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Database: UniProt
Entry: A0A2N5W580_9BASI
LinkDB: A0A2N5W580_9BASI
Original site: A0A2N5W580_9BASI 
ID   A0A2N5W580_9BASI        Unreviewed;       971 AA.
AC   A0A2N5W580;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Prolyl 4-hydroxylase alpha subunit Fe(2+) 2OG dioxygenase domain-containing protein {ECO:0000259|Pfam:PF13640};
GN   ORFNames=PCANC_01788 {ECO:0000313|EMBL:PLW57373.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW57373.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW57373.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW57373.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLW57373.1}.
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DR   EMBL; PGCJ01000011; PLW57373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5W580; -.
DR   STRING; 200324.A0A2N5W580; -.
DR   Proteomes; UP000235388; Unassembled WGS sequence.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR33099; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33099:SF7; MYND-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT   DOMAIN          199..282
FT                   /note="Prolyl 4-hydroxylase alpha subunit Fe(2+) 2OG
FT                   dioxygenase"
FT                   /evidence="ECO:0000259|Pfam:PF13640"
FT   REGION          39..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  107989 MW;  EC15E6EFFAFC570E CRC64;
     MLHHSTADGG WDLVKSECFV IQTPNLSLQL YHQSVPSNYH EMASNTPRDG PISNSENDLE
     GSNSQDSEDS GSEDLEYDES LKDDLYTALQ GIKASGTFAA WGALPTTPPA GLHVEGVGDI
     PFPIQAATIQ QLIAKAHQAP FGRRSETLID VSVRNTWEIH GDQLRFLDPD WVRFLLDVSE
     RVGADLGIQA PIRLDLYKML IYEKGAMFKA HTDTEKTPGM FGTLVICLPS AHTGGEVIVK
     HHGQTKTLRT SDAAQSYACW YSDAMHEVLP VQSGYRCVLT YNLALKPGLT PPVAPPPNYE
     KEMIQTTLRV WLKKMESDKK ERYLYCPLEH EYTEAAISLR ALKANDLARA QVMQDLASDL
     PFDIFLALLV KREDGIPEPD ESSYPPPKKR GRHAYIDYDK PDDDVPRKCY GDDTHFLEEV
     LETHHEVKSL RALDGTPIAH DFDFDVDACL EEDPFDGLNI AEEDYEPYMG NWGPTAIQWY
     RFAALVIVPH SELGTYLATC GSSNASATIG YLAKFCSLLT AKQHMLDAMS HLCRGQPSRT
     GLAGVNLANL PANFVDWAMR WLDTRPESER SEHYQNWIPI LLPGYPSFSD RIRIIQRLSH
     PTGNVAPTSS PLALKLTRQS ITDFISTLGP PAAEDGNVIV SAVFTLNDSW NNTSALLTSI
     FDRFSQANAV TFLIQFLSQF KALVRSTSTE TFPVASTTVL WKNLSSRFCE RNPTSMITST
     NATNSSERRV VVTPRALAGF ACDLHDLSAD GHNLLEPFIQ KISSHCSEFS AADMRSFWVP
     FFSELTRALA SRSFPLNTAF YQQLARRLIQ RMDDQLVGPC PQPTPSSGGP QQVSCSPSVA
     RTQVSCSCDD CVNLNRFLQD GSKTVARYKF VKARRQHLET IINRSNIPCT HITQLGGSPL
     TLVVTKSQSL VIQNTLDAWN KRQRHAYTSL LDKIEPEHLK AILGDQESAR VCLLARGNVL
     TSSNRNSLDL T
//
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