ID A0A436ZPF5_9PEZI Unreviewed; 687 AA.
AC A0A436ZPF5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase GRC3 {ECO:0000256|ARBA:ARBA00019824};
DE AltName: Full=Polynucleotide 5'-hydroxyl-kinase grc3 {ECO:0000256|ARBA:ARBA00018706};
GN ORFNames=DFL_008670 {ECO:0000313|EMBL:RVD80779.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD80779.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD80779.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD80779.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC {ECO:0000256|ARBA:ARBA00003798}.
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00011003}.
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:RVD80779.1}.
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DR EMBL; SAEB01000012; RVD80779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZPF5; -.
DR STRING; 97331.A0A436ZPF5; -.
DR VEuPathDB; FungiDB:DFL_008670; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF3; POLYNUCLEOTIDE 5'-HYDROXYL-KINASE NOL9; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 270..464
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 74258 MW; FE8F29A910E181E9 CRC64;
MSKRTSDSKV KAPLSALAAR RLRQQQLAAQ AEPSNSTPNG DSPAVTPGAE AAPVLHSKDV
PNTGPPAPLK SRSPSAMPPK ETTDFAPDLD TPRQISNFVQ TEDNYVYDTQ TLETTVKLRR
GESIVIQGEY RISVISGNIS ISGAILETSA SFDVIAPSTQ ALPVIECAPK SKKRKVDKTA
SKGGEYDAIF SLQSTQSGLN DIGRICPRFD RIWKPPLAST TVKSRASDSF TPILTAIQPT
PVLTLPPSWQ PAITSLSSTK QSPKSIFIIG GKSVGKSTFS RYLLNTLITN SQQSAVAYLD
LDPGQPSFTP PCILSLHKIT SPIVAPSFAT FGTTEIVRQH HMGYISPRED PKYYLRCAAD
LMRGYRRLVE QDERLTLIVN TCGWIKGMGR ELLQELVAVC EPTDVVGLGE VDGVFAEILP
DGKGAKRHLL EAAGAGAVVG NTPGGQQFTP ADLRMLQTIA YFHQQQPRNG GSGSGSTPSF
DFGKHLTAVP PLLAAYKGPA KVIHGITILD TGITPDLTFT ALNATIVAIK LVKKDDREHP
AIRYLEDLYG ENDDVTPYMP ANRFDGTSGM LPSEGTATAG LAIIRGVDEA NGELQVLTPM
HEDEINGHLE DGCRILLCRG RDEMPVYLMW DWRDGRAGQK GRGGTGSGGG VEKMPYLDFV
DGGEVTGKGA KEWKVRRNIM RRGQQRR
//
