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Conserved domains on  [gi|1577416155|ref|WP_130179702|]
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MULTISPECIES: glycine betaine/L-proline ABC transporter ATP-binding protein [Clostridia]

Protein Classification

quaternary amine ABC transporter ATP-binding protein( domain architecture ID 11467934)

quaternary amine ABC transporter ATP-binding protein is the ATPase catalytic subunit and is responsible for energy coupling to the transport system of an ABC transporter, such as Bacillus subtilis glycine betaine transport ATP-binding protein OpuAA

CATH:  3.40.50.300
EC:  7.6.2.9
Gene Ontology:  GO:0042626|GO:0140359|GO:0016887|GO:0005524|GO:0015697
PubMed:  25750732|24638992|21958115|15313236|19234479
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-390 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


:

Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 678.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG4175     1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG4175    81 AGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG4175   161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGII 320
Cdd:COG4175   241 RIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 321 TIDKVSELMKENRdDLKSVIDTDIRTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGIA 390
Cdd:COG4175   321 TADDALEAVKGEK-DLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
 
Name Accession Description Interval E-value
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-390 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 678.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG4175     1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG4175    81 AGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG4175   161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGII 320
Cdd:COG4175   241 RIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 321 TIDKVSELMKENRdDLKSVIDTDIRTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGIA 390
Cdd:COG4175   321 TADDALEAVKGEK-DLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 4-272 1.12e-171

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 479.83  E-value: 1.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03294     1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03294    81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03294   161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240

                         250       260
                  ....*....|....*....|....*....
gi 1577416155 244 QIGEPEEILNSPADAYVREFIQDVNRTKI 272
Cdd:cd03294   241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 35-394 1.54e-140

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 404.62  E-value: 1.54e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNF 114
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNRTKIVS 274
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 275 ASSIMRSSESIILEKA---GVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRdDLKSVIDTDIRTVGVDT 351
Cdd:TIGR01186 241 AERIAQRMNTGPITKTadkGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQ-GLQDVLIDDIYTVDAGT 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 352 SIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGIAGKEE 394
Cdd:TIGR01186 320 LLRETVRKVLKAGIKVPVVDEDQRLVGIVTRGSLVDALYDSRE 362
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
3-389 9.27e-126

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 368.59  E-value: 9.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   3 KIQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG 82
Cdd:PRK10070    4 KLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  83 EIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:PRK10070   84 QVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK10070  164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 243 VQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKA---GVRTAAKKMKDLEISSIFVTDKHKTLLGI 319
Cdd:PRK10070  244 VQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTpgfGPRSALKLLQDEDREYGYVIERGNKFVGA 323

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 320 ITIDKVSELMKENRDDLKSVIDTDIrTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGI 389
Cdd:PRK10070  324 VSIDSLKTALTQQQGLDAALIDAPL-AVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRAL 392
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 43-192 1.27e-48

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 162.05  E-value: 1.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklREIRRKKIAMVFQNFALLPHRTV 122
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 123 LENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYEN----AKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
 3-244 4.70e-48

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 163.76  E-value: 4.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   3 KIQVKNVYKVFgsapmqmisfleKGEKKtdllkkyKHSVgVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG 82
Cdd:NF040729    1 KLKIQNISKTF------------INNKK-------ENEV-LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  83 EIYIDNEKITQVSSAKlreirrkkiAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:NF040729   61 EILVNGNEVTKPGPDR---------GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPH 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIM--KDG 240
Cdd:NF040729  132 QISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKG 211


                  ....
gi 1577416155 241 NIVQ 244
Cdd:NF040729  212 KILE 215
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
43-237 1.37e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 99.62  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEiyidnekitqvssakLREIRRKKIAMVFQNFAL---LPh 119
Cdd:NF040873    8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVpdsLP- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGL-----EIQKVDVEERkKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:NF040873   72 LTVRDLVAMGRwarrgLWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 195 DPLIRKEMqNELLSLQTKMQKTIVFITHDLDEALKIgDRIAIM 237
Cdd:NF040873  151 DAESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
44-244 1.79e-20

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 92.93  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRlIEPT---SGEIYIDNEKitqvssAKLREIR---RKKIAMVFQNFALL 117
Cdd:NF040905   18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEV------CRFKDIRdseALGIVIIHQELALI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHRTVLENVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:NF040905   91 PYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 195 dplirkemqNE-----LLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIVQ 244
Cdd:NF040905  171 ---------NEedsaaLLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
41-251 2.78e-19

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.18  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEiyidnekitqvssAKL--REIR------RKKIAMVFQ 112
Cdd:NF033858  280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-------------AWLfgQPVDagdiatRRRVGYMSQ 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 NFALLPHRTVLENVA-----FGLEiqkvdvEERKKKAI-EMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:NF033858  347 AFSLYGELTVRQNLElharlFHLP------AAEIAARVaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKMQKTIvFI-THDLDEALKIgDRIAIMKDGNIVQIGEPEEI 251
Cdd:NF033858  421 LDEPTSGVDPVARDMFWRLLIELSREDGVTI-FIsTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
33-251 2.26e-08

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 55.51  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSG--KSTLIRclnRLIEPTSGE------IYIDNEKITQVSSAKLREIRR 104
Cdd:NF000106   19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPA---HV*GPDAGRrpwrf*TWCANRRALRRTIG*HRPVR* 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 KKiamvFQNFAllpHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKpkeLSGGMQQRVGLARALATDADI 184
Cdd:NF000106   96 GR----RESFS---GRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK---YSGGMRRRLDLAASMIGRPAV 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:NF000106  166 LYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-249 2.86e-08

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 52.38  E-value: 2.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   53 GEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE-IYIDNEKITQVSSAKLREIrrkkiamvfqnfallphrtvlenvafgle 131
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLI----------------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  132 iqkvdveerkkkaiemlevvglkgYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQT 211
Cdd:smart00382  53 ------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1577416155  212 KM-----QKTIVFITHDLDEalkIGDRIAIMKDGNIVQIGEPE 249
Cdd:smart00382 109 LLlksekNLTVILTTNDEKD---LGPALLRRRFDRRIVLLLIL 148
GguA NF040905
sugar ABC transporter ATP-binding protein;
43-243 7.49e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.94  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLI-----RCLNRLIeptSGEIYIDNEKItQVSSAKlREIR---------RKKIA 108
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgRSYGRNI---SGTVFKDGKEV-DVSTVS-DAIDaglayvtedRKGYG 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVF-----QNFAL-----LPHRTVLENVAfglEIqKVDVEERKK---KAIEMLEVVGlkgyenakpkELSGGMQQRVGLA 175
Cdd:NF040905  351 LNLiddikRNITLanlgkVSRRGVIDENE---EI-KVAEEYRKKmniKTPSVFQKVG----------NLSGGNQQKVVLS 416

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 176 RALATDADILLMDEAFSALDPLIRKEMQ---NELlslqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:NF040905  417 KWLFTDPDVLILDEPTRGIDVGAKYEIYtiiNEL----AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
116-252 1.85e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 50.12  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 LLPHRTVLENVAF-----GLeiqkvDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:NF033858   89 LYPTLSVFENLDFfgrlfGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 191 FSALDPLIRK---EMQNELLSLQTKMqkTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEIL 252
Cdd:NF033858  164 TTGVDPLSRRqfwELIDRIRAERPGM--SVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 305-389 5.46e-03

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 37.04  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 305 SSIFVTDKHKTLLGIITIDKVSELMKENRD---------DLKSVIDTDIRTVGVDTSIDEIIPL-----FLqsgypvAVV 370
Cdd:NF041630   43 SKIPVLDKDKKFVGLISLSDITDYMLGLERiefeklselKVADVMNTDVPTITDDYDLEEILHLlvdhpFL------PVV 116

                          90
                  ....*....|....*....
gi 1577416155 371 DDENKLKGIIFKSTVLAGI 389
Cdd:NF041630  117 DEDGIFLGIITRREILKAV 135
 
Name Accession Description Interval E-value
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-390 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 678.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG4175     1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG4175    81 AGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG4175   161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGII 320
Cdd:COG4175   241 RIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 321 TIDKVSELMKENRdDLKSVIDTDIRTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGIA 390
Cdd:COG4175   321 TADDALEAVKGEK-DLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 4-272 1.12e-171

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 479.83  E-value: 1.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03294     1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03294    81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03294   161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240

                         250       260
                  ....*....|....*....|....*....
gi 1577416155 244 QIGEPEEILNSPADAYVREFIQDVNRTKI 272
Cdd:cd03294   241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 35-394 1.54e-140

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 404.62  E-value: 1.54e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNF 114
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNRTKIVS 274
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 275 ASSIMRSSESIILEKA---GVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRdDLKSVIDTDIRTVGVDT 351
Cdd:TIGR01186 241 AERIAQRMNTGPITKTadkGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQ-GLQDVLIDDIYTVDAGT 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 352 SIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGIAGKEE 394
Cdd:TIGR01186 320 LLRETVRKVLKAGIKVPVVDEDQRLVGIVTRGSLVDALYDSRE 362
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
3-389 9.27e-126

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 368.59  E-value: 9.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   3 KIQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG 82
Cdd:PRK10070    4 KLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  83 EIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:PRK10070   84 QVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK10070  164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 243 VQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKA---GVRTAAKKMKDLEISSIFVTDKHKTLLGI 319
Cdd:PRK10070  244 VQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTpgfGPRSALKLLQDEDREYGYVIERGNKFVGA 323

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 320 ITIDKVSELMKENRDDLKSVIDTDIrTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGIIFKSTVLAGI 389
Cdd:PRK10070  324 VSIDSLKTALTQQQGLDAALIDAPL-AVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRAL 392
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 20-325 1.28e-120

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 351.70  E-value: 1.28e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  20 MISFlekgekkTDLLKKYKHS-VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAK 98
Cdd:COG1125     1 MIEF-------ENVTKRYPDGtVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  99 LReiRRkkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGL--KGYENAKPKELSGGMQQRVGLAR 176
Cdd:COG1125    74 LR--RR--IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVAR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 177 ALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:COG1125   150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 257 DAYVREFIQD---VNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKV 325
Cdd:COG1125   230 NDFVADFVGAdrgLRRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDL 301
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 17-269 9.22e-108

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 320.89  E-value: 9.22e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  17 PMQMISFlekgekkTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSS 96
Cdd:COG3842     2 AMPALEL-------ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  97 AKlreiRRkkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLAR 176
Cdd:COG3842    75 EK----RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 177 ALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:COG3842   149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228

                         250
                  ....*....|...
gi 1577416155 257 DAYVREFIQDVNR 269
Cdd:COG3842   229 TRFVADFIGEANL 241
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-262 3.24e-98

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 293.15  E-value: 3.24e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSapmqmisflekGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG1116     5 APALELRGVSKRFPT-----------GGGGVTALD---------DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSaklreirrkKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG1116    65 SGEVLVDGKPVTGPGP---------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAY 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG1116   136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1577416155 241 -----NIVQIGEP----EEILNSPA-DAYVRE 262
Cdd:COG1116   216 pgrivEEIDVDLPrprdRELRTSPEfAALRAE 247
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 32-265 7.06e-98

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 291.51  E-value: 7.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHS-VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAMV 110
Cdd:cd03295     5 NVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----RKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGL--KGYENAKPKELSGGMQQRVGLARALATDADILLMD 188
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 189 EAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-264 2.13e-95

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 289.28  E-value: 2.13e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPmqmisflekgekktdllkkykhsvGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG3839     1 MASLELENVSKSYGGVE------------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKlreiRRkkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG3839    57 SGEILIGGRDVTDLPPKD----RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRK 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG3839   131 PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG 210

                         250       260
                  ....*....|....*....|....
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFI 264
Cdd:COG3839   211 RIQQVGTPEELYDRPANLFVAGFI 234
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 4-245 1.98e-94

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 282.05  E-value: 1.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisfleKGEKKTdllkkykhsvGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03293     1 LEVRNVSKTYGG----------GGGAVT----------ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSsaklreirrKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03293    61 VLVDGEPVTGPG---------PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQ 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIM--KDGN 241
Cdd:cd03293   132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGR 211


                  ....
gi 1577416155 242 IVQI 245
Cdd:cd03293   212 IVAE 215
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 31-246 2.02e-94

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 281.72  E-value: 2.02e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklreIRRKKIAMV 110
Cdd:cd03259     4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PERRNIGMV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03259    78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03259   158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
4-272 5.87e-90

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 275.03  E-value: 5.87e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekgekktdllkKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1135     2 IELENLSKTFPT--------------------KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:COG1135    62 VLVDGVDLTALSERELRAARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDP--------LIRKemqnellsLQTKMQKTIVFITHDLDEALKIGDRIA 235
Cdd:COG1135   141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPettrsildLLKD--------INRELGLTIVLITHEMDVVRRICDRVA 212

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1577416155 236 IMKDGNIVQIGEPEEILNSPADAYVREFIQDVNRTKI 272
Cdd:COG1135   213 VLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDEL 249
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 4-280 1.14e-89

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 274.33  E-value: 1.14e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekgekkTDLLkkykhsvgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1118     3 IEVRNISKRFGS---------------FTLL---------DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKI-TQVSSaklreiRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:COG1118    59 IVLNGRDLfTNLPP------RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPS 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:COG1118   133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1577416155 243 VQIGEPEEILNSPADAYVREFIQDVNRTKIVSASSIMR 280
Cdd:COG1118   213 EQVGTPDEVYDRPATPFVARFLGCVNVLRGRVIGGQLE 250
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 2-264 9.18e-85

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 257.99  E-value: 9.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   2 AKIQVKNVYKVFGSapmQMIsflekgekktdllkkykhsvgVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTS 81
Cdd:COG1127     4 PMIEVRNLTKSFGD---RVV---------------------LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  82 GEIYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGL-EIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:COG1127    60 GEILVDGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKM 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG1127   139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218

                         250       260
                  ....*....|....*....|....
gi 1577416155 241 NIVQIGEPEEILNSPaDAYVREFI 264
Cdd:COG1127   219 KIIAEGTPEELLASD-DPWVRQFL 241
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 4-267 1.28e-84

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 257.62  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekgekkTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1126     2 IEIENLHKSFGD---------------LEVLK---------GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQvSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGL-EIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:COG1126    58 ITVDGEDLTD-SKKDINKLRRK-VGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPlirkEMQNELLSL-----QTKMqkTIVFITHDLDEALKIGDRIAIM 237
Cdd:COG1126   136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEVLDVmrdlaKEGM--TMVVVTHEMGFAREVADRVVFM 209

                         250       260       270
                  ....*....|....*....|....*....|
gi 1577416155 238 KDGNIVQIGEPEEILNSPADAYVREFIQDV 267
Cdd:COG1126   210 DGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 35-264 1.40e-84

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 257.17  E-value: 1.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMVFQNF 114
Cdd:cd03300     8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQNY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:cd03300    82 ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:cd03300   162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-267 1.44e-83

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 264.07  E-value: 1.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPmqmisfleKGEKKtdllkkykhsvGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1123   261 LEVRNLSKRYPVRG--------KGGVR-----------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQN-FA-LLPHRTVLENVAFGLEIQKV-DVEERKKKAIEMLEVVGL-KGYENA 159
Cdd:COG1123   322 ILFDGKDLTKLSRRSLRELRRR-VQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADR 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 160 KPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKD 239
Cdd:COG1123   401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480

                         250       260
                  ....*....|....*....|....*...
gi 1577416155 240 GNIVQIGEPEEILNSPADAYVREFIQDV 267
Cdd:COG1123   481 GRIVEDGPTEEVFANPQHPYTRALLAAV 508
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-242 3.64e-80

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 245.48  E-value: 3.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03255     1 IELKNLSKTYGG-----------GGEKVQALK---------GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03255    61 VRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEAlKIGDRIAIMKDGNI 242
Cdd:cd03255   141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 4-255 5.45e-79

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 242.87  E-value: 5.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPmqmisflekgekktdllkkyKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03258     2 IELKNVSKVFGDTG--------------------GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03258    62 VLVDGTDLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03258   141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220

                         250
                  ....*....|..
gi 1577416155 244 QIGEPEEILNSP 255
Cdd:cd03258   221 EEGTVEEVFANP 232
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 4-263 1.72e-77

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 239.33  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekgekKTDLlkkykhsvgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03261     1 IELRGLTKSFGG--------------RTVL----------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGL-EIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:cd03261    57 VLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:cd03261   136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215

                         250       260
                  ....*....|....*....|.
gi 1577416155 243 VQIGEPEEILNSPaDAYVREF 263
Cdd:cd03261   216 VAEGTPEELRASD-DPLVRQF 235
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
4-243 4.59e-77

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 238.02  E-value: 4.59e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1136     5 LELRNLTKSYGT-----------GEGEVTALR---------GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:COG1136    65 VLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIV 243
Cdd:COG1136   145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 58-293 3.73e-76

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 238.93  E-value: 3.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  58 VMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklreiRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDV 137
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 138 EERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTI 217
Cdd:TIGR01187  75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 218 VFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNrtkIVSASSIMRSSESIILEKAGVR 293
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEIN---VFEATVIERKSEQVVLAGVEGR 227
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 4-267 1.46e-75

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 238.16  E-value: 1.46e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPMQMisflekgekktdllkkykhsVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:PRK11153    2 IELKNISKVFPQGGRTI--------------------HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGR 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:PRK11153   62 VLVDGQDLTALSEKELRKARRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDP--------LIRKemQNELLSLqtkmqkTIVFITHDLDEALKIGDRIA 235
Cdd:PRK11153  141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPattrsileLLKD--INRELGL------TIVLITHEMDVVKRICDRVA 212

