#=GF ID   GlcV_C_terminal
#=GF AC   PF17847.8
#=GF DE   Glucose ABC transporter C-terminal domain
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   ECOD:EUF04280
#=GF GA   27.60 27.60;
#=GF TC   27.80 41.10;
#=GF NC   27.20 25.80;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 90746521 -E 1000 --cpu 8 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0021
#=GF RN   [1]
#=GF RM   12823973
#=GF RT   Crystal structures of the ATPase subunit of the glucose ABC
#=GF RT   transporter from Sulfolobus solfataricus: nucleotide-free and
#=GF RT   nucleotide-bound conformations.
#=GF RA   Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM;
#=GF RL   J Mol Biol. 2003;330:343-358.
#=GF DR   INTERPRO; IPR040856;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This is the C-terminal domain found at the ATPase subunit of the
#=GF CC   glucose ABC transporter from Sulfolobus solfataricus. Overall,
#=GF CC   the C-terminal domain (residues 243-353) contains only
#=GF CC   beta-strands, which form an elongated barrel-shaped structure
#=GF CC   composed of two parts. This entry represents the upper part
#=GF CC   which includes a three-stranded anti-parallel beta-sheets and
#=GF CC   two small anti-parallel beta-strands. The overall structure of
#=GF CC   this domain is very similar to that of the C-terminal domain of
#=GF CC   MalK from T. litoralis however, the function of the C-terminal
#=GF CC   domain in GlcV is not clear [1].
#=GF SQ   13
#=GS D9Q251_ACIS3/297-356      AC D9Q251.1
#=GS A0A8J8PS83_9CREN/269-329  AC A0A8J8PS83.1
#=GS G4RMS4_THETK/293-353      AC G4RMS4.1
#=GS Q6KZ73_PICTO/301-361      AC Q6KZ73.1
#=GS A0A830GXD9_9CREN/298-359  AC A0A830GXD9.1
#=GS Q97UF2_SACS2/295-356      AC Q97UF2.1
#=GS A0A348B696_9CREN/291-352  AC A0A348B696.1
#=GS GLCV_SACS2/291-351        AC Q97UY8.1
#=GS A0A031LV23_9CREN/297-356  AC A0A031LV23.1
#=GS A0A8J8PQ10_9CREN/96-157   AC A0A8J8PQ10.1
#=GS L0A9W3_CALLD/295-356      AC L0A9W3.1
#=GS S0APU6_FERAC/314-374      AC S0APU6.1
#=GS A0A9E5DFR8_9CREN/295-357  AC A0A9E5DFR8.1
D9Q251_ACIS3/297-356                 mtfa------GKVKVKVSSYVAGVFRTVVSPID.DDSvELMVNMGGYVEPGSEKNLLIRTQKIKLFD.
A0A8J8PS83_9CREN/269-329             ....DDWVLVGKGRVKVVGYQGGMFRITVMPIE.GSD.EIVTYVDHPLRSDEEVLIYVRKNSIKIF-k
G4RMS4_THETK/293-353                 ....EKWILVGKGRVKVVGYQGGFFRVTVSPLD.SEE.EIVTYSDHPIKAGEEILVYVKKGSIKIFT.
Q6KZ73_PICTO/301-361                 ....KGYKNIGEATVRVSSYASGQFKITLSFVN.SDI.QFSINSEIPYKTGKNVPIGIRENKIKFFD.
A0A830GXD9_9CREN/298-359             ....DEWVLVGKARVKVSSYSSGLFRVTVVPPS.NDNtEIVAMMDRPFDVGKEVNLFVRSGKVLVF-s
Q97UF2_SACS2/295-356                 ....DKYIDMGIVKVKLVSYGAGIFKIVVSPIT.DENiDIIVDAEEPLETGIETHLLAKPNKVKIFD.
A0A348B696_9CREN/291-352             .pgm---VSLGKVRVKVSSYTGSSFRLVVSPIE.DDRvELYVNSDRPMDINSIALLYVRPEKVKIF-r
GLCV_SACS2/291-351                   ....DSWILVGKGKVKVIGYQGGLFRITITPLD.SEE.EIFTYSDHPIHSGEEVLVYVRKDKIKVFE.
A0A031LV23_9CREN/297-356             ....EGWVEAGKVRVKITTYEGGHFKVTLTPLG.DDQ.EIIVFMDK-IPKEEEMKLFVRPSKIMFF-k
A0A8J8PQ10_9CREN/96-157              ....DKYMDVGMVKVKLVSYSSGIFKIIVNPIS.NEDiEIIVDSDEPLEIGSEKHLLIRAGKVKVF-s
L0A9W3_CALLD/295-356                 ...p-EFVNVGKVKVKVTSYVAGIFKAVVSPIN.DESiEFDVNTERHIKAGTEMNLFVRTNKIKIFD.
S0APU6_FERAC/314-374                 ...r-GFKECGEAEVAISSYYQGSFRVTLSFKD.SSE.SFFCFHNTPLQPGEKVNIYLNPDLIHLFN.
A0A9E5DFR8_9CREN/295-357             ....ENWILVGKGVVKVIGYQGGMFRITVTPLEgSEDeEIVTYMDHPLKRKEEVLIYVKKGSVKIFE.
#=GC seq_cons                        ....-pal.lGKs+VKVsSYpuGhFRlTVoPls.s-p.EIhs.sD+PlcsGcEshlaVRssKIKlFp.
//