ID A0A421JJS5_9ASCO Unreviewed; 670 AA.
AC A0A421JJS5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=JA1_004378 {ECO:0000313|EMBL:RLV90689.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV90689.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV90689.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV90689.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:RLV90689.1}.
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DR EMBL; NSGQ01000047; RLV90689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JJS5; -.
DR STRING; 2028339.A0A421JJS5; -.
DR Proteomes; UP000285775; 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, ECO:0000313|EMBL:RLV90689.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 263..450
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 75898 MW; 9C0DE04B668F5AA6 CRC64;
MSAYAALKDN SSIRSIFHES GDAYEEDAED EVHYQANSSG EDSDFGEDRI PVQSISNSHC
PREMGPPKTI TWSKFILTEE NTVFGENYVI FGLKTGEYLV LNGQCNVTIQ KGAVLFNQIH
YIASNPYRSF NIVGLQSQSL PIISSTERSN TSDKSLDTKT VENEDLFTNE FKSVIKIENL
STGLENIGKY HPPFKGLLFG NENDEDIISE DERMFQKYSF EIVLREKGVS ALCVSKIWSD
KALELSTLAS RLGSIANSTM IIGNKNSGKS TFSKVLLNSY LLSNESSPVC YLDIDPGQSE
FSPPYSISLR LVSEINFGSW FPSGSTQDCH DHYFGFTSPV HLPNRYLEII ENLLRCYETR
YKPKGHHLII NTPGWIKGYG KELLTIITEK INPDTLILLS SSLDLEGEDN SDILQNLRFK
SLTLLPGIYQ VSKYSPSQTR VLNKLLYFHQ NSPGMFDFQS HLLDKSPLKL SYETEGVNQS
TFKGINAVSV LNHSVGVNFN YEDVLTLIES TLMGVYCVKE EVYETIRGSL HSKEYHQNHP
YYLDPSRLLD LLSCTPHDNS NVTFMGLVML HSLNTAQKYM NIYLPRNMLK QFQQKLQSNF
KMILIRGEGD LPSAEIFHPE LVSKALNSNK QEHLSKAQTI YPYVSFERKP KLGGVWKARR
NVMRRGHKHA
//