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1577416155 236 IMKDGNIVQIGEPEEILNSPADAYVREFIQDV 267
Cdd:PRK11153  213 VIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 4-264 5.60e-75

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 233.00  E-value: 5.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPmqmisflekgekktdllkkykhsvGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03296     3 IEVRNVSKRFGDFV------------------------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSsaklreIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKV----DVEERKKKAIEMLEVVGLKGYENA 159
Cdd:cd03296    59 ILFGGEDATDVP------VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 160 KPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKD 239
Cdd:cd03296   133 YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212

                         250       260
                  ....*....|....*....|....*
gi 1577416155 240 GNIVQIGEPEEILNSPADAYVREFI 264
Cdd:cd03296   213 GRIEQVGTPDEVYDHPASPFVYSFL 237
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
31-287 3.02e-74

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 235.61  E-value: 3.02e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMV 110
Cdd:PRK09452   18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN------RHVNTV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:PRK09452   92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNrt 270
Cdd:PRK09452  172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN-- 249

                         250
                  ....*....|....*..
gi 1577416155 271 kIVSASSIMRSSESIIL 287
Cdd:PRK09452  250 -IFDATVIERLDEQRVR 265
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 32-240 3.87e-74

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 228.61  E-value: 3.87e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaKLREIRRKKIAMVF 111
Cdd:cd03229     5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE--DELPPLRRRIGMVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03229    83 QDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:cd03229   129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 43-252 5.14e-73

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 227.60  E-value: 5.14e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssAKLREIRRKkIAMVFQN-----FAll 117
Cdd:COG1122    17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRK-VGLVFQNpddqlFA-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 phRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG1122    91 --PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 198 IRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:COG1122   169 GRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 32-246 6.33e-73

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 226.75  E-value: 6.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMVF 111
Cdd:cd03301     5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------RDIAMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03301    79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03301   159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 32-246 8.25e-72

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 224.31  E-value: 8.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVG----VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsAKLREIRRKKI 107
Cdd:cd03257     6 NLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKIRRKEI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 108 AMVFQN--FALLPHRTVLENVAFGLEIQKVDV--EERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDA 182
Cdd:cd03257    85 QMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 183 DILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03257   165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
31-254 1.15e-71

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 224.17  E-value: 1.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklREIRRKkIAMV 110
Cdd:COG1131     4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVRRR-IGYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:COG1131    79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG1131   159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 43-256 1.27e-71

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 227.24  E-value: 1.27e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP---TSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNF--ALL 117
Cdd:COG0444    21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGREIQMIFQDPmtSLN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHRTVLENVAFGLEI-QKVDVEERKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:COG0444   101 PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 194 LDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:COG0444   181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 31-242 2.32e-71

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 222.79  E-value: 2.32e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvSSAKLREIRrKKIAMV 110
Cdd:cd03262     4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR-QKVGMV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGL-EIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDE 189
Cdd:cd03262    82 FQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 190 AFSALDPlirkEMQNELLSL-----QTKMqkTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:cd03262   162 PTSALDP----ELVGEVLDVmkdlaEEGM--TMVVVTHEMGFAREVADRVIFMDDGRI 213
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
45-237 3.67e-71

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 223.97  E-value: 3.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklreiRRkkiAMVFQNFALLPHRTVLE 124
Cdd:COG4525    25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA------DR---GVVFQKDALLPWLNVLD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQN 204
Cdd:COG4525    96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1577416155 205 ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIM 237
Cdd:COG4525   176 LLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-251 8.64e-68

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 214.92  E-value: 8.64e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekgekktdllkkykHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG3638     3 LELRNLSKRYPG-----------------------GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLENVAFGL---------EIQKVDVEERKKkAIEMLEVVGLK 154
Cdd:COG3638    60 ILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsLLGLFPPEDRER-ALEALERVGLA 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 155 GYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRI 234
Cdd:COG3638   138 DKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217

                         250
                  ....*....|....*..
gi 1577416155 235 AIMKDGNIVQIGEPEEI 251
Cdd:COG3638   218 IGLRDGRVVFDGPPAEL 234
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 33-251 6.95e-67

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 212.43  E-value: 6.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSV-GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIAMVF 111
Cdd:cd03256     6 LSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDV--------EERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDAD 183
Cdd:cd03256    85 QQFNLIERLSVLENVLSGRLGRRSTWrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 184 ILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:cd03256   165 LILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 45-264 1.01e-65

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 209.11  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMVFQNFALLPHRTVLE 124
Cdd:cd03299    17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHMTVYK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQN 204
Cdd:cd03299    91 NIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 205 ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:cd03299   171 ELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
32-304 4.27e-65

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 212.39  E-value: 4.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMVF 111
Cdd:PRK11607   24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK11607   98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNrtk 271
Cdd:PRK11607  178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN--- 254

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1577416155 272 IVSASSIMRSSESIILEKAGVRTAAKKMKDLEI 304
Cdd:PRK11607  255 VFEGVLKERQEDGLVIDSPGLVHPLKVDADASV 287
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 43-261 4.35e-65

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 210.74  E-value: 4.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRkKIAMVFQN-FALL-PHR 120
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVFQDpYASLnPRM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQKV-DVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLI 198
Cdd:COG4608   113 TVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 199 RKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVR 261
Cdd:COG4608   193 QAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
35-269 5.03e-65

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 211.10  E-value: 5.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklreiRRKKIAMVFQNF 114
Cdd:PRK10851   10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQHY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEI----QKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:PRK10851   84 ALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVNR 269
Cdd:PRK10851  164 FGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-265 9.51e-65

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 206.96  E-value: 9.51e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGsapmqmisflekgekktdllKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG1124     2 LEVRNLSVSYG--------------------QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQvssAKLREIRRKkIAMVFQNF--ALLPHRTVLENVAFGLEIQKVDveERKKKAIEMLEVVGL-KGYENAK 160
Cdd:COG1124    62 VTFDGRPVTR---RRRKAFRRR-VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRY 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG1124   136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215

                         250       260
                  ....*....|....*....|....*
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:COG1124   216 RIVEELTVADLLAGPKHPYTRELLA 240
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
47-264 2.31e-64

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 205.37  E-value: 2.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  47 SFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrKKIAMVFQNFALLPHRTVLENV 126
Cdd:COG3840    19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQENNLFPHLTVAQNI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 127 AFGLEIQ-KVDVEERKKkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNE 205
Cdd:COG3840    93 GLGLRPGlKLTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 206 LLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:COG3840   172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 44-240 4.23e-64

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 203.85  E-value: 4.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAMVFQN-----FALlp 118
Cdd:cd03225    18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNpddqfFGP-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 hrTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLI 198
Cdd:cd03225    92 --TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1577416155 199 RKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:cd03225   170 RRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 43-256 1.16e-63

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 212.07  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT---SGEIYIDNEKITQVSSAklreIRRKKIAMVFQNF--ALL 117
Cdd:COG1123    22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA----LRGRRIGMVFQDPmtQLN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHrTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG1123    98 PV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVT 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:COG1123   177 TQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 41-251 3.69e-62

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 200.22  E-value: 3.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHR 120
Cdd:TIGR02315  16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR-IGMIFQHYNLIERL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQKVDV--------EERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:TIGR02315  95 TVLENVLHGRLGYKPTWrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIA 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 193 ALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:TIGR02315 175 SLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
35-267 6.71e-62

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 199.55  E-value: 6.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvSSAKLREIRRKKiAMVFQNF 114
Cdd:PRK09493    9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA-GMVFQQF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFG-LEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:PRK09493   87 YLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 194 LDPLIRKEMQNELLSLQTK-MqkTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDV 267
Cdd:PRK09493  167 LDPELRHEVLKVMQDLAEEgM--TMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
20-250 8.25e-62

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 198.35  E-value: 8.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  20 MISFlekgekkTDLLKKYKHSV-GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAK 98
Cdd:COG2884     1 MIRF-------ENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  99 LREIRRKkIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARAL 178
Cdd:COG2884    74 IPYLRRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 179 ATDADILLMDEAFSALDPlirkEMQNELLSLQT---KMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEE 250
Cdd:COG2884   153 VNRPELLLADEPTGNLDP----ETSWEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 43-253 3.31e-60

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 196.11  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekITQVSSAKLREIRRKkIAMVFQNfallPH--- 119
Cdd:TIGR04520  18 LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK-VGMVFQN----PDnqf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 --RTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:TIGR04520  91 vgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
35-268 1.35e-59

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 197.25  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssaklREIRRKKIAMVFQNF 114
Cdd:PRK11432   14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK11432   88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDVN 268
Cdd:PRK11432  168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDAN 241
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-264 7.43e-58

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 192.94  E-value: 7.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPmqmISflekgekktdllkkykhsvgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:PRK11000    1 MASVTLRNVTKAYGDVV---IS---------------------KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKlreirrKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAK 160
Cdd:PRK11000   57 SGDLFIGEKRMNDVPPAE------RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRK 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 161 PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:PRK11000  131 PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210

                         250       260
                  ....*....|....*....|....
gi 1577416155 241 NIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK11000  211 RVAQVGKPLELYHYPANRFVAGFI 234
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 43-251 1.95e-57

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 187.39  E-value: 1.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE-----PTSGEIYIDNEKITQVSSAKLReiRRKKIAMVFQNFALL 117
Cdd:cd03260    16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE--LRRRVGMVFQKPNPF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PhRTVLENVAFGLEIQKV-DVEERKKKAIEMLEVVGLKGYEN--AKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:cd03260    94 P-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 195 DPLIRKEMqnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:cd03260   173 DPISTAKI--EELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 32-252 3.94e-57

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 186.99  E-value: 3.94e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkitqvSSAKLREIRRKKIAMVF 111
Cdd:COG4555     6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-----DVRKEPREARRQIGVLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:COG4555    81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 192 SALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:COG4555   161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 43-259 5.88e-56

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 184.48  E-value: 5.88e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRkKIAMVFQNFALLPHRTV 122
Cdd:COG1120    17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---RELAR-RIAYVPQEPPAPFGLTV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGL-----EIQKVDVEERkKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG1120    93 RELVALGRyphlgLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP--ADAY 259
Cdd:COG1120   172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPEllEEVY 235
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 45-246 2.23e-55

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 181.72  E-value: 2.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEgEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdNEKITQVSSAKLR-EIRRKKIAMVFQNFALLPHRTVL 123
Cdd:cd03297    16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKKINlPPQQRKIGLVFQQYALFPHLNVR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLeiQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQ 203
Cdd:cd03297    94 ENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 204 NELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03297   172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 32-242 6.22e-55

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 179.13  E-value: 6.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaKLREIRRKKIAMVF 111
Cdd:cd03230     5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-----KEPEEVKRRIGYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVafgleiqkvdveerkkkaiemlevvglkgyenakpkELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03230    80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 192 SALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:cd03230   124 SGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 33-265 7.47e-55

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 181.49  E-value: 7.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG-----EIYIDNEKITQVSSAKLREIRrKKI 107
Cdd:PRK11264    9 LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLIRQLR-QHV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 108 AMVFQNFALLPHRTVLENVAFG-LEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:PRK11264   88 GFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:PRK11264  168 FDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
2-265 7.60e-55

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 181.92  E-value: 7.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   2 AKIQVKNVYKVFGSapmqmisfLE--KGekktdllkkykhsvgvnnVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP 79
Cdd:COG4598     7 PALEVRDLHKSFGD--------LEvlKG------------------VSLTARKGDVISIIGSSGSGKSTFLRCINLLETP 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  80 TSGEIYIDNEKITQVSS-------AKLREIR--RKKIAMVFQNFALLPHRTVLENVAFG-LEIQKVDVEERKKKAIEMLE 149
Cdd:COG4598    61 DSGEIRVGGEEIRLKPDrdgelvpADRRQLQriRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 150 VVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPlirkEMQNELLSLqtkMQ------KTIVFITHD 223
Cdd:COG4598   141 KVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP----ELVGEVLKV---MRdlaeegRTMLVVTHE 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1577416155 224 LDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:COG4598   214 MGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLS 255
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-264 7.88e-55

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 184.66  E-value: 7.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSapmqmisflekgekktdllkkyKHSVgVNNVSFSVNEGEiFVVM-GLSGSGKSTLIRCLNRLIEP 79
Cdd:PRK11650    1 MAGLKLQAVRKSYDG----------------------KTQV-IKGIDLDVADGE-FIVLvGPSGCGKSTLLRMVAGLERI 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  80 TSGEIYIDNEKITQVssaklrEIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVD---VEERKKKAIEMLEvvgLKGY 156
Cdd:PRK11650   57 TSGEIWIGGRVVNEL------EPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPkaeIEERVAEAARILE---LEPL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 157 ENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAI 236
Cdd:PRK11650  128 LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVV 207

                         250       260
                  ....*....|....*....|....*...
gi 1577416155 237 MKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK11650  208 MNGGVAEQIGTPVEVYEKPASTFVASFI 235
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
45-228 1.28e-54

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 181.05  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirrkkiAMVFQNFALLPHRTVLE 124
Cdd:PRK11248   19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRNVQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQN 204
Cdd:PRK11248   90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169

                         170       180
                  ....*....|....*....|....
gi 1577416155 205 ELLSLQTKMQKTIVFITHDLDEAL 228
Cdd:PRK11248  170 LLLKLWQETGKQVLLITHDIEEAV 193
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 33-265 5.43e-54

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 186.81  E-value: 5.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIePTSGEIYIDNEKITQVSSAKLREIRRKkIAMVFQ 112
Cdd:COG4172   292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQ 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 N-FALL-PHRTVLENVAFGLEIQKV--DVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:COG4172   370 DpFGSLsPRMTVGQIIAEGLRVHGPglSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLD--EALkiGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:COG4172   450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRAL--AHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLA 527
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 43-259 6.78e-52

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 174.07  E-value: 6.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFALLPHRTV 122
Cdd:COG0411    20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP---HRIARLGIARTFQNPRLFPELTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQ-------------KVDVEERK--KKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:COG0411    97 LENVLVAAHARlgrgllaallrlpRARREEREarERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA--DAY 259
Cdd:COG0411   177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRviEAY 250
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-265 1.17e-51

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 173.87  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFgsapmqmisflekgEKKTDLLKKyKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:COG4167     2 SALLEVRNLSKTF--------------KYRTGLFRR-QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEKITQVSSAKlreiRRKKIAMVFQ--NFALLPHRTVLENVAFGLEIQ-KVDVEERKKKAIEMLEVVGLKG-Y 156
Cdd:COG4167    67 SGEILINGHKLEYGDYKY----RCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPeH 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 157 ENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAI 236
Cdd:COG4167   143 ANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLV 222

                         250       260
                  ....*....|....*....|....*....
gi 1577416155 237 MKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:COG4167   223 MHQGEVVEYGKTAEVFANPQHEVTKRLIE 251
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 43-256 4.74e-51

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 171.08  E-value: 4.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFALLPHRTV 122
Cdd:cd03219    16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIARLGIGRTFQIPRLFPELTV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKV----------DVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:cd03219    93 LENVMVAAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 193 ALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:cd03219   173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 43-254 8.13e-51

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 171.71  E-value: 8.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvSSAKLREIRrKKIAMVFQNfallPHR-- 120
Cdd:PRK13632   25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIR-KKIGIIFQN----PDNqf 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 ---TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13632   97 igaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK13632  177 GKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
32-242 1.33e-50

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 169.23  E-value: 1.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVF 111
Cdd:COG4619     5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHrTVLENVAFGLEIQKVDVEErkKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:COG4619    81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:COG4619   158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 32-251 3.00e-50

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 168.45  E-value: 3.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYK--HSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssAKLREIRRKKIAM 109
Cdd:cd03263     5 NLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKAARQSLGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDE 189
Cdd:cd03263    80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 190 AFSALDPLIRKEMQNELLSLQTkmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:cd03263   160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 43-251 5.76e-50

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 168.03  E-value: 5.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirrkkiaMVFQNFALLPHRTV 122
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKVDVEERKKKAI--EMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRK 200
Cdd:TIGR01184  72 RENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 201 EMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
43-251 4.61e-49

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 167.50  E-value: 4.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekiTQVSSAKLREIRRKkIAMVFQNfallPHR-- 120
Cdd:PRK13635   23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQ-VGMVFQN----PDNqf 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 ---TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13635   95 vgaTVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEI 251
Cdd:PRK13635  175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 43-192 1.27e-48

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 162.05  E-value: 1.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklREIRRKKIAMVFQNFALLPHRTV 122
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 123 LENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYEN----AKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 43-264 1.73e-48

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 172.18  E-value: 1.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKS----TLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQN--FAL 116
Cdd:COG4172    26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQEpmTSL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEI-QKVDVEERKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:COG4172   106 NPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTT 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 193 ALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:COG4172   186 ALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
 3-244 4.70e-48

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 163.76  E-value: 4.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   3 KIQVKNVYKVFgsapmqmisfleKGEKKtdllkkyKHSVgVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG 82
Cdd:NF040729    1 KLKIQNISKTF------------INNKK-------ENEV-LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  83 EIYIDNEKITQVSSAKlreirrkkiAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:NF040729   61 EILVNGNEVTKPGPDR---------GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPH 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIM--KDG 240
Cdd:NF040729  132 QISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKG 211


                  ....
gi 1577416155 241 NIVQ 244
Cdd:NF040729  212 KILE 215
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 43-264 4.74e-48

