEPV EERLDEAEEE ILHLTEETIE
EEPPTASDQE EISDHPAEGH LDVADEEILH VIEDKIVKAF EQLQNPAEQA QSEPEEIQDV
LTEEILQDDK AEESLLVPEE QQETPTDEHK EVPEEKTEQP AGDASVTTDK KQKAKNKKPK
LFNKFDKTIK AELDAAEKLR KKGKVDEALR AFESLVDKYP QSPKARYGKA QSEDALAEKM
RSNDILLQAI NTYGEVAELP NAPAELIKLT LKRRADRQQF LGRTRGSVVT LHKLVQLYPE
DVTFRNELGV GYLLLGDNSN AKAVFEQVLA MSPNDGFAKV HYGFILKAEN YIAESIPYLK
EGLESGEPGT DDGRFYFHLG DALQRVGSQE AYIWYEAGHK KGHFASVWQR SLYNVNGLKA
QPWWTAKETS YTDLVRTLEA NWKLIRDEGL AVIDTEKGLF VPEDENLREK GDWSQYTLWQ
QGRKNEKSCA AAPRTCALLE RFPESTGCRR GQIKYSVMHP GTHVWPHTGP TNCRLRMHLG
LVIPKEGCRI RCANDTRSWE EGKVLIFDDS FEHEVWQEAN SYRLIFIVDV WHPELTSYQR
RTLPAI
//
