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Database: UniProt
Entry: G0S8L5_CHATD
LinkDB: G0S8L5_CHATD
Original site: G0S8L5_CHATD 
ID   G0S8L5_CHATD            Unreviewed;      1272 AA.
AC   G0S8L5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Putative transporter protein {ECO:0000313|EMBL:EGS21975.1};
GN   ORFNames=CTHT_0038510 {ECO:0000313|EMBL:EGS21975.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS21975.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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DR   EMBL; GL988041; EGS21975.1; -; Genomic_DNA.
DR   RefSeq; XP_006694271.1; XM_006694208.1.
DR   AlphaFoldDB; G0S8L5; -.
DR   GeneID; 18257889; -.
DR   KEGG; cthr:CTHT_0038510; -.
DR   eggNOG; KOG0062; Eukaryota.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_263823_0_0_1; -.
DR   OrthoDB; 47478at2759; -.
DR   Proteomes; UP000008066; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd03221; ABCF_EF-3; 1.
DR   CDD; cd17356; MFS_HXT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR48022:SF61; HIGH AFFINITY GLUCOSE TRANSPORTER RGT2; 1.
DR   PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        406..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..501
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   DOMAIN          566..903
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1004..1240
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          927..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1210..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          717..767
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        928..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1228
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1272 AA;  139633 MW;  1024475882DB327C CRC64;
     MVGAVLFPIE GTADLRRVEA PVSFGAYLLC AFAAFGGIFF GYDTGWMSGV LGMPYFITMY
     TGMQYDYEAG KPIGVDPTKF GLPSSTKSLM TSILSCGTFL GSLVAGDVAD YIGRRPTIIS
     GCFVFCIGCS MQIASTNQTA LFVMGRLIAG LGVGFISAVI ILYMAEVAPR KVRGALVAGY
     QFCITVGILL ANCVVYSTQA RNDPGSYRIP IGVQFIWAVI LGIGLFLLPE SPRYHVMKGM
     IKEAAKDLSR VRGQPVDSNY IKDELAEIVA NHEYEMQVIP QMSYIGSWLA CFQGGFRRRG
     GNLRRTLIGC GSQLFQQITG INFIFYFGVT FFQQLGTISD PFFMSLVTTL VNVVSTTISF
     WAVEKIGRRP LLIYGGTGMV ISQLVVAVIG VTAGRPEEHN DAAVKTMIAF ICIFIFFFAS
     TWGPVGWILV GELFPLPIRS RGVGISTASN WLFNMIIALV APYMVGNDEH SADLGPKVFF
     IWGACCVGST LFAYFCVPEM KGLTLEQIDQ MMEETSARES TSESVATILV SCKQTRFDIK
     CPNYRELDVE GLNITVTSRP VDNGEAKGRG KAKASEGTEI LSNAKLRLKA GGRYALVGRN
     GTGKSTLMRA IAEKLIPGIP EETRISILQQ TSVKDVNADD LPETSGPSDG PSVLEEVIDK
     ATSKTELEKE INALSTGLNS PFPHDAVFAL RKLRLDRMKK RLFVLDKDAR LRSGTRGLQA
     RKALVEYEKQ VAAAEAQLSQ PPKEISSETL QAETQEAADL LGELQAQVEP SRMAEVEGNA
     KKILMGLGFK EGDMAKSAGS LSGGWRMRAA LATALLKEAD ILILDEPTNF LDLFGILWLQ
     KWLQHMEDTL ATPPTLVFVS HDRDFASSVC TDLIILKDKE LTYFHGDLPS YEAAQAEKRI
     YLTKMKEAQD KQRAHMQESI RQNLIQGRKN DDQNKIRQAK SRQKRLEDRM GMQVNEKGGR
     FKLNRDLVGW HTSSRAEIVV PQEERGVTIV LPDPTELRFP GSLISLEKVS FRYAGEKGQK
     VRPPATLIDV SLTVGMGDRI GILGLNGAGK STLIRLLVGD PAPAGAKVTG NVTTHPRLKL
     AYYSQHAVEA LQRLGQSDPS LTALSLLTSE VSPDAGLDES DIRGLLSSLG LRGNLVSSVP
     IRRLSGGQLV RLELARLLWR RPLCLVLDEV TTHLDYETVT GLRKALREWE GAVVLVSHDR
     WFMRGVVEGE RDNEDGEEEQ DEEEEEGRKD GEGVGRRRVV YKLAGGKLSL LEGGVREFEE
     GMERRVGRLI GD
//
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