ID F7KYD2_9FUSO Unreviewed; 214 AA.
AC F7KYD2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Ser/Thr and Tyr protein phosphatase (Dual specificity) {ECO:0000313|EMBL:EGN63242.1};
GN ORFNames=HMPREF0401_00603 {ECO:0000313|EMBL:EGN63242.1};
OS Fusobacterium animalis 11_3_2.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=457403 {ECO:0000313|EMBL:EGN63242.1, ECO:0000313|Proteomes:UP000004160};
RN [1] {ECO:0000313|EMBL:EGN63242.1, ECO:0000313|Proteomes:UP000004160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11_3_2 {ECO:0000313|EMBL:EGN63242.1,
RC ECO:0000313|Proteomes:UP000004160};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P.,
RA Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 11_3_2.";
RL Submitted (MAY-2011) 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:EGN63242.1}.
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DR EMBL; ACUO01000008; EGN63242.1; -; Genomic_DNA.
DR AlphaFoldDB; F7KYD2; -.
DR PATRIC; fig|457403.8.peg.605; -.
DR HOGENOM; CLU_080647_1_0_0; -.
DR Proteomes; UP000004160; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..202
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
SQ SEQUENCE 214 AA; 25200 MW; 3E061BC79457D37D CRC64;
MGGENFKVDK LLKLKVKCTI FISIFFVIFY KGAEFYTYTV DNVPSYFMEW ERNIPFLPVF
MLPYMTSAPF FLVTIFLEKN ENSLKLLMKR AIFLTVVSTF IFVIFPMKFY FPKPEIANPI
FKILFHILGL LDSNFNQCPS LHVSFAFLSV AVYCREVKSK FLKLFLCLWG FLLAISILFV
YQHHFIDFVG GTLIFLITCI IFPRKNRLLN FNKK
//
