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Database: UniProt
Entry: A0A150UZF8_9PEZI
LinkDB: A0A150UZF8_9PEZI
Original site: A0A150UZF8_9PEZI 
ID   A0A150UZF8_9PEZI        Unreviewed;       297 AA.
AC   A0A150UZF8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chromatin associated protein KTI12 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M433DRAFT_25910 {ECO:0000313|EMBL:KYG43736.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG43736.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG43736.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG43736.1,
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   -!- SIMILARITY: Belongs to the KTI12 family.
CC       {ECO:0000256|ARBA:ARBA00025768}.
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:KYG43736.1}.
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DR   EMBL; JPDO01000286; KYG43736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UZF8; -.
DR   STRING; 766039.A0A150UZF8; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013641; KTI12/PSTK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12435:SF2; PROTEIN KTI12 HOMOLOG; 1.
DR   PANTHER; PTHR12435; UNCHARACTERIZED; 1.
DR   Pfam; PF08433; KTI12; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
SQ   SEQUENCE   297 AA;  33427 MW;  78FC2A48CA673099 CRC64;
     MPLILISGYP SSGKTYRSRQ LVDFFTRAIA EAGGDQAHVK RLKVYHINDQ SLGISRDAYA
     AARPEKDARA AFSSAIKRVL SRDAIVVADG MNYIKGFRYQ LYCEAKAVQT PSCVVYVGVT
     PEKARELNER VRQQGNGGYD PETFENLVYR YEEPNGMNRW DAPLFIVPFD DAEPPCQGIW
     EAMVGSDGNA KVVRPNAATV LKPASEHDYL YELDRMTSDV IGAITTWQQD HPGEGGGEVK
     LPDAEQSLVL PTTIPSLPQL QRLRRQFISL NRQHTLSKAR IRDLFINYLN DTFQRKE
//
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