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Database: UniProt
Entry: A0A1Y2V494_9PEZI
LinkDB: A0A1Y2V494_9PEZI
Original site: A0A1Y2V494_9PEZI 
ID   A0A1Y2V494_9PEZI        Unreviewed;       344 AA.
AC   A0A1Y2V494;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=RNA polymerase II elongator complex subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M434DRAFT_341725 {ECO:0000313|EMBL:OTA91598.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA91598.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA91598.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA91598.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SIMILARITY: Belongs to the KTI12 family.
CC       {ECO:0000256|ARBA:ARBA00025768}.
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DR   EMBL; KZ112497; OTA91598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2V494; -.
DR   STRING; 1001938.A0A1Y2V494; -.
DR   Proteomes; UP000194361; 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:UP000194361}.
FT   REGION          134..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38802 MW;  23B4620CFB02DCE7 CRC64;
     MPLIIVTGFP TSGKTTRAKQ LHNYLSERIR ESSSSTPPKY RLHLISDQTL SIPRSVYDLS
     ATPAHVRSAN ASEKDARASI YGAVKRVLSD RDIVILDGLN YIKGWRYQLF CESKAVRTPS
     CVLQIGCSRE KAKEVNEQRL RRRQERQDAG ADAGNENGDG KEKPSEEEDG PYEPENWENL
     VFRYEEPNPM TRWDSPLFTL IWEDGEDQTR QVFDSMWDTI AGEARKPVRP NQATVQRSRD
     AGGDYLYVLD RETQDIVKRI LDQQSDDGGD DIRIPSGSGK DGDELVVELP AGKKIGLPQL
     QRLRRAYMSL HRGGIGLEGV GNMGPERIRE TFVGYLNDAF EKDG
//
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