ID A0A150VGD0_9PEZI Unreviewed; 1237 AA.
AC A0A150VGD0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PUM-HD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_58980 {ECO:0000313|EMBL:KYG49497.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49497.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49497.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49497.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- FUNCTION: RNA-binding nucleolar protein required for pre-rRNA
CC processing. Involved in production of 18S rRNA and assembly of small
CC ribosomal subunit. {ECO:0000256|ARBA:ARBA00024893}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
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:KYG49497.1}.
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DR EMBL; JPDO01000022; KYG49497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VGD0; -.
DR STRING; 766039.A0A150VGD0; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1035
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 1237 AA; 137278 MW; 68F862F029C0E56A CRC64;
MPQEQKKRGR RMKRKYATDN EEESDLHGNG SVKRQKPTEV VAEYETALVP TGLRDERVDT
TYAHKQYAFF GALSDEEQEY FKRADEMLEL NSFADASERE LFLNSVYREA AGKELKMAQS
QSCSRLMERL VQNSSESQVK QLFQAFSGNF VHLFTHRFAS HCCEALFLRA APMVSEEMLA
PAVSQDVVNP DCIYVSLENL FLHTIAELEG SLGYLITDKW ASHVLRVLFL VLAGDPLNIS
SISGVLHSKR KESIAIEGLQ DQELEKSRVV PEAFRQALKG LIAESVAGLD TAQLRALATH
PDGNPTLQVL LKLELTQFRK QKAKDRTSII SKLLPDDPIT SDSDSASFIS SLMYDPVGSH
LVEQIVRYAP GKMFKSLNRE IFKDRLDSFA RNEVASYVVC RVLERMGQDD LDEAHEKLIP
LLPGLLARNR TMVITTLIKR CTIRGVDTRA IAAQIDQANH GRDGFDIQSF LKLDPFSHEG
NNANGTSKDS IQANAAENAV AITNHAEPVK IHFNLLAQAM LNIPGALSGL ILDSLIQLSP
PALLQIAKDP IASRTVQAAL TTQNASMIQR RKLIQHCYGH IGEMALDRNA SHAVDCIWEG
THGLAFIRER IAEELAENEI QLRDSPYGRA VWKNWKMDIY KHRRHEWIRQ SKVKASNDGF
QSFSELDRNK HEGGIRKTPL DLARERHVKQ REEKKATEHK VRSSSSGSRQ SRFKTGPAST
AITSGDGKRE HSLLTAVKNS IIDFIQAADD DAATKFQGDS NRKSENVPKT VILKPHPPNE
LAQMFEIPFS VDGKGKDGLL RTMKEIQKYS VNTWHQGFLD KLYASTNPVG MAADLLLSSL
NTNVHVYQVS PALTIVEKQT SKALASLFGL KDPFSGGVSQ PGGSAANQSS MIIARNTLFP
ETKRQGNGER KFVLFTSIHG HYSTEKAAQI LGFGSDAVRN VPVDEAGCMI SSELSRMIDE
SKLRGETPFY VSATAGTTVL GSFDPLEDIA DVCQKHGLWF HVDGSWGGAV VLSGKHLHKI
CGIHRADSIT ICPHKMVGVP LTCSFLLGKD LRHFQKAMSL PAGYLFHGYE DAETANSSAP
DLQSNRTTDN NQDIWDLADL TPQCGRRGDS LKLALSWVYY GSSGFQTYID SAFSVAAYMA
EIISGNPRFS LVSSNPPPCL QVCFYYKKKT EAEGVDWRDR NGRTTAMITK LLVARGFMID
YAPGKDGKFF RVVVNGHTKR TTVECLIKAI EEVGDGI
//