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 164.05  E-value: 4.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE--P---TSGEIYIDNEKI--TQVSSAKLReirrKKIAMVFQNFA 115
Cdd:COG1117    27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELR----RRVGMVFQKPN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 LLPHrTVLENVAFGLEIQ----KVDVEERKKKAiemLEVVGLkgYENAKPK------ELSGGMQQRVGLARALATDADIL 185
Cdd:COG1117   103 PFPK-SIYDNVAYGLRLHgiksKSELDEIVEES---LRKAAL--WDEVKDRlkksalGLSGGQQQRLCIARALAVEPEVL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 186 LMDEAFSALDP--------LIRkemqnELlslqtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPAD 257
Cdd:COG1117   177 LMDEPTSALDPistakieeLIL-----EL-----KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246


                  ....*..
gi 1577416155 258 AYVREFI 264
Cdd:COG1117   247 KRTEDYI 253
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
44-255 5.25e-48

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 163.65  E-value: 5.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKI---TQVSSAKLREIRRKkIAMVFQNFALLPHR 120
Cdd:COG4161    19 FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMVFQQYNLWPHL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLEN-VAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:COG4161    98 TVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 200 KEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEpEEILNSP 255
Cdd:COG4161   178 AQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 31-240 3.24e-47

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 158.56  E-value: 3.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAMV 110
Cdd:cd00267     3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQnfallphrtvlenvafgleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd00267    79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 191 FSALDPLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:cd00267   108 TSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
cbiO PRK13650
energy-coupling factor transporter ATPase;
43-251 4.12e-47

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 162.21  E-value: 4.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssAKLREIRRKkIAMVFQNfallPHR-- 120
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDIRHK-IGMVFQN----PDNqf 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 ---TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13650   95 vgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEaLKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:PRK13650  175 GRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 4-244 5.99e-47

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 160.29  E-value: 5.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSapmqmisflekGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:COG4181     9 IELRGLTKTVGT-----------GAGELTILK---------GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDveERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:COG4181    69 VRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIgDRIAIMKDGNIV 243
Cdd:COG4181   147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLV 225


                  .
gi 1577416155 244 Q 244
Cdd:COG4181   226 E 226
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 45-256 7.23e-47

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 163.73  E-value: 7.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkiTQVSSAKLR----EIRRkkIAMVFQNFALLPHR 120
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--VLQDSARGIflppHRRR--IGYVFQEARLFPHL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLeiQKVDVEERKkkaIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG4148    93 SVRGNLLYGR--KRAPRAERR---ISFDEVVELLGIGhllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:COG4148   168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 43-253 3.20e-46

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 168.47  E-value: 3.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTV 122
Cdd:COG2274   491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLF-SGTI 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEiqKVDVEErkkkAIEMLEVVGL--------KGY-----ENAKPkeLSGGMQQRVGLARALATDADILLMDE 189
Cdd:COG2274   566 RENITLGDP--DATDEE----IIEAARLAGLhdfiealpMGYdtvvgEGGSN--LSGGQRQRLAIARALLRNPRILILDE 637

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 190 AFSALDPLIRKEMQNELLSLqtKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:COG2274   638 ATSALDAETEAIILENLRRL--LKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA 698
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 37-256 3.36e-46

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 158.71  E-value: 3.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssaklreiRRKKIAMVFQNFAL 116
Cdd:COG1121    16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------ARRRIGYVPQRAEV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHR--TVLENVAFGLeIQKVDV-----EERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDE 189
Cdd:COG1121    87 DWDFpiTVRDVVLMGR-YGRRGLfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 190 AFSALDPlirkEMQNELLSL---QTKMQKTIVFITHDLDEALKIGDRIAIMKDGnIVQIGEPEEILNSPA 256
Cdd:COG1121   166 PFAGVDA----ATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 30-261 6.05e-46

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 160.52  E-value: 6.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  30 KTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNrLIE-PTSGEIYIDNEKITQVSSAKLREiRRKKIA 108
Cdd:PRK11308   18 KRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLKADPEAQKL-LRQKIQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVFQN-FALL-PHRTVLENVAFGLEIQ-KVDVEERKKKAIEMLEVVGLKGyENAK--PKELSGGMQQRVGLARALATDAD 183
Cdd:PRK11308   96 IVFQNpYGSLnPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRP-EHYDryPHMFSGGQRQRIAIARALMLDPD 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 184 ILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVR 261
Cdd:PRK11308  175 VVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 36-246 7.19e-46

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 155.67  E-value: 7.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  36 KYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreiRRKKIAMVFQnfa 115
Cdd:cd03214     8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 llphrtvlenvafgleiqkvdveerkkkaieMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:cd03214    81 -------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 196 PlirkEMQNELLS----LQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03214   130 I----AHQIELLEllrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
31-265 7.52e-46

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 158.21  E-value: 7.52e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKIT---------QVSSAKLRE 101
Cdd:PRK10619    9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 102 IRRKKIAMVFQNFALLPHRTVLENVAFG-LEIQKVDVEERKKKAIEMLEVVGLKGYENAK-PKELSGGMQQRVGLARALA 179
Cdd:PRK10619   89 LLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 180 TDADILLMDEAFSALDPlirkEMQNELLSLQTKMQ---KTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:PRK10619  169 MEPEVLLFDEPTSALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244


                  ....*....
gi 1577416155 257 DAYVREFIQ 265
Cdd:PRK10619  245 SPRLQQFLK 253
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 45-246 8.16e-46

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 157.87  E-value: 8.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIR--RKKIAMVFQNFALLPHRTV 122
Cdd:PRK11124   20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRelRRNVGMVFQQYNLWPHLTV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LEN-VAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPlirkE 201
Cdd:PRK11124  100 QQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP----E 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1577416155 202 MQNELLSLQTKMQKT-I--VFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:PRK11124  176 ITAQIVSIIRELAETgItqVIVTHEVEVARKTASRVVYMENGHIVEQG 223
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 37-238 3.06e-45

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 155.38  E-value: 3.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaklreirRKKIAMVFQNFAL 116
Cdd:cd03235     9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------RKRIGYVPQRRSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHR--TVLENVAFGLEIQKVDV----EERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03235    80 DRDFpiSVRDVVLMGLYGHKGLFrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 191 FSALDPlirkEMQNELLSLQTKMQ---KTIVFITHDLDEALKIGDRIAIMK 238
Cdd:cd03235   160 FAGVDP----KTQEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLLN 206
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 32-269 3.52e-45

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 156.53  E-value: 3.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNE----------KITQVSSAKLRE 101
Cdd:TIGR03005   5 DVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEqlyhmpgrngPLVPADEKHLRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 102 IRrKKIAMVFQNFALLPHRTVLENVAFG-LEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALAT 180
Cdd:TIGR03005  85 MR-NKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAM 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 181 DADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYV 260
Cdd:TIGR03005 164 RPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERT 243


                  ....*....
gi 1577416155 261 REFIQDVNR 269
Cdd:TIGR03005 244 REFLSKVIA 252
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
45-264 5.50e-45

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 156.46  E-value: 5.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRrKKIAMVFQNFALLPHRTVLE 124
Cdd:PRK11831   25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVDVEERKKKAIEM-LEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQ 203
Cdd:PRK11831  104 NVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 204 NELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPaDAYVREFI 264
Cdd:PRK11831  184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFL 243
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 32-251 5.82e-45

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 154.84  E-value: 5.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklREIRRKkIAMVF 111
Cdd:cd03265     5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVRRR-IGIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03265    80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:cd03265   160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
44-251 6.62e-45

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 161.72  E-value: 6.62e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFALLPHRTVL 123
Cdd:COG1129    21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP---RDAQAAGIAIIHQELNLVPNLSVA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPlirK 200
Cdd:COG1129    98 ENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE---R 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 201 EMQNeLLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:COG1129   175 EVER-LFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 32-223 1.09e-44

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 153.72  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSV-GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIAMV 110
Cdd:cd03292     5 NVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03292    84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1577416155 191 FSALDPLIRKEMQNeLLSLQTKMQKTIVFITHD 223
Cdd:cd03292   164 TGNLDPDTTWEIMN-LLKKINKAGTTVVVATHA 195
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 34-246 1.87e-44

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 153.03  E-value: 1.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  34 LKKYKHSVGVNNVSFSVN--EGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAklreirRKKIAMVF 111
Cdd:cd03298     3 LDKIRFSYGEQPMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLeIQKVDVEERKKKAIE-MLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03298    77 QENNLFAHLTVEQNVGLGL-SPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03298   156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
43-252 3.30e-44

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 161.49  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTV 122
Cdd:COG1132   356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTI 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFG-LEIQKVDVEERKKKA-----IEMLE-----VVGLKGYenakpkELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:COG1132   431 RENIRYGrPDATDEEVEEAAKAAqahefIEALPdgydtVVGERGV------NLSGGQRQRIAIARALLKDPPILILDEAT 504

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 192 SALDPlirkemQNELL---SLQTKMQ-KTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:COG1132   505 SALDT------ETEALiqeALERLMKgRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELL 562
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 45-257 5.37e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 154.41  E-value: 5.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKIT-QVSSAKLREIRrKKIAMVFQnF--ALLPHRT 121
Cdd:PRK13634   25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLR-KKVGIVFQ-FpeHQLFEET 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAFGLEIQKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRK 200
Cdd:PRK13634  103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 201 EMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPAD 257
Cdd:PRK13634  183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 43-240 8.09e-44

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 150.23  E-value: 8.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTV 122
Cdd:cd03228    18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVafgleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEM 202
Cdd:cd03228    93 RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1577416155 203 QNELLSLqtKMQKTIVFITHDLdEALKIGDRIAIMKDG 240
Cdd:cd03228   136 LEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDG 170
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 46-256 1.21e-43

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 155.27  E-value: 1.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkITQVSSAKLR-EIRRKKIAMVFQNFALLPHRTVLE 124
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRKGIFlPPEKRRIGYVFQEARLFPHLSVRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLeiQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQN 204
Cdd:TIGR02142  95 NLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 205 ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
PhnK COG4107
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ...
 41-259 2.76e-43

ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];


Pssm-ID: 443283 [Multi-domain]  Cd Length: 262  Bit Score: 151.50  E-value: 2.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEK-----ITQVSSAKLREIRRKKIAMVFQN-- 113
Cdd:COG4107    26 VACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprdLFALSEAERRRLRRTDWGMVYQNpr 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 114 FALLPHRTVLENVAFGLeiqkVDVEER-----KKKAIEMLEVVglkgyE------NAKPKELSGGMQQRVGLARALATDA 182
Cdd:COG4107   106 DGLRMDVSAGGNIAERL----MAAGERhygdiRARALEWLERV-----EipleriDDLPRTFSGGMQQRVQIARALVTNP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 183 DILLMDEAFSALD--------PLIRKemqnellsLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG4107   177 RLLFLDEPTTGLDvsvqarllDLIRR--------LQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLED 248


                  ....*
gi 1577416155 255 PADAY 259
Cdd:COG4107   249 PQHPY 253
cbiO PRK13637
energy-coupling factor transporter ATPase;
40-253 3.83e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 152.12  E-value: 3.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  40 SVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvSSAKLREIRrKKIAMVFQ--NFALL 117
Cdd:PRK13637   20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQypEYQLF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 pHRTVLENVAFG---LEIQKVDVEERKKKAIEMlevVGLK--GYENAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:PRK13637   98 -EETIEKDIAFGpinLGLSEEEIENRVKRAMNI---VGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 193 ALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK13637  174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 18-252 4.18e-43

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 157.66  E-value: 4.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  18 MQMISFLEKGEK--------KTDLLKKYKHSV------GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:TIGR03269 261 MEGVSEVEKECEvevgepiiKVRNVSKRYISVdrgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IY--IDNEKITQVSSAKLREIRRKK-IAMVFQNFALLPHRTVLENV--AFGLEIQKvdvEERKKKAIEMLEVVGLKGYE- 157
Cdd:TIGR03269 341 VNvrVGDEWVDMTKPGPDGRGRAKRyIGILHQEYDLYPHRTVLDNLteAIGLELPD---ELARMKAVITLKMVGFDEEKa 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 158 ----NAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDR 233
Cdd:TIGR03269 418 eeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497

                         250
                  ....*....|....*....
gi 1577416155 234 IAIMKDGNIVQIGEPEEIL 252
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEIV 516
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 43-250 1.39e-42

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 148.40  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP---TSGEIYIDNEKITQVSsaklreIRRKKIAMVFQNFALLPH 119
Cdd:COG4136    17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP------AEQRRIGILFQDDLLFPH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGL--EIQKvdvEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG4136    91 LSVGENLAFALppTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 198 IRKEMQnELLSLQTKMQKTIV-FITHDLDEALkigdriaimKDGNIVQIGEPEE 250
Cdd:COG4136   168 LRAQFR-EFVFEQIRQRGIPAlLVTHDEEDAP---------AAGRVLDLGNWQH 211
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
47-258 1.73e-42

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 148.58  E-value: 1.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  47 SFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAklreirRKKIAMVFQNFALLPHRTVLENV 126
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 127 AFGLEIQ-KVDVEERKKKAiEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNE 205
Cdd:PRK10771   93 GLGLNPGlKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 206 LLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADA 258
Cdd:PRK10771  172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
25-244 1.60e-41

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 146.11  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  25 EKGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRR 104
Cdd:PRK11629   16 QEGSVQTDVLH---------NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 KKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADI 184
Cdd:PRK11629   87 QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIgDRIAIMKDGNIVQ 244
Cdd:PRK11629  167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 35-254 4.11e-41

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 147.18  E-value: 4.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaklREIRRKkiamvfqnF 114
Cdd:COG4152     9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRR--------I 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPH-R------TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:COG4152    74 GYLPEeRglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG4152   154 DEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 31-227 5.06e-41

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 143.77  E-value: 5.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaklREIRRKKIAMV 110
Cdd:COG4133     6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-----REDYRRRLAYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKkkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:COG4133    81 GHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1577416155 191 FSALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEA 227
Cdd:COG4133   159 FTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL 194
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 35-242 5.25e-41

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 145.59  E-value: 5.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYidnekitqVSSAKLREIRrKKIAMVFQNF 114
Cdd:PRK11247   20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAR-EDTRLMFQDA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEiqkvdvEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK11247   91 RLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK11247  165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
 35-339 6.21e-41

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 146.77  E-value: 6.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssaKLREIRRKkIAMVFQNF 114
Cdd:TIGR01188   1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRS-IGIVPQYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:TIGR01188  76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 195 DPLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQDV-NRTKIV 273
Cdd:TIGR01188 156 DPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIqSLKVEV 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 274 SASSIMrssesiILEKAGVRTAAKKMKDleissifvTDKHKTLLGIITIDKVSELMKENRDDLKSV 339
Cdd:TIGR01188 235 SMLIAE------LGETGLGLLAVTVDSD--------RIKILVPDGDETVPEIVEAAIRNGIRIRSI 286
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 43-265 6.90e-41

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 152.23  E-value: 6.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAMVFQNFALLpHRTV 122
Cdd:COG4987   351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR----RIAVVPQRPHLF-DTTL 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEiqKVDVEErkkkAIEMLEVVGLKGYENAKPK-------E----LSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:COG4987   426 RENLRLARP--DATDEE----LWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDAPILLLDEPT 499

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 192 SALDPLIRKEMQNELLSLQTkmQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNspADAYVREFIQ 265
Cdd:COG4987   500 EGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 43-254 7.98e-41

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 151.83  E-value: 7.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNfALLPHRTV 122
Cdd:COG4988   353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQN-PYLFAGTI 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGleiqKVDV-EERKKKAIE---MLEVV-GL-KGY-----ENAKPkeLSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:COG4988   428 RENLRLG----RPDAsDEELEAALEaagLDEFVaALpDGLdtplgEGGRG--LSGGQAQRLALARALLRDAPLLLLDEPT 501

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDPLIRKEMQNELLSLQTkmQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG4988   502 AHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 32-262 1.65e-40

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 143.45  E-value: 1.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsakLREIRRKKIAMVF 111
Cdd:cd03218     5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MHKRARLGIGYLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03218    82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDPLIRKEMQNELLSLQtkmQKTI-VFIT-HDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPAdayVRE 262
Cdd:cd03218   162 AGVDPIAVQDIQKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL---VRK 228
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 43-261 3.22e-40

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 145.62  E-value: 3.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRrKKIAMVFQN--FALLPHR 120
Cdd:PRK15079   37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEI--QKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK15079  116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVR 261
Cdd:PRK15079  196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 44-250 4.33e-40

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 149.02  E-value: 4.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFALLPHRTVL 123
Cdd:COG3845    22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP---RDAIALGIGMVHQHFMLVPNLTVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLE---IQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRK 200
Cdd:COG3845    99 ENIVLGLEptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEAD 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 201 EMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEE 250
Cdd:COG3845   179 ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 37-253 5.88e-40

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 141.80  E-value: 5.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFAL 116
Cdd:cd03224    10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP---HERARAGIGYVPEGRRI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQ-KVDVEERKKKAIEMLEVvgLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:cd03224    87 FPELTVEENLLLGAYARrRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 196 PLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:cd03224   165 PKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 46-255 6.51e-40

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 142.36  E-value: 6.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE-----PTSGEIYIDNEKITQVSSAKLReirrKKIAMVFQNFALLPHR 120
Cdd:PRK14247   22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR----RRVQMVFQIPNPIPNL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQKV-----DVEERKKKAIEMLEVVG-LKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK14247   98 SIFENVALGLKLNRLvkskkELQERVRWALEKAQLWDeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 195 DPLIRKEMQNELLSLQTKMqkTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK14247  178 DPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 29-243 9.50e-40

