ID D3D1U0_9ACTN Unreviewed; 1613 AA.
AC D3D1U0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glycoside hydrolase family 3 domain protein {ECO:0000313|EMBL:EFC83089.1};
GN ORFNames=FrEUN1fDRAFT_3761 {ECO:0000313|EMBL:EFC83089.1};
OS Parafrankia sp. EUN1f.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC83089.1, ECO:0000313|Proteomes:UP000004777};
RN [1] {ECO:0000313|EMBL:EFC83089.1, ECO:0000313|Proteomes:UP000004777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC83089.1,
RC ECO:0000313|Proteomes:UP000004777};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA Fernandez M., Tisa L.;
RT "The draft genome of Frankia sp. EUN1f.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:EFC83089.1}.
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DR EMBL; ADGX01000057; EFC83089.1; -; Genomic_DNA.
DR Proteomes; UP000004777; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03224; ABC_TM1139_LivF_branched; 1.
DR CDD; cd06174; MFS; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFC83089.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 934..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1197..1218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1230..1248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1289..1309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1321..1339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 942..1346
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT DOMAIN 1376..1609
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 821..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 169936 MW; 31B71BF9EC7A89A7 CRC64;
MPLNTTSSPE TRATELLRKL TVEEKAQQVT GIMPVGLLGV GGLLPDEADR QLGLGIGHVA
ALGMLGHKTP DQVARAVNEI QRFLVTRTRL GIPAIFHVEA LNGVVSPGFS TFPTAIGLAA
TWNPDGVEEM ADVLRRQVRA IGHPFVLSPV MDVARDARWG RVHETYGEDP YLVSAMSVAF
TRGLQGGDLR EGAIATGKHF LGYGATEAGQ NMAATTVGAR ELYEVYARPF EAAIKLAGLA
AVMNSYSTVD GVPAGASHEV LTRLLRGRLG FAGTVVSDYD TIGHLHRRLR VARDAAEAGT
LALAAGIDVE LPIAEGYGPV LARAVRDGDV PIGQLDQACW RVLRDKFALG LFDQPYVPED
PVVINATARD GVELSRRLAE QSVTLLKNDG LLPLSRGLRR IAVIGPHADS VAVAFPAYTY
PGALQMFAAR FRGERATIPG TEQMAGAVSE DAVRLMIEEL SGPLGKTIDD YLREMYGAQS
IAEAVRAAVP DAQVAVAAGC GVLDGEPADI PAAVAAAQDA DVVILALGGR GGWFTANITE
GEGSDTANID LPANQVALVQ AVAATGTPCV GVVQTGRPLA LNAIADALPA LLYGYYGGQH
AAAAIAEVLF GTANPGGRLP ISLPRHSGQV PIHVGQPTGS GFRRTGHDMH QGYLDMPSTP
LFPFGHGLSY TTFDYTDLAI SPSQVDVDAA VSVRLTVRNS GERAGDEVVQ LYLADQATGV
TRPAQELVGF TRIGLAPGAS STVEFTVAMS QLGYVGLDGR FLLEPGHIQV LVGGSSDDIR
LRGVFEVVGE PVVLEGRRTY LSAVTIGDAS PASRTTLRKQ ANGVRHVRVP GRTRRPGTPM
STPDVSTTPD TPEVANPDTP EVANPDTPEV ANPDTPEVVA SAPETTTSVA GLAAGLIDAE
ADRRARQAQD SRDVLFADEL LPGVGGEALS LREGLAAGGS LTFLILVLLN ALDELESAAL
SVLAPDIRDS FGLSDGAIVF ISAAAGAFLV LGALPMGYLA DHLRRSRVIG WAGVAFSAMV
LASGLAANAF LFFLARFGVG IAKSSNNTVH GSLIADAYPI GVRGRLSASV YGAARVAGAL
SPLIVAGIAT LAGGDEGWRW PFLILGLPAL VVAIIAFRLP EPARGQQEMK SVLGEVVEDA
EPMPISIEAA FARLMRIRTV RTAVIAFSAL GFSLFTTSVL ANLRADDHYG MSTFQRGLMG
SLGGAALVVA LPIVAPRYDR LYHRDPQRAV KLLGLCVLPG AVLLPIQWLM PNWIAFMVLS
IPGAVFASVA FAMVGPVVQS VTPYRLRGLG MALAAVYMFF VGATGGAILS GLISNAYDPR
VAVLVIGIPA TLVGGLMMIR GASFVKSDLS MVVADLREEL AERDRQKADP ENIPVLHVNN
IDFSYGNVQV LFDVAFEVSR GETLALLGTN GAGKSTILKV VCGLGTPSRG VVRLGGRTIT
YVSPEQRGKY GVHLLPGGKG VFADMTIREN LEMAAFRMRR DRAGRDRRFA YVLELFPDLA
GRQSQLAGSL SGGQQQMLAL AMVLLHDPEV LLIDELSLGL APAVVQDLLA ILERLKADGL
TIVVVEQSLN IALAIADRAV FLEKGQVRFT GPTRELAERD DLARAVFLGR EGG
//
