ID A0A1G1C3C8_9BACT Unreviewed; 445 AA.
AC A0A1G1C3C8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN ORFNames=A2Z41_01655 {ECO:0000313|EMBL:OGV89534.1};
OS Microgenomates group bacterium RBG_19FT_COMBO_39_10.
OC Bacteria.
OX NCBI_TaxID=1817748 {ECO:0000313|EMBL:OGV89534.1, ECO:0000313|Proteomes:UP000176844};
RN [1] {ECO:0000313|EMBL:OGV89534.1, ECO:0000313|Proteomes:UP000176844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV89534.1}.
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DR EMBL; MHDD01000015; OGV89534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1C3C8; -.
DR STRING; 1817748.A2Z41_01655; -.
DR Proteomes; UP000176844; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.30.420.430; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR044016; Big_13.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR Pfam; PF19077; Big_13; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR PROSITE; PS50853; FN3; 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 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..140
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 230..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 47383 MW; 94D097135BCA0FDE CRC64;
MRKRIPTAIG LVILIVGMTA AVFLINRSTH WFSRAAPGAA PKQIKFTNIT DSNFSVSWIT
DESTSGFLKY GPNNKIDQTS RDDRDELTGK TGNYTIHHIT LRNLKPNTTY QFQIGSGGSS
FDNNGQNYQV TTTATLTAPS PPSDVAYGTI NDQAGSPADG LIVYLSLPSA VTQSTLTKSS
GNWVIPLNLA RSEDLKGYAQ YDSQATIEDI LVQGGTKGTA TAVVTTKNDS PVPTITLGES
HDFKGTVTTD ETDKTTGSSK FNLEDSDSTP SSDKVEITNP EDEEGVSTQK PEIQGIGPVG
TILNITVEST KTYTGTIVVD ELGNWSWTPP ADLEPGEHTV TINYQDENGQ QQTLSHTFIV
LAAGEDGLPA FEATPSGTAT PSPTPSPSVS PSPSVSPSGR VSIPSTESGV PDSGYLTPTF
LVFIMGLVLM TFGLFSNILL KKKVF
//