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 140.82  E-value: 9.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  29 KKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAklreirRKKIA 108
Cdd:cd03268     2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVFQNFALLPHRTVLENV-AFGLEIQKvdveeRKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:cd03268    76 ALIEAPGFYPNLTARENLrLLARLLGI-----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03268   151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 43-254 1.65e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 141.81  E-value: 1.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssAKLREIRrKKIAMVFQNfallPHR-- 120
Cdd:PRK13648   25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKLR-KHIGIVFQN----PDNqf 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 ---TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13648   97 vgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK13648  177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 3-253 2.31e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 142.53  E-value: 2.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   3 KIQVKNVYKVFgsapmqmisflekgEKKTDLLKKykhsvGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG 82
Cdd:PRK13651    2 QIKVKNIVKIF--------------NKKLPTELK-----ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  83 EI---YIDNEKITQ------------VSSAKLREIR-----RKKIAMVFQnFA--LLPHRTVLENVAFGLEIQKVDVEER 140
Cdd:PRK13651   63 TIewiFKDEKNKKKtkekekvleklvIQKTRFKKIKkikeiRRRVGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEEA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 141 KKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQtKMQKTIVF 219
Cdd:PRK13651  142 KKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIIL 220

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1577416155 220 ITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK13651  221 VTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 32-263 3.74e-39

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 140.16  E-value: 3.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreiR-RKKI--- 107
Cdd:COG1137     8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK----RaRLGIgyl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 108 ---AMVFQNFallphrTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADI 184
Cdd:COG1137    84 pqeASIFRKL------TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLQtkmQKTI-VFIT-HDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPAdayVRE 262
Cdd:COG1137   158 ILLDEPFAGVDPIAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL---VRK 231


                  .
gi 1577416155 263 F 263
Cdd:COG1137   232 V 232
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 32-255 7.71e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 140.21  E-value: 7.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKY-KHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirRKKIAMV 110
Cdd:PRK13639    6 DLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV--RKTVGIV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQN-----FAllphRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK13639   84 FQNpddqlFA----PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 186 LMDEAFSALDPLIRKEMQNeLLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK13639  160 VLDEPTSGLDPMGASQIMK-LLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 44-253 2.81e-38

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 137.75  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTVL 123
Cdd:cd03253    18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLF-NDTIG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFG-LEIQKVDVEERKKKAIEMLEVVGL-KGYeNAKPKE----LSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:cd03253    93 YNIRYGrPDATDEEVIEAAKAAQIHDKIMRFpDGY-DTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 198 IRKEMQNELLSLQTKmqKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:cd03253   172 TEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
cbiO PRK13641
energy-coupling factor transporter ATPase;
42-255 3.06e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 139.19  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKIT-QVSSAKLREIrRKKIAMVFQnF--ALLP 118
Cdd:PRK13641   22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKL-RKKVSLVFQ-FpeAQLF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 HRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13641  100 ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 198 IRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK13641  180 GRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 32-246 3.09e-38

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 136.64  E-value: 3.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaklrEIRRKKIAMVF 111
Cdd:cd03269     5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--------IAARNRIGYLP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03269    77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03269   157 SGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
35-251 4.65e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 138.30  E-value: 4.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekITQVSSAKLREIRRKKiAMVFQNf 114
Cdd:PRK13633   18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKA-GMVFQN- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 allPHRT-----VLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDE 189
Cdd:PRK13633   94 ---PDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 190 AFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEI 251
Cdd:PRK13633  171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
33-244 1.08e-37

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 137.13  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIAMVFQ 112
Cdd:PRK10419   18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 NF--ALLPHRTVLENVAFGLE-IQKVDVEERKKKAIEMLEVVGLKGYENAK-PKELSGGMQQRVGLARALATDADILLMD 188
Cdd:PRK10419   97 DSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 189 EAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQ 244
Cdd:PRK10419  177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 35-243 1.99e-37

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 132.94  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKitqVSSAKLREIRRKKIAMVFQnf 114
Cdd:cd03216     8 KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---VSFASPRDARRAGIAMVYQ-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 allphrtvlenvafgleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:cd03216    83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 195 DPlirKEMQN--ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03216   114 TP---AEVERlfKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 30-267 2.15e-37

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 143.07  E-value: 2.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  30 KTDLLKKYKHSV-GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIA 108
Cdd:PRK10261  326 RSGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQ 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVFQN--FALLPHRTVLENVAFGLEIQKV-DVEERKKKAIEMLEVVGLKGyENA--KPKELSGGMQQRVGLARALATDAD 183
Cdd:PRK10261  405 FIFQDpyASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPK 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 184 ILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREF 263
Cdd:PRK10261  484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKL 563


                  ....
gi 1577416155 264 IQDV 267
Cdd:PRK10261  564 MAAV 567
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 31-246 1.28e-36

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 132.70  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGeIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaKLREIRRKKIAMV 110
Cdd:cd03264     4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-----KQPQKLRRRIGYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03264    78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTkmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03264   158 TAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 39-265 1.85e-36

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 139.46  E-value: 1.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  39 HSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIePTSGEIYIDNEKITQVSSAKLREIRRKkIAMVFQ--NFAL 116
Cdd:PRK15134  298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSL 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQK--VDVEERKKKAIEMLEVVGLKGYENAK-PKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:PRK15134  376 NPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 194 LDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQ 265
Cdd:PRK15134  456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 32-264 3.97e-36

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 132.59  E-value: 3.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRL--IEP---TSGEIYIDNEKI--TQVSSAKLReirr 104
Cdd:PRK14239   10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLR---- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 KKIAMVFQNFALLPHrTVLENVAFGLEIQKVDVEERKKKAIEMlEVVGLKGYENAKPK------ELSGGMQQRVGLARAL 178
Cdd:PRK14239   86 KEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 179 ATDADILLMDEAFSALDPLIRKEMQNELLSLqtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADA 258
Cdd:PRK14239  164 ATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241


                  ....*.
gi 1577416155 259 YVREFI 264
Cdd:PRK14239  242 ETEDYI 247
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
43-259 1.39e-35

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 131.01  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRrkkiAMVFQ----NFALlp 118
Cdd:COG4559    17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR----AVLPQhsslAFPF-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 hrTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALA-----TDAD--ILLMDEAF 191
Cdd:COG4559    91 --TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPT 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDPLirkeMQNELLSLQ---TKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP--ADAY 259
Cdd:COG4559   169 SALDLA----HQHAVLRLArqlARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEllERVY 237
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 45-252 1.88e-35

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 130.04  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAMVFQNFALLPhRTVLE 124
Cdd:cd03254    21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVLQDTFLFS-GTIME 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVDVEERKKKAIEMLEVV-----GLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:cd03254    96 NIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 200 KEMQNELLSLQTkmQKTIVFITHDLDeALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:cd03254   176 KLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
cbiO PRK13646
energy-coupling factor transporter ATPase;
37-263 2.22e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 131.44  E-value: 2.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHsVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvSSAKLREIR--RKKIAMVFQnF 114
Cdd:PRK13646   18 YEH-QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT--HKTKDKYIRpvRKRIGMVFQ-F 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 --ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK13646   94 peSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSpaDAYVREF 263
Cdd:PRK13646  174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
30-264 3.90e-35

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 130.29  E-value: 3.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  30 KTDLLKKYkHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAklreIRRKKIAM 109
Cdd:PRK15112   17 RTGWFRRQ-TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQRIRM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQN--FALLPHRTVLENVAFGLEIQ-KVDVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK15112   92 IFQDpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVI 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 186 LMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK15112  172 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 37-259 7.98e-35

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 128.56  E-value: 7.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAklrEIRRKKIAMVFQNFAL 116
Cdd:COG0410    13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH---RIARLGIGYVPEGRRI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEI--QKVDVEERKKKAIEMLEVvgLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:COG0410    90 FPSLTVEENLLLGAYArrDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 195 DPLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA--DAY 259
Cdd:COG0410   168 APLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEvrEAY 233
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-253 9.18e-35

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 128.66  E-value: 9.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAK-IQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP 79
Cdd:COG1134     1 MSSmIEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWAL--KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  80 TSGEIyidnekitqvssaklreIRRKKIAmvfqnfALL-------PHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVG 152
Cdd:COG1134    79 TSGRV-----------------EVNGRVS------ALLelgagfhPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAE 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 153 LKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGD 232
Cdd:COG1134   136 LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCD 214

                         250       260
                  ....*....|....*....|.
gi 1577416155 233 RIAIMKDGNIVQIGEPEEILN 253
Cdd:COG1134   215 RAIWLEKGRLVMDGDPEEVIA 235
cbiO PRK13642
energy-coupling factor transporter ATPase;
32-257 9.30e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 129.44  E-value: 9.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNN---VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIA 108
Cdd:PRK13642    9 NLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR----RKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVFQN-FALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK13642   85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILNSPAD 257
Cdd:PRK13642  165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 43-262 1.26e-34

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 128.57  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreIRRKKIAMVFQNFALLPHRTV 122
Cdd:PRK11300   21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ---IARMGVVRTFQHVRLFREMTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVafgLEIQKVDVE----------------ERKK--KAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADI 184
Cdd:PRK11300   98 IENL---LVAQHQQLKtglfsgllktpafrraESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA--DAYVRE 262
Cdd:PRK11300  175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDviKAYLGE 254
cbiO PRK13644
energy-coupling factor transporter ATPase;
43-256 1.44e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 128.95  E-value: 1.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekITQVSSAKLREIRrKKIAMVFQNfallPH--- 119
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIR-KLVGIVFQN----PEtqf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 --RTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:PRK13644   91 vgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 198 IRKEMQNELLSLQTKmQKTIVFITHDLDEaLKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:PRK13644  171 SGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
43-252 1.56e-34

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 128.21  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKkiamvfqnFALLPHR-- 120
Cdd:PRK11231   18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARR--------LALLPQHhl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 -----TVLENVAFG----LEI-QKVDVEERKK--KAIEMLEVVGLKgyeNAKPKELSGGMQQRVGLARALATDADILLMD 188
Cdd:PRK11231   87 tpegiTVRELVAYGrspwLSLwGRLSAEDNARvnQAMEQTRINHLA---DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 189 EAFSALDplirKEMQNELLSLQTKMQ---KTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK11231  164 EPTTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 43-295 1.67e-34

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 134.98  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYID-------NEKITQV---SSAKLREIRRKKIAMVFQ 112
Cdd:PRK10261   32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELseqSAAQMRHVRGADMAMIFQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 N--FALLPHRTVLENVAFGLEI-QKVDVEERKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:PRK10261  112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFIQD 266
Cdd:PRK10261  192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271

                         250       260
                  ....*....|....*....|....*....
gi 1577416155 267 VNRTKIVSASSIMRSSESIILEKAGVRTA 295
Cdd:PRK10261  272 VPQLGAMKGLDYPRRFPLISLEHPAKQEP 300
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 44-252 2.73e-34

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 127.27  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLPhRTVL 123
Cdd:cd03249    20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFD-GTIA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGL-EIQKVDVEERKKKA-----IEML-----EVVGLKGyenakpKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:cd03249    95 ENIRYGKpDATDEEVEEAAKKAnihdfIMSLpdgydTLVGERG------SQLSGGQKQRIAIARALLRNPKILLLDEATS 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 193 ALDPLIRKEMQNELlsLQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:cd03249   169 ALDAESEKLVQEAL--DRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
27-354 2.83e-34

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 134.47  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  27 GEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKK 106
Cdd:PRK10535   17 GEEQVEVLK---------GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 107 IAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:PRK10535   88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKMQkTIVFITHDLDEALKiGDRIAIMKDGNIVQigepeeilNSPADAYVREFIQD 266
Cdd:PRK10535  168 ADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIVR--------NPPAQEKVNVAGGT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 267 VNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLeissifvtdkhKTLLGIIT-IDKVSELMKENrDDLKSVIDTDIR 345
Cdd:PRK10535  238 EPVVNTASGWRQFVSGFREALTMAWRAMAANKMRTL-----------LTMLGIIIgIASVVSIVVVG-DAAKQMVLADIR 305


                  ....*....
gi 1577416155 346 TVGVDTsID 354
Cdd:PRK10535  306 AIGTNT-ID 313
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 43-254 3.00e-34

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 127.51  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSG-EIYIDNEKITQVSsakLREIRrKKIAMV---FQNFaLLP 118
Cdd:COG1119    19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWELR-KRIGLVspaLQLR-FPR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 HRTVLENVAFGLE--I---QKVDVEERKKkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:COG1119    94 DETVLDVVLSGFFdsIglyREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 194 LDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG1119   173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
cbiO PRK13640
energy-coupling factor transporter ATPase;
43-255 6.82e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 127.22  E-value: 6.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE---IYIDNEKITQVSSAKLREirrkKIAMVFQNfallPH 119
Cdd:PRK13640   23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE----KVGIVFQN----PD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 R-----TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK13640   95 NqfvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 195 DPLIRKEMQNELLSLQTKMQKTIVFITHDLDEAlKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK13640  175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
cbiO PRK13645
energy-coupling factor transporter ATPase;
42-254 1.05e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 127.05  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqVSSAKLREIR--RKKIAMVFQ--NFALL 117
Cdd:PRK13645   26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP-ANLKKIKEVKrlRKEIGLVFQfpEYQLF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 pHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:PRK13645  105 -QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 197 LIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK13645  184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 4-246 1.43e-33

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 124.95  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSAPMQMISFLEKGEKKTDLLKKYKHSVgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03220     1 IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWAL--KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IYIDNekitQVSSaklreirrkkiaMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKE 163
Cdd:cd03220    79 VTVRG----RVSS------------LLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03220   143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221


                  ...
gi 1577416155 244 QIG 246
Cdd:cd03220   222 FDG 224
cbiO PRK13643
energy-coupling factor transporter ATPase;
45-252 1.78e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 126.39  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekITQVSSAKLREIR--RKKIAMVFQ-NFALLPHRT 121
Cdd:PRK13643   24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGD--IVVSSTSKQKEIKpvRKKVGVVFQfPESQLFEET 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAFGLEIQKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRK 200
Cdd:PRK13643  102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 201 EMQNELLSLQTKMQkTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK13643  182 EMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 43-264 2.02e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 125.53  E-value: 2.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTS-----GEIYIDNEKITQvSSAKLREIRRKkIAMVFQNFALL 117
Cdd:PRK14258   23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVNLNRLRRQ-VSMVHPKPNLF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PhRTVLENVAFGLEI----QKVDVE---ERKKKAIEMLEVVGLKGYENAKpkELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:PRK14258  101 P-MSVYDNVAYGVKIvgwrPKLEIDdivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEP 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKD-----GNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK14258  178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYV 256
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 43-255 5.26e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 124.18  E-value: 5.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE-----PTSGEIYIDNEKITqvsSAKLREIR-RKKIAMVFQNFAL 116
Cdd:PRK14267   20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIY---SPDVDPIEvRREVGMVFQYPNP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQKV-----DVEERK----KKAIEMLEVvglKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK14267   97 FPHLTIYDNVAIGVKLNGLvkskkELDERVewalKKAALWDEV---KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLqtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
cbiO PRK13649
energy-coupling factor transporter ATPase;
45-251 5.66e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 124.86  E-value: 5.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvSSAKLREIR--RKKIAMVFQnFA--LLPHR 120
Cdd:PRK13649   25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT--STSKNKDIKqiRKKVGLVFQ-FPesQLFEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:PRK13649  102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 200 KemqnELLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:PRK13649  182 K----ELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 31-246 2.39e-32

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 121.32  E-value: 2.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKY----KHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekiTQVSSAKlREIRRkK 106
Cdd:cd03266     5 DALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEP-AEARR-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 107 IAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:cd03266    80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 187 MDEAFSALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03266   160 LDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 21-243 2.58e-32

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 120.82  E-value: 2.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  21 ISFleKGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssaKLR 100
Cdd:cd03226     5 ISF--SYKKGTEILD---------DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 101 EiRRKKIAMVFQNfallPHR-----TVLENVAFGLEiqkvDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLA 175
Cdd:cd03226    68 E-RRKSIGYVMQD----VDYqlftdSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 176 RALATDADILLMDEAFSALDpliRKEMQN--ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03226   139 AALLSGKDLLIFDEPTSGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 32-255 2.92e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 122.99  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGV-NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssAKLREIRrKKIAMV 110
Cdd:PRK13652    8 DLCYSYSGSKEAlNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVR-KFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQN-----FAllphRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK13652   84 FQNpddqiFS----PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 186 LMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK13652  160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
32-254 4.70e-32

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 122.99  E-value: 4.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklrEIRRKKIAMVF 111
Cdd:PRK13537   12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----RHARQRVGVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVA-----FGLEIQKVdveerKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:PRK13537   87 QFDNLDPDFTVRENLLvfgryFGLSAAAA-----RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK13537  162 LDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 41-256 1.33e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 122.27  E-value: 1.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKI-------TQVSSAKLREIR-----RKKIA 108
Cdd:PRK13631   40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhELITNPYSKKIKnfkelRRRVS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVFQ--NFALLpHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK13631  120 MVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 186 LMDEAFSALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:PRK13631  199 IFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 43-264 1.33e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 120.54  E-value: 1.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNE------KITQVSSAKLReirrKKIAMVFQNFAL 116
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLR----KEVGMVFQQPNP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQKV-DVEERKKKAIEMLEVVGL--KGYE--NAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK14246  102 FPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkEVYDrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMqkTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK14246  182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 43-252 2.00e-31

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 119.26  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNfALLPHRTV 122
Cdd:cd03251    18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQD-VFLFNDTV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFG-LEIQKVDVEERKKKA-----IEMLE-----VVGLKGYenakpkELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03251    93 AENIAYGrPGATREEVEEAARAAnahefIMELPegydtVIGERGV------KLSGGQRQRIAIARALLKDPPILILDEAT 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 192 SALDPLIRKEMQNELLSLQtKMQKTIVfITHDLdEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:cd03251   167 SALDTESERLVQAALERLM-KNRTTFV-IAHRL-STIENADRIVVLEDGKIVERGTHEELL 224
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 43-269 5.87e-31

