ID A0A328VVH8_9CHLR Unreviewed; 642 AA.
AC A0A328VVH8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A4R35_21370 {ECO:0000313|EMBL:RAQ98105.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ98105.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ98105.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ98105.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ98105.1}.
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DR EMBL; MCIF01000002; RAQ98105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VVH8; -.
DR Proteomes; UP000248706; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000248706}.
FT DOMAIN 1..121
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 530..580
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 127..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 66455 MW; 7C8AA764D0801D01 CRC64;
MLADVGLAHF VRRFGRLQRP ILPVTAAPEQ LGGRATQASD QFALAVIVYT WITGRPPYLG
LPEEIAQAKL SESFPSLLSL NPQIPVEVEG VIRRALSVYP EDRYPSVLAF AEALQQAAPR
LVTVAGQAFP GPQGEPLQGG PISLPADGEE REPASDGGQL EQTAAEQSEA VMVAGGEVQA
TVQTAPDEPA EAEPSAEEVS AASAEALMAS PVQEAIHADA EVVTGLAGSQ SNETVLAAEA
EIQVADGGAC DEQLATGGAG SSAPLAPEPQ QAAASDQNQV TAPEESEPAA ELLTASGEAA
LPEPGLNPES TAIEATIKQT DGHALSGSAL TYFEALLQAT RPPNVPAPES PSEAASSAVS
EPAACAPEVA ATIVAGQEQA DPSESEAVAQ QTVTVELPPT SPAEVSLLEV LSGLHTRPST
SPVSATQRTP QTEVVPIAEA AQVLRGANGA QPEATHEEAS AVTDGRGEAS QEGERGWTEG
ESVKARIELV PAPAPAEEAH VEAAPAYILV LPPTMSGRQA TIVELSAPEV SIGRAGDSGI
LLEGDRRVSR RHAFLRWAGT ELLIQDGDNT EGVFVNGQRL EQGGSRVLRS GDQLRIGDHE
LIVCRSREEA RQLQQERTVS TDQADTQEAS DSTASSSSSP TL
//