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 120.62  E-value: 5.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE-P---TSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQN--FAL 116
Cdd:PRK11022   23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEI-QKVDVEERKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:PRK11022  103 NPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 193 ALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVR-------EFIQ 265
Cdd:PRK11022  183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQallralpEFAQ 262


                  ....
gi 1577416155 266 DVNR 269
Cdd:PRK11022  263 DKAR 266
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 43-253 7.71e-31

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 118.34  E-value: 7.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRrkkiAMVFQNFALLPHRTV 122
Cdd:PRK13548   18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFPFTV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALA--TDAD----ILLMDEAFSALDP 196
Cdd:PRK13548   94 EEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlWEPDgpprWLLLDEPTSALDL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 197 LirkeMQNELL----SLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK13548  174 A----HQHHVLrlarQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 43-252 1.30e-30

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 123.29  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaKLREIRRKkIAMVFQNFALLpHRTV 122
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLRRQ-VALVSQDVVLF-NDTI 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKVDVE-ERKKKAIEMLEVV-----GLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:TIGR02203 423 ANNIAYGRTEQADRAEiERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 197 LIRKEMQNellSLQTKMQ-KTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:TIGR02203 503 ESERLVQA---ALERLMQgRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELL 555
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 37-264 2.04e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 117.58  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNR---LIEP--TSGEIYIDNEKI--TQVSSAklrEIRRKkIAM 109
Cdd:PRK14243   20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLyaPDVDPV---EVRRR-IGM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPhRTVLENVAFGLEIQ--KVD----VEERKKKAIEMLEVvglKGYENAKPKELSGGMQQRVGLARALATDAD 183
Cdd:PRK14243   96 VFQKPNPFP-KSIYDNIAYGARINgyKGDmdelVERSLRQAALWDEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 184 ILLMDEAFSALDPLirKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIM---------KDGNIVQIGEPEEILNS 254
Cdd:PRK14243  172 VILMDEPCSALDPI--STLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNS 249

                         250
                  ....*....|
gi 1577416155 255 PADAYVREFI 264
Cdd:PRK14243  250 PQQQATRDYV 259
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 43-242 3.37e-30

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 114.45  E-value: 3.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMV---FQNFALLPH 119
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDAIRAGIAYVpedRKREGLVLD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGLEiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:cd03215    93 LSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 200 KEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:cd03215   141 AEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 33-259 3.47e-30

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 116.47  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNE-----KITQVSSAKLREIRRKKI 107
Cdd:TIGR02323   9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAERRRLMRTEW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 108 AMVFQNfallPHRTVLENVAFGLEIQK--VDVEER-----KKKAIEMLEVVGL-KGYENAKPKELSGGMQQRVGLARALA 179
Cdd:TIGR02323  89 GFVHQN----PRDGLRMRVSAGANIGErlMAIGARhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 180 TDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAY 259
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPY 244
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 41-240 4.18e-30

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 115.61  E-value: 4.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYID-NEKITQVSSAKLREI---RRKKIAMVFQNFAL 116
Cdd:COG4778    25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQASPREIlalRRRTIGYVSQFLRV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLkgyenakPKEL--------SGGMQQRVGLARALATDADILLMD 188
Cdd:COG4778   105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGGEQQRVNIARGFIADPPLLLLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 189 EAFSALDPLIR---KEMQNELLSLQTkmqkTIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:COG4778   178 EPTASLDAANRavvVELIEEAKARGT----AIIGIFHDEEVREAVADRVVDVTPF 228
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
31-253 5.65e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 118.01  E-value: 5.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvSSAKLReirRKKIAMV 110
Cdd:PRK13536   45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLA---RARIGVV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLEN-VAFGleiQKVDVEERKKKAI--EMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK13536  120 PQFDNLDLEFTVRENlLVFG---RYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK13536  197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
18-271 6.21e-30

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 116.27  E-value: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  18 MQMISFLEKgekktdLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE-PTSGEIYIDNEKITQVSS 96
Cdd:PRK09984    1 MQTIIRVEK------LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgDKSAGSHIELLGRTVQRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  97 AKL-REIR--RKKIAMVFQNFALLPHRTVLENVAFGL--------EIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELS 165
Cdd:PRK09984   75 GRLaRDIRksRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 166 GGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQI 245
Cdd:PRK09984  155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234

                         250       260
                  ....*....|....*....|....*.
gi 1577416155 246 GEPEEILNSPADAYVRefiqDVNRTK 271
Cdd:PRK09984  235 GSSQQFDNERFDHLYR----SINRVE 256
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 31-273 1.09e-29

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 115.18  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAMV 110
Cdd:COG4604     5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRLAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFG--------LEiqkvdvEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDA 182
Cdd:COG4604    81 RQENHINSRLTVRELVAFGrfpyskgrLT------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 183 DILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP--ADAYV 260
Cdd:COG4604   155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEvlSDIYD 234

                         250
                  ....*....|....
gi 1577416155 261 REF-IQDVNRTKIV 273
Cdd:COG4604   235 TDIeVEEIDGKRIC 248
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 44-265 1.68e-29

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 119.93  E-value: 1.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAMVFQNFALLPHrTVL 123
Cdd:PRK11160  357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFSA-TLR 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLEiqkvdvEERKKKAIEMLEVVGL-KGYENAKP---------KELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:PRK11160  432 DNLLLAAP------NASDEALIEVLQQVGLeKLLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 194 LDplirKEMQNELLSL--QTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNspADAYVREFIQ 265
Cdd:PRK11160  506 LD----AETERQILELlaEHAQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA--QQGRYYQLKQ 572
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
58-256 1.88e-29

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 116.90  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  58 VMGLSGSGKSTLIRCLNRLIEPTSGEIYI------DNEKITQVSSAKlreirrKKIAMVFQNFALLPHRTVLENVAFGLe 131
Cdd:PRK11144   29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEK------RRIGYVFQDARLFPHYKVRGNLRYGM- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 132 iqkvdveeRKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDpLIRKemqNELLS 208
Cdd:PRK11144  102 --------AKSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRK---RELLP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 209 -LQTKMQKT---IVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPA 256
Cdd:PRK11144  170 yLERLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 43-242 3.21e-29

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 111.54  E-value: 3.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIrrkkIAMVFQNFALLPHrTV 122
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH----VGYLPQDDELFSG-SI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVafgleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSALDPlIRKEM 202
Cdd:cd03246    93 AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV-EGERA 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1577416155 203 QNELLSLQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNI 242
Cdd:cd03246   135 LNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 45-254 3.48e-29

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 113.35  E-value: 3.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTVLE 124
Cdd:cd03252    20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQENVLF-NRSIRD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQKVD-VEERKKKA------IEMLE----VVGLKGyenakpKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:cd03252    95 NIALADPGMSMErVIEAAKLAgahdfiSELPEgydtIVGEQG------AGLSGGQRQRIAIARALIHNPRILIFDEATSA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 194 LDplirkeMQNElLSLQTKMQK-----TIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:cd03252   169 LD------YESE-HAIMRNMHDicagrTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 43-264 3.93e-29

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 118.65  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKS-TLIRCLNRLIEP----TSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQN--FA 115
Cdd:PRK15134   25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 LLPHRTVLENVAFGLEIQK-VDVEERKKKAIEMLEVVGL---KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK15134  105 LNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK15134  185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 46-256 4.92e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 114.06  E-value: 4.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssAKLREIRrKKIAMVFQN-----FALlphr 120
Cdd:PRK13647   24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVR-SKVGLVFQDpddqvFSS---- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLiRK 200
Cdd:PRK13647   96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQ 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 201 EMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPeEILNSPA 256
Cdd:PRK13647  175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 44-252 5.89e-29

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 118.77  E-value: 5.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIrrkkIAMVfqnfallPHRTVL 123
Cdd:COG5265   375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIV-------PQDTVL 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ------ENVAFG-LEIQKVDVEERKKKA-----IEMLE-----VV---GLKgyenakpkeLSGGMQQRVGLARALATDAD 183
Cdd:COG5265   444 fndtiaYNIAYGrPDASEEEVEAAARAAqihdfIESLPdgydtRVgerGLK---------LSGGEKQRVAIARTLLKNPP 514

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 184 ILLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVfITHDLD---EAlkigDRIAIMKDGNIVQIGEPEEIL 252
Cdd:COG5265   515 ILIFDEATSALDSRTERAIQAALREV-ARGRTTLV-IAHRLStivDA----DEILVLEAGRIVERGTHAELL 580
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-243 6.48e-29

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 113.26  E-value: 6.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVF--GSApmqmisfLEKgekktdllkkykhsVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTS 81
Cdd:COG1101     2 LELKNLSKTFnpGTV-------NEK--------------RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDS 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  82 GEIYIDNEKITQVSSAKlreiRRKKIAMVFQNFAL--LPHRTVLENVA----------FGLEIQKvdveERKKKAIEMLE 149
Cdd:COG1101    61 GSILIDGKDVTKLPEYK----RAKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrrgLRRGLTK----KRRELFRELLA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 150 VVGLkGYEN---AKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPlirkEMQNELLSLQTKMQK----TIVFITH 222
Cdd:COG1101   133 TLGL-GLENrldTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKIVEennlTTLMVTH 207

                         250       260
                  ....*....|....*....|.
gi 1577416155 223 DLDEALKIGDRIAIMKDGNIV 243
Cdd:COG1101   208 NMEQALDYGNRLIMMHEGRII 228
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 40-237 9.00e-29

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 117.39  E-value: 9.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  40 SVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLPh 119
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFA- 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGLEIQKVDveerkkKAIEMLEVVGLKGYENAKPK-----------ELSGGMQQRVGLARALATDADILLMD 188
Cdd:TIGR02857 410 GTIAENIRLARPDASDA------EIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLLD 483

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 189 EAFSALDPLIRKEMQNELLSLqtkMQ-KTIVFITHDLdEALKIGDRIAIM 237
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRAL---AQgRTVLLVTHRL-ALAALADRIVVL 529
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 43-264 1.06e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 113.27  E-value: 1.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIR--RKKIAMVFQNFALLPhR 120
Cdd:PRK14271   37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLefRRRVGMLFQRPNPFP-M 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFGLEIQK-VDVEERKKKAIEMLEVVGL----KGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:PRK14271  116 SIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 196 PLIRKEMQNELLSLQTKMqkTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREFI 264
Cdd:PRK14271  196 PTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 43-259 2.14e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 114.94  E-value: 2.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRkKIAMVFQNFAL------ 116
Cdd:PRK09536   19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASR-RVASVPQDTSLsfefdv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 --------LPHRTVLENvafgleiqkvdVEERKKKAIE-MLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK09536   95 rqvvemgrTPHRSRFDT-----------WTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 188 DEAFSALDplIRKEMQN-ELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP--ADAY 259
Cdd:PRK09536  164 DEPTASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlRAAF 236
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
45-253 3.47e-28

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 115.65  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDN---EKITQVSSAKLreirrkKIAMVFQNFALLPHRT 121
Cdd:PRK09700   23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAQL------GIGIIYQELSVIDELT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAFG-LEIQKV------DVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK09700   97 VLENLYIGrHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 195 DP-------LIRKEMQNEllslqtkmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK09700  177 TNkevdylfLIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 43-243 3.63e-28

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 109.99  E-value: 3.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLpHRTV 122
Cdd:cd03245    20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF-YGTL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLeiQKVDVEErkkkAIEMLEVVGLKGYENAKPK-----------ELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:cd03245    95 RDNITLGA--PLADDER----ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 192 SALDplIRKEMQ-NELLSlQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIV 243
Cdd:cd03245   169 SAMD--MNSEERlKERLR-QLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 43-254 9.91e-28

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 114.85  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklREIRRKKIAMVFQNFALLPHrTV 122
Cdd:COG4618   348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD----REELGRHIGYLPQDVELFDG-TI 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVA-FGlEIQKVDVEERKKKA--IEMleVVGL-KGY-----ENAKPkeLSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:COG4618   423 AENIArFG-DADPEKVVAAAKLAgvHEM--ILRLpDGYdtrigEGGAR--LSGGQRQRIGLARALYGDPRLVVLDEPNSN 497

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 194 LDPLIRKEMQNELLSLQtKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:COG4618   498 LDDEGEAALAAAIRALK-ARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 32-253 1.17e-27

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 114.13  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRL--IEPTSGEI-----------YID----------- 87
Cdd:TIGR03269   5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvgepcpv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  88 -NEKITQVS------SAKLREIRRKKIAMVFQ-NFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENA 159
Cdd:TIGR03269  85 cGGTLEPEEvdfwnlSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 160 KPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKD 239
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244

                         250
                  ....*....|....
gi 1577416155 240 GNIVQIGEPEEILN 253
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 46-242 1.31e-27

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 109.10  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLPHRTVLEN 125
Cdd:PRK10584   29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALEN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 126 VAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNE 205
Cdd:PRK10584  109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1577416155 206 LLSLQTKMQKTIVFITHDLDEALKIGDRIAiMKDGNI 242
Cdd:PRK10584  189 LFSLNREHGTTLILVTHDLQLAARCDRRLR-LVNGQL 224
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
42-254 2.00e-27

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 113.90  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNfALLPHRT 121
Cdd:PRK13657  350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQD-AGLFNRS 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAFG------------LEI-QKVDVEERKKKAIEMleVVGLKGyenakpKELSGGMQQRVGLARALATDADILLMD 188
Cdd:PRK13657  425 IEDNIRVGrpdatdeemraaAERaQAHDFIERKPDGYDT--VVGERG------RQLSGGERQRLAIARALLKDPPILILD 496

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 189 EAFSALDPLIRKEMQnelLSLQTKMQ-KTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK13657  497 EATSALDVETEAKVK---AALDELMKgRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELVAR 559
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
43-265 2.21e-27

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 110.77  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP----TSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQN--FAL 116
Cdd:COG4170    23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEpsSCL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVafgleIQKVDVEE-----------RKKKAIEMLEVVGLKGYE---NAKPKELSGGMQQRVGLARALATDA 182
Cdd:COG4170   103 DPSAKIGDQL-----IEAIPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQP 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 183 DILLMDEAFSALDPLirkeMQNELLSLQTKMQK----TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADA 258
Cdd:COG4170   178 RLLIADEPTNAMEST----TQAQIFRLLARLNQlqgtSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253


                  ....*..
gi 1577416155 259 YVREFIQ 265
Cdd:COG4170   254 YTKALLR 260
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 43-248 2.50e-27

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 107.96  E-value: 2.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLPHrTV 122
Cdd:cd03244    20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLFSG-TI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVA-FGL----EIQKVdveerkkkaiemLEVVGLKGYENAKPKEL-----------SGGMQQRVGLARALATDADILL 186
Cdd:cd03244    95 RSNLDpFGEysdeELWQA------------LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 187 MDEAFSALDPLIRKEMQNellSLQTKM-QKTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEP 248
Cdd:cd03244   163 LDEATASVDPETDALIQK---TIREAFkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 42-248 3.72e-27

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 114.34  E-value: 3.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreirRKKIAMVFQNFALLPHRT 121
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCPQHNILFHHLT 1019

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  122 VLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKE 201
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1577416155  202 MQNELLSLQTKmqKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEP 248
Cdd:TIGR01257 1100 IWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 32-259 7.37e-27

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 107.70  E-value: 7.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAmvf 111
Cdd:PRK11701   11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLL--- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 qnfallphRT----VLENVAFGLEIQkV----DVEERkkkaiemLEVVGLKGYENAK--------------------PKE 163
Cdd:PRK11701   88 --------RTewgfVHQHPRDGLRMQ-VsaggNIGER-------LMAVGARHYGDIRatagdwlerveidaariddlPTT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:PRK11701  152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231

                         250
                  ....*....|....*.
gi 1577416155 244 QIGEPEEILNSPADAY 259
Cdd:PRK11701  232 ESGLTDQVLDDPQHPY 247
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 43-224 1.04e-26

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 111.68  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAMVFQNfALLPHRTV 122
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQD-AHLFDTTV 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEiqKVDVEErkkkAIEMLEVVGLKGYENAKP-----------KELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:TIGR02868 426 RENLRLARP--DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1577416155 192 SALDPLIRKEMQNELLSLQTkmQKTIVFITHDL 224
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALS--GRTVVLITHHL 530
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 37-268 2.71e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 106.86  E-value: 2.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVG---VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItQVSSAKLREIRrKKIAMVFQN 113
Cdd:PRK13636   13 YNYSDGthaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 114 -FALLPHRTVLENVAFG---LEIQKVDVEERKKKAIEMLEVVGLKGyenaKPKE-LSGGMQQRVGLARALATDADILLMD 188
Cdd:PRK13636   91 pDNQLFSASVYQDVSFGavnLKLPEDEVRKRVDNALKRTGIEHLKD----KPTHcLSFGQKKRVAIAGVLVMEPKVLVLD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 189 EAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILnspADayvREFIQDVN 268
Cdd:PRK13636  167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF---AE---KEMLRKVN 240
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 44-240 3.58e-26

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 104.09  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdnekitqvssaklreirRKKIAMVFQNfALLPHRTVL 123
Cdd:cd03250    22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----------------PGSIAYVSQE-PWIQNGTIR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLEIQkvdvEERKKKAI---------EMLE-----VVGLKGYEnakpkeLSGGMQQRVGLARALATDADILLMDE 189
Cdd:cd03250    84 ENILFGKPFD----EERYEKVIkacalepdlEILPdgdltEIGEKGIN------LSGGQKQRISLARAVYSDADIYLLDD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 190 AFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLdEALKIGDRIAIMKDG 240
Cdd:cd03250   154 PLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
42-251 4.02e-26

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 109.72  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssaKLREIR---RKKIAMVFQN---FA 115
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------RIRSPRdaiRAGIAYVPEDrkgEG 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 LLPHRTVLENVA---------FGLeiqkVDVEERKKKAIEMLEVVGLK-GYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:COG1129   341 LVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 186 LMDEafsaldP--------------LIRkemqnELlslqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:COG1129   417 ILDE------PtrgidvgakaeiyrLIR-----EL----AAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 43-259 1.06e-25

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 105.96  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP---TSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQN--FALL 117
Cdd:PRK09473   32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmTSLN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHRTVLENVAFGLEIQK-VDVEERKKKAIEMLEVVglKGYENAK-----PKELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK09473  112 PYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAV--KMPEARKrmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAY 259
Cdd:PRK09473  190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 32-253 1.23e-25

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 103.82  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsakLREIRRKKIAMVF 111
Cdd:PRK10895    8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQK-VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:PRK10895   85 QEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKMQKtiVFIT-HDLDEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK10895  165 FAGVDPISVIDIKRIIEHLRDSGLG--VLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
46-243 1.72e-25

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 103.03  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKkIAMVFQNFALLPHRTVLEN 125
Cdd:PRK10908   21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 126 VAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDplirKEMQNE 205
Cdd:PRK10908  100 VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEG 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1577416155 206 LLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:PRK10908  176 ILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 43-240 1.83e-25

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 107.71  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRlIEPT---SGEIYIDNEKITqvsSAKLREIRRKKIAMVFQNFALLPH 119
Cdd:PRK13549   21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQ---ASNIRDTERAGIAIIHQELALVKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAldp 196
Cdd:PRK13549   97 LSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS--- 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1577416155 197 LIRKEMQnELLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDG 240
Cdd:PRK13549  174 LTESETA-VLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDG 219
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 45-259 3.79e-25

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 107.50  E-value: 3.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNfALLPHRTVLE 124
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQE-PVLFSGSVRE 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGL------EIQKVDVEERKKKAIEMLE-----VVGLKGyenakpKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:TIGR00958 574 NIAYGLtdtpdeEIMAAAKAANAHDFIMEFPngydtEVGEKG------SQLSGGQKQRIAIARALVRKPRVLILDEATSA 647

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 194 LDPLIRKEMQNellsLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILNSPaDAY 259
Cdd:TIGR00958 648 LDAECEQLLQE----SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ-GCY 707
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 278-387 4.28e-25

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341402 [Multi-domain]  Cd Length: 116  Bit Score: 98.79  E-value: 4.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 278 IMRSSESIILEKA--GVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDDLKSVIDTDIRTVGVDTSIDE 355
Cdd:cd09831     2 IARKTQVTVIEKTgdGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENAQSLEDAFLTDVETVPADTSLSD 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1577416155 356 IIPLFLQSGYPVAVVDDENKLKGIIFKSTVLA 387
Cdd:cd09831    82 ILGLVASAPCPLPVVDEDGRYLGVISKASLLE 113
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 43-226 5.89e-25

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 101.71  E-value: 5.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklrEIRRKKIAMVFQNFALLPHrTV 122
Cdd:PRK10247   23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQVSYCAQTPTLFGD-TV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKVDVEErkKKAIEMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADILLMDEAFSALDPLiRKE 201
Cdd:PRK10247   98 YDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKH 174

                         170       180
                  ....*....|....*....|....*.
gi 1577416155 202 MQNELLSLQTKMQK-TIVFITHDLDE 226
Cdd:PRK10247  175 NVNEIIHRYVREQNiAVLWVTHDKDE 200
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 45-242 7.97e-25

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 101.39  E-value: 7.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAMVFQNFALLPhRTVLE 124
Cdd:cd03248    32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLFA-RSLQD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLeiQKVDVEERKKKA--------IEMLEvvglKGYE---NAKPKELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:cd03248   107 NIAYGL--QSCSFECVKEAAqkahahsfISELA----SGYDtevGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1577416155 194 LDplIRKEMQNELLSLQTKMQKTIVFITHDLDEALKiGDRIAIMKDGNI 242
Cdd:cd03248   181 LD--AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
45-275 8.77e-25

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 105.76  E-value: 8.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkitQVSSAKLREIRRKKIAMVFQNFALLPHRTVLE 124
Cdd:PRK11288   22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---EMRFASTTAALAAGVAIIYQELHLVPEMTVAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDpliRKE 201
Cdd:PRK11288   99 NLYLGQLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS---ARE 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 202 MQNeLLSLQTKMQ---KTIVFITHDLDEALKIGDRIAIMKDGNivqigepeeilnspadaYVREF--IQDVNRTKIVSA 275
Cdd:PRK11288  176 IEQ-LFRVIRELRaegRVILYVSHRMEEIFALCDAITVFKDGR-----------------YVATFddMAQVDRDQLVQA 236
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 36-246 1.03e-24

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 99.69  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  36 KYKHS--VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssAKLREIRRKKIAMVFQN 113
Cdd:cd03247     9 SYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-----SDLEKALSSLISVLNQR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 114 fallPH---RTVLENVAfgleiqkvdveerkkkaiemlevvglkgyenakpKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03247    84 ----PYlfdTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 191 FSALDPlirkEMQNELLSLQTKM--QKTIVFITHDLdEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03247   126 TVGLDP----ITERQLLSLIFEVlkDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
45-254 1.05e-24

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 101.99  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRkKIAMVFQNFALLPHRTVLE 124
Cdd:PRK10253   25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVAR-RIGLLAQNATTPGDITVQE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFG-LEIQKVDVEERKKKA---IEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDplirK 200
Cdd:PRK10253  101 LVARGrYPHQPLFTRWRKEDEeavTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD----I 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 201 EMQNELLSLQTKMQK----TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PRK10253  177 SHQIDLLELLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
43-237 1.37e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 99.62  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEiyidnekitqvssakLREIRRKKIAMVFQNFAL---LPh 119
Cdd:NF040873    8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVpdsLP- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGL-----EIQKVDVEERkKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:NF040873   72 LTVRDLVAMGRwarrgLWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1577416155 195 DPLIRKEMqNELLSLQTKMQKTIVFITHDLDEALKIgDRIAIM 237
Cdd:NF040873  151 DAESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 41-251 1.81e-24

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 104.72  E-value: 1.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMV---FQNFALL 117
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RERRRLGVAYIpedRLGRGLV 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHRTVLENVAFGLE----------IQKVDVEERKKKAIEMLEVVGlkGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:COG3845   349 PDMSVAENLILGRYrrppfsrggfLDRKAIRAFAEELIEEFDVRT--PGPDTPARSLSGGNQQKVILARELSRDPKLLIA 426

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 188 DEAFSALDP----LIRKemqnELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:COG3845   427 AQPTRGLDVgaieFIHQ----RLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
44-253 2.92e-24

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 104.72  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAMVFQNFALLpHRTVL 123
Cdd:PRK11176  360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN----QVALVSQNVHLF-NDTIA 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLEIQ--KVDVEERKKKA-----IEMLE-----VVGlkgyENAKpkELSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:PRK11176  435 NNIAYARTEQysREQIEEAARMAyamdfINKMDngldtVIG----ENGV--LLSGGQRQRIAIARALLRDSPILILDEAT 508

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 192 SALDPLIRKEMQNELLSLQTkmQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:PRK11176  509 SALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 43-243 3.11e-24

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 98.78  E-value: 3.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLN--RLIEPTSGEIYIDNEKITQVSSaklreirRKKIAMVFQNFALLPHR 120
Cdd:cd03213    25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSF-------RKIIGYVPQDDILHPTL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 TVLENVAFgleiqkvdveerkkkaiemlevvglkgyeNAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLirk 200
Cdd:cd03213    98 TVRETLMF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS--- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1577416155 201 emqNELLSLQT-----KMQKTIVFITHDL-DEALKIGDRIAIMKDGNIV 243
Cdd:cd03213   146 ---SALQVMSLlrrlaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 43-265 4.55e-24

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 99.77  E-value: 4.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKStlIRCLNRL------IEPTSGEIYIDNEKitqVSSAKLREirrKKIAMVFQN--F 114
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKP---VAPCALRG---RKIATIMQNprS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVlenVAFGLE-IQKVDVEERKKKAIEMLEVVGLkgyENAK------PKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK10418   91 AFNPLHTM---HTHAREtCLALGKPADDATLTAALEAVGL---ENAArvlklyPFEMSGGMLQRMMIALALLCEAPFIIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 188 DEAFSALDPLIrkemQNELLSLQTKMQKT----IVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVREF 263
Cdd:PRK10418  165 DEPTTDLDVVA----QARILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240


                  ..
gi 1577416155 264 IQ 265
Cdd:PRK10418  241 VS 242
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 43-245 5.06e-24

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 103.90  E-value: 5.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssAKLREIRRKKIAMVFQNFALLPHrtV 122
Cdd:PRK10522  339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT----AEQPEDYRKLFSAVFTDFHLFDQ--L 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKVDVE-ERkkkaIEMLEVVGLKGYENAKPKeLSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKE 201
Cdd:PRK10522  413 LGPEGKPANPALVEKWlER----LKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1577416155 202 MQNELLSLQTKMQKTIVFITHDlDEALKIGDRIAIMKDGNIVQI 245
Cdd:PRK10522  488 FYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 45-196 1.36e-23

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 97.04  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssAKLREIRRKKIAMVFQNFALLPHRTVLE 124
Cdd:TIGR01189  18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPELSALE 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 125 NVAFGLEIQkvDVEERKkkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:TIGR01189  93 NLHFWAAIH--GGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 46-251 2.47e-23

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 101.67  E-value: 2.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIrrkKIAMVFQNFALLPHRTVLEN 125
Cdd:PRK15439   30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVKEN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 126 VAFGLEIQkvdvEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNE 205
Cdd:PRK15439  107 ILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSR 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1577416155 206 LLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:PRK15439  183 IRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
45-195 3.35e-23

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 96.03  E-value: 3.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvssAKLREIRRkkiamvfQNFALLPHR---- 120
Cdd:PRK13538   19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDEYH-------QDLLYLGHQpgik 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 121 ---TVLENVAFGLEI-QKVDVEErkkkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:PRK13538   87 telTALENLRFYQRLhGPGDDEA----LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
43-265 3.85e-22

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 96.02  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKStlirclnrLIEPTSGEIYIDNEKIT------------QVSSAKLREIRRKKIAMV 110
Cdd:PRK15093   23 VDRVSMTLTEGEIRGLVGESGSGKS--------LIAKAICGVTKDNWRVTadrmrfddidllRLSPRERRKLVGHNVSMI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNfallPHRTVLENVAFGLE-IQKVD-----------VEERKKKAIEMLEVVGLKGYENAK---PKELSGGMQQRVGLA 175
Cdd:PRK15093   95 FQE----PQSCLDPSERVGRQlMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKDHKDAMrsfPYELTEGECQKVMIA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 176 RALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK15093  171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250

                         250
                  ....*....|
gi 1577416155 256 ADAYVREFIQ 265
Cdd:PRK15093  251 HHPYTQALIR 260
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 45-255 4.30e-22

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 97.99  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLircLNRLIE--PTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNfALLPHRTV 122
Cdd:PRK11174  368 PLNFTLPAGQRIALVGPSGAGKTSL---LNALLGflPYQGSLKINGIELRELDPESW----RKHLSWVGQN-PQLPHGTL 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFG---LEIQKVDVEERKKKAIEMLEVV--GLK---GYENAKpkeLSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK11174  440 RDNVLLGnpdASDEQLQQALENAWVSEFLPLLpqGLDtpiGDQAAG---LSVGQAQRLALARALLQPCQLLLLDEPTASL 516

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 195 DplirkeMQNE---LLSLQTKMQ-KTIVFITHDLDEaLKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK11174  517 D------AHSEqlvMQALNAASRrQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAG 574
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
43-255 5.03e-22

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 94.47  E-value: 5.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSV-------------NEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrKKIAM 109
Cdd:PRK10575   14 LRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPHRTVLENVAFGL-----EIQKVDVEERKKKAiEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADI 184
Cdd:PRK10575   90 LPQQLPAAEGMTVRELVAIGRypwhgALGRFGAADREKVE-EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 185 LLMDEAFSALDplirKEMQNELLSLQTKMQK----TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK10575  169 LLLDEPTSALD----IAHQVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 33-240 9.62e-22

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 96.82  E-value: 9.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRlIEPT---SGEIYIDNEKItqvSSAKLREIRRKKIAM 109
Cdd:TIGR02633   7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPL---KASNIRDTERAGIVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPHRTVLENVAFGLEI----QKVDVEERKKKAIEMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADI 184
Cdd:TIGR02633  83 IHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 185 LLMDEAFSAldpLIRKEMQNELLSLQTKMQKTI--VFITHDLDEALKIGDRIAIMKDG 240
Cdd:TIGR02633 163 LILDEPSSS---LTEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDG 217
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 45-248 1.59e-21

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 91.70  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvSSAKLREIRRkKIAMVFQNFALLPHrTVLE 124
Cdd:cd03369    26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRS-SLTIIPQDPTLFSG-TIRS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NvafgleiqkVDVEER--KKKAIEMLEVVGlkGYENakpkeLSGGMQQRVGLARALATDADILLMDEAFSALD------- 195
Cdd:cd03369   101 N---------LDPFDEysDEEIYGALRVSE--GGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDyatdali 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 196 -PLIRKEMQNellslqtkmqKTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEP 248
Cdd:cd03369   165 qKTIREEFTN----------STILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 35-246 2.70e-21

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 91.56  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP---TSGEIYIDNEKITqvssaklREIRRKKIAMVF 111
Cdd:cd03234    15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK-------PDQFQKCVAYVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFG--LEIQKVDVEERKKK--AIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:cd03234    88 QDDILLPGLTVRETLTYTaiLRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 188 DEAFSALDPLIrkemQNELLSL--QTKMQKTIVFIT-HD-LDEALKIGDRIAIMKDGNIVQIG 246
Cdd:cd03234   168 DEPTSGLDSFT----ALNLVSTlsQLARRNRIVILTiHQpRSDLFRLFDRILLLSSGEIVYSG 226
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 45-195 5.48e-21

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 89.93  E-value: 5.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvsSAKLREirrkkiAMVF---QNfALLPHRT 121
Cdd:PRK13539   20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAE------ACHYlghRN-AMKPALT 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 122 VLENVAFGLEIQKvdveERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:PRK13539   90 VAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 44-228 1.13e-20

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 89.63  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE--PTSGEIYIDNEKITQVssaklreirrkkiamvfqnfallphRT 121
Cdd:COG2401    47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE-------------------------AS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAfgleiQKVDVeerkKKAIEMLEVVGLKgyEN----AKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPL 197
Cdd:COG2401   102 LIDAIG-----RKGDF----KDAVELLNAVGLS--DAvlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1577416155 198 IRKEMQNELLSLQTKMQKTIVFITH--DLDEAL 228
Cdd:COG2401   171 TAKRVARNLQKLARRAGITLVVATHhyDVIDDL 203
GguA NF040905
sugar ABC transporter ATP-binding protein;
44-244 1.79e-20

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 92.93  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRlIEPT---SGEIYIDNEKitqvssAKLREIR---RKKIAMVFQNFALL 117
Cdd:NF040905   18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEV------CRFKDIRdseALGIVIIHQELALI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 118 PHRTVLENVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:NF040905   91 PYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 195 dplirkemqNE-----LLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIVQ 244
Cdd:NF040905  171 ---------NEedsaaLLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 44-242 2.81e-20

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 92.44  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnekitqvssaklreiRRKKIAMVFQNFALLPHRTVL 123
Cdd:COG0488    15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFG------LEIQKVDVEERKKKAIEMLEVVG--------LKGYE-------------------NAKPKELSGGMQQ 170
Cdd:COG0488    80 DTVLDGdaelraLEAELEELEAKLAEPDEDLERLAelqeefeaLGGWEaearaeeilsglgfpeedlDRPVSELSGGWRR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 171 RVGLARALATDADILLMDEAFSALDplirKEM----QNELLSLqtkmQKTIVFITHD---LDEalkIGDRIAIMKDGNI 242
Cdd:COG0488   160 RVALARALLSEPDLLLLDEPTNHLD----LESiewlEEFLKNY----PGTVLVVSHDryfLDR---VATRILELDRGKL 227
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
43-255 3.54e-20

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 92.47  E-value: 3.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaKLREIRRKkIAMVFQNfALLPHRTV 122
Cdd:PRK10789  331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVVSQT-PFLFSDTV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGL-EIQKVDVEERKKKAIEMLEVVGL-KGYENA---KPKELSGGMQQRVGLARALATDADILLMDEAFSALDPl 197
Cdd:PRK10789  406 ANNIALGRpDATQQEIEHVARLASVHDDILRLpQGYDTEvgeRGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG- 484

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 198 iRKEMQnELLSL-QTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK10789  485 -RTEHQ-ILHNLrQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 46-195 1.90e-19

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 85.62  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaklREIRRKKIAMVFQNFALLPHRTVLEN 125
Cdd:cd03231    19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-----RDSIARGLLYLGHAPGIKTTLSVLEN 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 126 VAFGLEIQKVDVEErkkkaiEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:cd03231    94 LRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
43-243 2.70e-19

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 86.09  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKlreIRRKKIAMVFQNFALLPHRTV 122
Cdd:PRK11614   21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK---IMREAVAIVPEGRRVFSRMTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAF-GLEIQKVDVEERKKKAIEMLEVVGLKGYENAkpKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKE 201
Cdd:PRK11614   98 EENLAMgGFFAERDQFQERIKWVYELFPRLHERRIQRA--GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1577416155 202 MQNELLSLQTKMQkTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:PRK11614  176 IFDTIEQLREQGM-TIFLVEQNANQALKLADRGYVLENGHVV 216
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
41-251 2.78e-19

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.18  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  41 VGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEiyidnekitqvssAKL--REIR------RKKIAMVFQ 112
Cdd:NF033858  280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-------------AWLfgQPVDagdiatRRRVGYMSQ 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 NFALLPHRTVLENVA-----FGLEiqkvdvEERKKKAI-EMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILL 186
Cdd:NF033858  347 AFSLYGELTVRQNLElharlFHLP------AAEIAARVaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLQTKMQKTIvFI-THDLDEALKIgDRIAIMKDGNIVQIGEPEEI 251
Cdd:NF033858  421 LDEPTSGVDPVARDMFWRLLIELSREDGVTI-FIsTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 4-243 9.00e-19

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 84.69  E-value: 9.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFgsAPMQMISFLeKGEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE 83
Cdd:cd03267     1 IEVSNLSKSY--RVYSKEPGL-IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  84 IyidneKITQVSSAKLREIRRKKIAMVF-QNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPK 162
Cdd:cd03267    78 V-----RVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 163 ELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:cd03267   153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232


                  .
gi 1577416155 243 V 243
Cdd:cd03267   233 L 233
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 43-240 1.23e-18

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 83.92  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIRRKKIAMVFQNFALLpHRTV 122
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFGLEIQKvdveERKKKAIEMLEV--------------VGLKGYEnakpkeLSGGMQQRVGLARALATDADILLMD 188
Cdd:cd03290    96 EENITFGSPFNK----QRYKAVTDACSLqpdidllpfgdqteIGERGIN------LSGGQRQRICVARALYQNTNIVFLD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 189 EAFSALD-PLIRKEMQNELLSLQTKMQKTIVFITHDLdEALKIGDRIAIMKDG 240
Cdd:cd03290   166 DPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 31-240 1.67e-18

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 87.09  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMV 110
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSS---KEALENGISMV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNFALLPHRTVLENVAFGLEIQK---VDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK10982   79 HQELNLVLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 188 DEAFSALDpliRKEMqNELLSLQTKMQKT---IVFITHDLDEALKIGDRIAIMKDG 240
Cdd:PRK10982  159 DEPTSSLT---EKEV-NHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDG 210
PTZ00243 PTZ00243
ABC transporter; Provisional
 43-255 4.50e-18

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 86.76  E-value: 4.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvSSAKLREIRRKkiamvfqnFALLPHRTV 122
Cdd:PTZ00243  1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQ--------FSMIPQDPV 1394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  123 LENvafGLEIQKVD--VEERKKKAIEMLEVVGLKGY-----ENAKPKELSGGMQQRVG------LARA-LATDADILLMD 188
Cdd:PTZ00243  1395 LFD---GTVRQNVDpfLEASSAEVWAALELVGLRERvasesEGIDSRVLEGGSNYSVGqrqlmcMARAlLKKGSGFILMD 1471

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155  189 EAFSALDPLIRKEMQNELLSLQTKMqkTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PTZ00243  1472 EATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
31-252 4.98e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 83.13  E-value: 4.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreIRRKKIAMV 110
Cdd:PRK13638    5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL--ALRQQVATV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQNfallPHRTVL-----ENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK13638   83 FQD----PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 186 LMDEAFSALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK13638  159 LLDEPTAGLDPAGRTQMI-AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 43-222 1.91e-17

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 84.09  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIyidnekitqvssaklreIRRKKIAMVFqnfalLPHR-- 120
Cdd:COG4178   379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------------ARPAGARVLF-----LPQRpy 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 ----TVLENVAFGLEIQKVDVEErkkkAIEMLEVVGLKGY------ENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:COG4178   437 lplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1577416155 191 FSALDPlirkEMQNELLS-LQTKMQK-TIVFITH 222
Cdd:COG4178   513 TSALDE----ENEAALYQlLREELPGtTVISVGH 542
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 46-255 2.68e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 80.75  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIePTSGEIYIDNEKITQVSSAKLREIR-------RKKIAM-VFQNFAL- 116
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTLh 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEiqkvdveerkkkaiEMLEVVGLKGYENAKPKELSGGMQQRVGLA-------RALATDADILLMDE 189
Cdd:PRK03695   94 QPDKTRTEAVASALN--------------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 190 AFSALDplirKEMQNELLSLQTKMQK---TIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILNSP 255
Cdd:PRK03695  160 PMNSLD----VAQQAALDRLLSELCQqgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
43-245 6.91e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 82.14  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSS--------AKLREIRRKKiaMVFQNF 114
Cdd:PRK09700  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmAYITESRRDN--GFFPNF 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTV---LENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYE-NAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:PRK09700  357 SIAQNMAIsrsLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 191 FSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQI 245
Cdd:PRK09700  437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
48-196 8.41e-17

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 78.74  E-value: 8.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  48 FSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaklREIRRKKIAMVFQNFALLPHRTVLENVA 127
Cdd:PRK13543   32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-------RGDRSRFMAYLGHLPGLKADLSTLENLH 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 128 FGLEIQKVDVEERKKKAiemLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:PRK13543  105 FLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 43-252 8.42e-17

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 82.69  E-value: 8.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdnekitqvssaklreirRKKIAMVFQNfALLPHRTV 122
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------------KGSVAYVPQQ-AWIQNDSL 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  123 LENVAFGLEIQkvdvEERKKKAIEM------LEVV--GLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:TIGR00957  716 RENILFGKALN----EKYYQQVLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155  195 DPLIRKEMQNELLSLQTKMQ-KTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:TIGR00957  792 DAHVGKHIFEHVIGPEGVLKnKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELL 849
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-253 1.25e-16

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 80.13  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   4 IQVKNVYKVFGSApmqmisflEKGEKKTDLLK-----KYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIE 78
Cdd:COG4586     2 IEVENLSKTYRVY--------EKEPGLKGALKglfrrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  79 PTSGEIYIDNEKITQvssaklREIR-RKKIAMVF-QNFALLPHRTVLENvaFGL--EIQKVDVEERKKKAIEMLEVVGLK 154
Cdd:COG4586    74 PTSGEVRVLGYVPFK------RRKEfARRIGVVFgQRSQLWWDLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 155 GYENaKP-KELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDR 233
Cdd:COG4586   146 ELLD-TPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224

                         250       260
                  ....*....|....*....|
gi 1577416155 234 IAIMKDGNIVQIGEPEEILN 253
Cdd:COG4586   225 VIVIDHGRIIYDGSLEELKE 244
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
40-252 2.28e-16

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 80.92  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  40 SVGVNNVSFSVNEGEI-------------FVVM-GLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRK 105
Cdd:PRK10790  340 RIDIDNVSFAYRDDNLvlqninlsvpsrgFVALvGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQ 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 106 KIAMVFQNFALLPHrTVLENVAFGLEIQkvdvEERKKKAIEMLEVV--------GLKGYENAKPKELSGGMQQRVGLARA 177
Cdd:PRK10790  416 GVAMVQQDPVVLAD-TFLANVTLGRDIS----EEQVWQALETVQLAelarslpdGLYTPLGEQGNNLSVGQKQLLALARV 490

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 178 LATDADILLMDEAFSALDPLIRKEMQNELLSLqtKMQKTIVFITHDLD---EAlkigDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK10790  491 LVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLL 562
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 35-262 3.04e-16

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 80.48  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEP---TSGEIYIDNEKITqvssakLREIRRKKiAMVF 111
Cdd:TIGR00955  35 RPRKHLL--KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID------AKEMRAIS-AYVQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNFALLPHRTVLENVAFGLEIQ---KVDVEERKKKAIEMLEVVGLK-------GYENAKpKELSGGMQQRVGLARALATD 181
Cdd:TIGR00955 106 QDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 182 ADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEILN-------- 253
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghp 264

                         250
                  ....*....|....
gi 1577416155 254 -----SPADAYVRE 262
Cdd:TIGR00955 265 cpenyNPADFYVQV 278
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 39-252 5.12e-16

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.19  E-value: 5.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  39 HSVGVNN----VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIePTSGEIYIDNEKITQVSSAKLREIRrkkiAMVFQNF 114
Cdd:COG4138     4 NDVAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR----AYLSQQQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLeiQKVDVEERKKKAIEML-EVVGLKgyenakPK------ELSGGMQQRVGLARALAT------- 180
Cdd:COG4138    79 SPPFAMPVFQYLALHQ--PAGASSEAVEQLLAQLaEALGLE------DKlsrpltQLSGGEWQRVRLAAVLLQvwptinp 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 181 DADILLMDEAFSALDplIRKE-MQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:COG4138   151 EGQLLLLDEPMNSLD--VAQQaALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
46-243 6.01e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 79.18  E-value: 6.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItQVSSAKlREIR---------RKKIAMVfqnfal 116
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPR-DAIRagimlcpedRKAEGII------ 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 lPHRTVLENVA---------FGLEIQKVDVEERKKKAIEMLEVvglKGYENAKP-KELSGGMQQRVGLARALATDADILL 186
Cdd:PRK11288  344 -PVHSVADNINisarrhhlrAGCLINNRWEAENADRFIRSLNI---KTPSREQLiMNLSGGNQQKAILGRWLSEDMKVIL 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 187 MDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:PRK11288  420 LDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 43-243 7.77e-16

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 78.95  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdnekitqvsSAKLreirrkKIAMVFQNFALL-PHRT 121
Cdd:COG0488   331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETV------KIGYFDQHQEELdPDKT 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLEnvafglEIQKVDVEERKKKAIEMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADILLMDEAFSALDPlirk 200
Cdd:COG0488   396 VLD------ELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI---- 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1577416155 201 EMQNELLSLQTKMQKTIVFITHD---LDealKIGDRIAIMKDGNIV 243
Cdd:COG0488   466 ETLEALEEALDDFPGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 46-249 8.72e-16

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 79.07  E-value: 8.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  46 VSFSVNEGEI-FVVMGlSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssAKLREIRRKKIAMVFQNFALLPHrtvle 124
Cdd:COG4615   351 IDLTIRRGELvFIVGG-NGSGKSTLAKLLTGLYRPESGEILLDGQPVT----ADNREAYRQLFSAVFSDFHLFDR----- 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 nvAFGLEIQKVDveerkKKAIEMLEVVGLKG---YENAK--PKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:COG4615   421 --LLGLDGEADP-----ARARELLERLELDHkvsVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR 493

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 200 KEMQNELLSLQTKMQKTIVFITHD---LDEAlkigDRIAIMKDGNIVQIGEPE 249
Cdd:COG4615   494 RVFYTELLPELKARGKTVIAISHDdryFDLA----DRVLKMDYGKLVELTGPA 542
PLN03130 PLN03130
ABC transporter C family member; Provisional
 46-252 3.80e-15

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 77.47  E-value: 3.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   46 VSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLReirrkkiamvfQNFALLPHRTVL-- 123
Cdd:PLN03130  1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR-----------KVLGIIPQAPVLfs 1326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  124 ENVAFGL----EIQKVDVEERKKKAiEMLEVV-----GL-----KGYENakpkeLSGGMQQRVGLARALATDADILLMDE 189
Cdd:PLN03130  1327 GTVRFNLdpfnEHNDADLWESLERA-HLKDVIrrnslGLdaevsEAGEN-----FSVGQRQLLSLARALLRRSKILVLDE 1400

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155  190 AFSAL----DPLIRKEMQNELLSLqtkmqkTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PLN03130  1401 ATAAVdvrtDALIQKTIREEFKSC------TMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLL 1460
PLN03232 PLN03232
ABC transporter C family member; Provisional
 29-261 5.18e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 77.32  E-value: 5.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   29 KKTDLLKKYKHSVG--VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIrrkk 106
Cdd:PLN03232  1236 KFEDVHLRYRPGLPpvLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV---- 1311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  107 iamvfqnFALLPHRTVL--ENVAFGL----EIQKVDVEERKKKAiEMLEVV-----GLKGYENAKPKELSGGMQQRVGLA 175
Cdd:PLN03232  1312 -------LSIIPQSPVLfsGTVRFNIdpfsEHNDADLWEALERA-HIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLA 1383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  176 RALATDADILLMDEAFSAL----DPLIRKEMQNELLSLqtkmqkTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEI 251
Cdd:PLN03232  1384 RALLRRSKILVLDEATASVdvrtDSLIQRTIREEFKSC------TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQEL 1456

                          250
                   ....*....|
gi 1577416155  252 LNSPADAYVR 261
Cdd:PLN03232  1457 LSRDTSAFFR 1466
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 27-260 5.32e-15

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 77.36  E-value: 5.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   27 GEKKTDLLKKYK--------HSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssak 98
Cdd:TIGR01257 1931 GGNKTDILRLNEltkvysgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----- 2005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   99 lreirrkKIAMVFQNFALLPHRTVLENVAFGLE-------IQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQR 171
Cdd:TIGR01257 2006 -------NISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRK 2078

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  172 VGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157


                   ....*....
gi 1577416155  252 LNSPADAYV 260
Cdd:TIGR01257 2158 KSKFGDGYI 2166
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
35-252 7.97e-15

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 74.08  E-value: 7.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  35 KKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkitqvssaklreirrkkIAMVFQNF 114
Cdd:PRK13546   32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 115 ALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PRK13546   95 GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155 195 DPLIRKEMQNELLSLQtKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK13546  175 DQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 49-248 1.25e-14

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 72.83  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  49 SVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKItqvsSAKLREIRRKKIAMVfqnFALLPHRT--VLENV 126
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----SYKPQYIKADYEGTV---RDLLSSITkdFYTHP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 127 AFGLEIqkvdveerkkkaIEMLEVVGLkgYENAKPkELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNEL 206
Cdd:cd03237    94 YFKTEI------------AKPLQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1577416155 207 LSLQTKMQKTIVFITHDLDEALKIGDRIaimkdgnIVQIGEP 248
Cdd:cd03237   159 RRFAENNEKTAFVVEHDIIMIDYLADRL-------IVFEGEP 193
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 24-265 1.60e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.84  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   24 LEKGEKKTDLlKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRclnrliePTSGEIYIDNEKITQVSSAKLREIr 103
Cdd:PTZ00265  1227 VFKNEHTNDM-TNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDLRNL- 1297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  104 rkkIAMVFQNfALLPHRTVLENVAFGLE-IQKVDVEERKKKAI--EMLEVVGLKGYENAKP--KELSGGMQQRVGLARAL 178
Cdd:PTZ00265  1298 ---FSIVSQE-PMLFNMSIYENIKFGKEdATREDVKRACKFAAidEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARAL 1373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  179 ATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLdEALKIGDRIAIM----KDGNIVQIGEPEEILNS 254
Cdd:PTZ00265  1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFnnpdRTGSFVQAHGTHEELLS 1452

                          250
                   ....*....|.
gi 1577416155  255 PADAYVREFIQ 265
Cdd:PTZ00265  1453 VQDGVYKKYVK 1463
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
45-249 1.82e-14

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 72.99  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVssaklreIRRKKIAMVFQN------FALLP 118
Cdd:PRK15056   25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------LQKNLVAYVPQSeevdwsFPVLV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 HRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDplI 198
Cdd:PRK15056   98 EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD--V 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 199 RKEMQneLLSLQTKMQ---KTIVFITHDLDEALKIGDrIAIMKDGNIVQIGEPE 249
Cdd:PRK15056  176 KTEAR--IISLLRELRdegKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 21-243 3.18e-14

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 70.75  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  21 ISFLEKGEKKTDLLKkykhsvgvnNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT---SGEIYIDNekitqVSSA 97
Cdd:cd03233    10 SFTTGKGRSKIPILK---------DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG-----IPYK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  98 KLREIRRKKIAMVFQNFALLPHRTVLENVAFGLEiqkvdveerkkkaiemlevvgLKGyeNAKPKELSGGMQQRVGLARA 177
Cdd:cd03233    76 EFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR---------------------CKG--NEFVRGISGGERKRVSIAEA 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 178 LATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVF-ITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:cd03233   133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 45-257 3.69e-14

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 74.56  E-value: 3.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYidnekitqvssaklreiRRKKIAMVFQNFALLPHrTVLE 124
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------------HSGRISFSPQTSWIMPG-TIKD 505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  125 NVAFGLE---------IQKVDVEERKKKAIEMLEVVGLKGyenakPKELSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:TIGR01271  506 NIIFGLSydeyrytsvIKACQLEEDIALFPEKDKTVLGEG-----GITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155  196 PLIRKEMQNELLSlQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNSPAD 257
Cdd:TIGR01271  581 VVTEKEIFESCLC-KLMSNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 43-242 4.53e-14

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 73.71  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT-SGEIYIDNEKITQVSSAKlreIRRKKIAMVFQN---FALLP 118
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQ---AIRAGIAMVPEDrkrHGIVP 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 119 HRTVLENVAFGL-----EIQKVDVEERKKKAIEMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:TIGR02633 353 ILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 193 ALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:TIGR02633 433 GVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PTZ00243 PTZ00243
ABC transporter; Provisional
 45-261 4.84e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 74.04  E-value: 4.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnekitqvssaklreirrKKIAMVFQNfALLPHRTVLE 124
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------------RSIAYVPQQ-AWIMNATVRG 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  125 NVAFGLEiqkvDVEERKKKAIEM--LEV------VGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:PTZ00243   740 NILFFDE----EDAARLADAVRVsqLEAdlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155  197 LIRKEMQNELLsLQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNSPADAYVR 261
Cdd:PTZ00243   816 HVGERVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 42-242 2.08e-13

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 71.62  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAK--------LREIRRKK----IAM 109
Cdd:PRK15439  278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDRQSSglylDAP 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPHrtvlENVAFGLEIQK-VDVEERKKKAIemlevvGLKGYENAKP-KELSGGMQQRVGLARALATDADILLM 187
Cdd:PRK15439  358 LAWNVCALTH----NRRGFWIKPAReNAVLERYRRAL------NIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIV 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 188 DEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK15439  428 DEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 44-247 2.41e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 71.19  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEkitQVSSAKLREIRRKKIAMVFQNFALLPHRTVL 123
Cdd:PRK10762   21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTFNGPKSSQEAGIGIIHQELNLIPQLTIA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFGLEIQ----KVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALdplir 199
Cdd:PRK10762   98 ENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL----- 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 200 keMQNELLSL-----QTKMQKT-IVFITHDLDEALKIGDRIAIMKDGNIvqIGE 247
Cdd:PRK10762  173 --TDTETESLfrvirELKSQGRgIVYISHRLKEIFEICDDVTVFRDGQF--IAE 222
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 43-242 3.21e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 71.11  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCL-----NRliepTSGEIYIDNEKITQVSSaklREIRRKKIAMV------- 110
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKIRNP---QQAIAQGIAMVpedrkrd 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 --------FQNFALlphrTVLENVAFGLEIQKVDVEERKKKAIEMLEVvglkgyENAKP----KELSGGMQQRVGLARAL 178
Cdd:PRK13549  351 givpvmgvGKNITL----AALDRFTGGSRIDDAAELKTILESIQRLKV------KTASPelaiARLSGGNQQKAVLAKCL 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 179 ATDADILLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK13549  421 LLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 47-252 3.47e-13

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 70.81  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  47 SFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREIrrkkIAMVFQ--NFALLphrTVLE 124
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQrnNTDML---SPGE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NvAFGLEIQKVDVEERKKKAI--EMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEM 202
Cdd:PRK10938   96 D-DTGRTTAEIIQDEVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 203 QNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIL 252
Cdd:PRK10938  175 AELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 45-252 3.50e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 71.52  E-value: 3.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLreirRKKIAMVFQNFALLPHRTVLE 124
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLFSGSLRMN 1379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  125 NVAFGleiqkvdvEERKKKAIEMLEVVGLKGYENAKP-----------KELSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:TIGR00957 1380 LDPFS--------QYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  194 LDPLIRKEMQNellSLQTKMQK-TIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEIL 252
Cdd:TIGR00957 1452 VDLETDNLIQS---TIRTQFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 45-240 3.53e-13

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 69.50  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYidnekitqvssaklreiRRKKIAMVFQNFALLPHrTVLE 124
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------------HSGRISFSSQFSWIMPG-TIKE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 125 NVAFGLE---------IQKVDVEERKKKAIEMLEVVGLKGYENakpkeLSGGMQQRVGLARALATDADILLMDEAFSALD 195
Cdd:cd03291   117 NIIFGVSydeyryksvVKACQLEEDITKFPEKDNTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1577416155 196 PLIRKEMQNELLSlQTKMQKTIVFITHDLdEALKIGDRIAIMKDG 240
Cdd:cd03291   192 VFTEKEIFESCVC-KLMANKTRILVTSKM-EHLKKADKILILHEG 234
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 28-269 5.65e-13

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 70.30  E-value: 5.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  28 EKKTDLLKKYKHSV---GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnekitqvSSAKLREIrr 104
Cdd:PRK13545   22 DKLKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK-------GSAALIAI-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 kkiamvfqNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADI 184
Cdd:PRK13545   93 --------SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEIlnspADAYvREFI 264
Cdd:PRK13545  165 LVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV----VDHY-DEFL 238


                  ....*
gi 1577416155 265 QDVNR 269
Cdd:PRK13545  239 KKYNQ 243
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 43-252 5.70e-13

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 67.17  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCL--NRLIEPTSGEIYIDNEKITQVSsakLREIRRKKIAMVFQNFAllphr 120
Cdd:cd03217    16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLP---PEERARLGIFLAFQYPP----- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 121 tvlenvafglEIQKVdveerkkKAIEMLEVVGLKgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSALDPLIRK 200
Cdd:cd03217    88 ----------EIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 201 EMQNELLSLQTKmQKTIVFITHDLDEALKI-GDRIAIMKDGNIVQIGEPEEIL 252
Cdd:cd03217   142 LVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 43-222 6.17e-13

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 66.41  E-value: 6.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnekitqvssaklreiRRKKIAMVFQNfALLPHRTV 122
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLFLPQR-PYLPLGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LENVAFgleiqkvdveerkkkaiemlevvglkgyenakP--KELSGGMQQRVGLARALATDADILLMDEAFSALDPlirk 200
Cdd:cd03223    81 REQLIY--------------------------------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---- 124

                         170       180
                  ....*....|....*....|..
gi 1577416155 201 EMQNELLSLQTKMQKTIVFITH 222
Cdd:cd03223   125 ESEDRLYQLLKELGITVISVGH 146
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
275-394 6.83e-13

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 65.27  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 275 ASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDD----------LKSVIDTDI 344
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlldlpVEDVMTRPV 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 345 RTVGVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGIIFKSTVLAGIAGKEE 394
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHrLPVVDDDGRLVGIVTRTDLLRALARLLE 134
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 42-242 7.27e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 69.65  E-value: 7.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  42 GVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSS--------AKLREIRRKK---IAM- 109
Cdd:PRK10762  267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdglangiVYISEDRKRDglvLGMs 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFAL--LPHrtvLENVAFGL----EIQKVD--VEERKKKAIEMLEVVGLkgyenakpkeLSGGMQQRVGLARALATD 181
Cdd:PRK10762  347 VKENMSLtaLRY---FSRAGGSLkhadEQQAVSdfIRLFNIKTPSMEQAIGL----------LSGGNQQKVAIARGLMTR 413

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 182 ADILLMDEAFSALDPLIRKEMQnELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNI 242
Cdd:PRK10762  414 PKVLILDEPTRGVDVGAKKEIY-QLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 37-214 9.00e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 66.51  E-value: 9.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  37 YKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaKLREIRRKKIAMVFQNFAL 116
Cdd:PRK13540   11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTYQKQLCFVGHRSGI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 117 LPHRTVLENVAFGLEIQKVDVEerkkkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDP 196
Cdd:PRK13540   86 NPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160

                         170
                  ....*....|....*...
gi 1577416155 197 LirkemqnELLSLQTKMQ 214
Cdd:PRK13540  161 L-------SLLTIITKIQ 171
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 31-240 1.75e-12

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 64.39  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIyidnekitqvssaklREIRRKKIAMV 110
Cdd:cd03221     4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TWGSTVKIGYF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 111 FQnfallphrtvlenvafgleiqkvdveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEA 190
Cdd:cd03221    69 EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577416155 191 FSALDPLIRKEMQNELLSLqtkmQKTIVFITHD---LDealKIGDRIAIMKDG 240
Cdd:cd03221    98 TNHLDLESIEALEEALKEY----PGTVILVSHDryfLD---QVATKIIELEDG 143
hmuV PRK13547
heme ABC transporter ATP-binding protein;
38-256 1.82e-12

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 67.16  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  38 KHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCL-NRLIEPT-------SGEIYIDNEKITQVSSAKLREIR------ 103
Cdd:PRK13547   12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqa 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 104 -RKKIAMVFQNFALL---PHrtvlENVAFGLEIQKVDVeerkkkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALA 179
Cdd:PRK13547   92 aQPAFAFSAREIVLLgryPH----ARRAGALTHRDGEI------AWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 180 ---------TDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEE 250
Cdd:PRK13547  162 qlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241


                  ....*.
gi 1577416155 251 ILnSPA 256
Cdd:PRK13547  242 VL-TPA 246
PLN03211 PLN03211
ABC transporter G-25; Provisional
 27-222 2.47e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 68.37  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  27 GEKKTDLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTS--GEIYIDNEKITQVSsaklreirR 104
Cdd:PLN03211   68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI--------L 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 KKIAMVFQNFALLPHRTVLENVAFG--LEIQKVDVEERKKKAIE-MLEVVGLKGYE-----NAKPKELSGGMQQRVGLAR 176
Cdd:PLN03211  140 KRTGFVTQDDILYPHLTVRETLVFCslLRLPKSLTKQEKILVAEsVISELGLTKCEntiigNSFIRGISGGERKRVSIAH 219

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1577416155 177 ALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITH 222
Cdd:PLN03211  220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
CBS COG0517
CBS domain [Signal transduction mechanisms];
273-386 2.49e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 63.35  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 273 VSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDDL-----KSVIDTDIRTV 347
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLldtpvSEVMTRPPVTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1577416155 348 GVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGIIFKSTVL 386
Cdd:COG0517    81 SPDTSLEEAAELMEEHKIRrLPVVDDDGRLVGIITIKDLL 120
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 32-195 4.68e-12

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 67.27  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdNEKItqvssaklreirrkKIAMVF 111
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------------KLAYVD 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNF-ALLPHRTVLENVAFGLEIQKVDVEERKKKAieMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADILLMDE 189
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVLLLDE 469


                  ....*.
gi 1577416155 190 AFSALD 195
Cdd:TIGR03719 470 PTNDLD 475
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 285-387 5.11e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 62.26  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 285 IILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDDLKSVID----TDIRTVGVDTSIDEIIPLF 360
Cdd:cd02205     6 TVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAevmtPDVITVSPDTDLEEALELM 85

                          90       100
                  ....*....|....*....|....*...
gi 1577416155 361 LQSGYP-VAVVDDENKLKGIIFKSTVLA 387
Cdd:cd02205    86 LEHGIRrLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 286-386 6.29e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 61.77  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 286 ILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRdDLKSVIDTDIRTVGVDTSIDEIIPLFLQSGY 365
Cdd:cd04583     7 ITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRKAK-KVGEIMERDVFTVKEDSLLRDTVDRILKRGL 85

                          90       100
                  ....*....|....*....|..
gi 1577416155 366 P-VAVVDDENKLKGIIFKSTVL 386
Cdd:cd04583    86 KyVPVVDEQGRLVGLVTRASLV 107
PLN03130 PLN03130
ABC transporter C family member; Provisional
 45-254 8.22e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 67.07  E-value: 8.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSsaklreirrkKIAMVFqnfallpHRTVLE 124
Cdd:PLN03130   635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP----------QVSWIF-------NATVRD 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  125 NVAFGLEIQKvdveERKKKAIEM------LEVvgLKGYENAKPKE----LSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:PLN03130   698 NILFGSPFDP----ERYERAIDVtalqhdLDL--LPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  195 DPLIRKEMQNELLSLQTKmQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PLN03130   772 DAHVGRQVFDKCIKDELR-GKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSNN 829
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 45-204 5.01e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 61.43  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIF------------VVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQvssaklreIRRKKIAMVFQ 112
Cdd:PRK13541    6 QLQFNIEQKNLFdlsitflpsaitYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 113 NFALLPHRTVLENVAFGLEIqkVDVEERKKKAIEMLEvvgLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFS 192
Cdd:PRK13541   78 NLGLKLEMTVFENLKFWSEI--YNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152

                         170
                  ....*....|..
gi 1577416155 193 ALDPLIRKEMQN 204
Cdd:PRK13541  153 NLSKENRDLLNN 164
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 43-264 8.89e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 61.67  E-value: 8.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIyidnekitqVSSAKLReirrkkIAMVFQNFAL---LPh 119
Cdd:PRK09544   20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR------IGYVPQKLYLdttLP- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 RTVLENVAFGLEIQKVDVeerkkkaIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIR 199
Cdd:PRK09544   84 LTVNRFLRLRPGTKKEDI-------LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 200 KEMQNELLSLQTKMQKTIVFITHDLDEALKIGDRIAIMkDGNIVQIGEPEEILNSPadayvrEFI 264
Cdd:PRK09544  157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP------EFI 214
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 45-203 8.94e-11

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 63.78  E-value: 8.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEpTSGEIYIDNEKITQVSSAKLReirrkkiamvfQNFALLPHRTVLE 124
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-----------KAFGVIPQKVFIF 1304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  125 NVAFGleiQKVDVEER--KKKAIEMLEVVGLKGYENAKPKE-----------LSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:TIGR01271 1305 SGTFR---KNLDPYEQwsDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381

                          170
                   ....*....|....*.
gi 1577416155  192 SALDP----LIRKEMQ 203
Cdd:TIGR01271 1382 AHLDPvtlqIIRKTLK 1397
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 31-272 1.18e-10

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 61.79  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYK---HSVgVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEpTSGEIYIDNEKITQVSSAKLReirrkki 107
Cdd:cd03289     6 KDLTAKYTeggNAV-LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 108 amvfQNFALLPHRTVLENVAFGLEIQ---KVDVEERKKKAIEmlevVGLKGYENAKPKEL-----------SGGMQQRVG 173
Cdd:cd03289    77 ----KAFGVIPQKVFIFSGTFRKNLDpygKWSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 174 LARALATDADILLMDEAFSALDPLIRKEMQNELlsLQTKMQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILN 253
Cdd:cd03289   149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLN 225

                         250
                  ....*....|....*....
gi 1577416155 254 SpaDAYVREFIQDVNRTKI 272
Cdd:cd03289   226 E--KSHFKQAISPSDRLKL 242
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 45-224 1.30e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 63.51  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNekitqvsSAKLREIR----RKKIAMVFQNfALLPHR 120
Cdd:PTZ00265   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-------SHNLKDINlkwwRSKIGVVSQD-PLLFSN 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  121 TVLENVAFGLE----------------------------------------IQKVD----VEERKK-KAIEMLEVVGLK- 154
Cdd:PTZ00265   475 SIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDsnelIEMRKNyQTIKDSEVVDVSk 554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  155 -------------GYEN---AKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIV 218
Cdd:PTZ00265   555 kvlihdfvsalpdKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634


                   ....*.
gi 1577416155  219 FITHDL 224
Cdd:PTZ00265   635 IIAHRL 640
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
256-386 4.76e-10

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 58.74  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 256 ADAYVREFIQDVNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKtLLGIITIDKVSELMKENRDD 335
Cdd:COG2524    69 AAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLLKALAEGRDL 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 336 L----KSVIDTDIRTVGVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGIIFKSTVL 386
Cdd:COG2524   148 LdapvSDIMTRDVVTVSEDDSLEEALRLMLEHGIGrLPVVDDDGKLVGIITRTDIL 203
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 32-261 6.91e-10

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 59.15  E-value: 6.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVG--VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITQVSSAKLREirrkKIAM 109
Cdd:cd03288    24 DLCVRYENNLKpvLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 VFQNFALLPHrtvleNVAFGLEIQKVDVEERKKKAIEM-------------LEVVGLKGYENakpkeLSGGMQQRVGLAR 176
Cdd:cd03288   100 ILQDPILFSG-----SIRFNLDPECKCTDDRLWEALEIaqlknmvkslpggLDAVVTEGGEN-----FSVGQRQLFCLAR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 177 ALATDADILLMDEAFSALDPLIRKEMQNELLSlqTKMQKTIVFITHDLDEALKiGDRIAIMKDGNIVQIGEPEEIL---N 253
Cdd:cd03288   170 AFVRKSSILIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLaqeD 246


                  ....*...
gi 1577416155 254 SPADAYVR 261
Cdd:cd03288   247 GVFASLVR 254
PLN03232 PLN03232
ABC transporter C family member; Provisional
 43-254 1.20e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 60.37  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRC-LNRLIEPTSGEIYIdnekitqvssaklreirRKKIAMVFQnFALLPHRT 121
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVI-----------------RGSVAYVPQ-VSWIFNAT 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  122 VLENVAFGLEIQkvdvEERKKKAIEMLEVVG----LKGYENAKPKE----LSGGMQQRVGLARALATDADILLMDEAFSA 193
Cdd:PLN03232   695 VRENILFGSDFE----SERYWRAIDVTALQHdldlLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155  194 LDPLIRKEMQNELLSLQTKmQKTIVFITHDLdEALKIGDRIAIMKDGNIVQIGEPEEILNS 254
Cdd:PLN03232   771 LDAHVAHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKS 829
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 275-380 2.72e-09

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 54.84  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 275 ASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITI-DKVSELMKENRDDL----KSVIDTDIRTVGV 349
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDrDLRRRVLAEGLDPLdtpvSEVMTRPPITVSP 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1577416155 350 DTSIDEIIPLFLQSGYPVAVVDDENKLKGII 380
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIV 111
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 1-223 4.16e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.42  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   1 MAKIQVKNVYKVFGSAPmqmisflekgekktdLLkkykhsvgvNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPT 80
Cdd:PRK11147    1 MSLISIHGAWLSFSDAP---------------LL---------DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  81 SGEIYIDNEkitqVSSAKLREIRRKKIAmvfqnfallphRTVLENVAFGLEIQ------------KVDVEERKK------ 142
Cdd:PRK11147   57 DGRIIYEQD----LIVARLQQDPPRNVE-----------GTVYDFVAEGIEEQaeylkryhdishLVETDPSEKnlnela 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 143 KAIEMLEVVGLKGYEN--------------AKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLS 208
Cdd:PRK11147  122 KLQEQLDHHNLWQLENrinevlaqlgldpdAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT 201

                         250
                  ....*....|....*
gi 1577416155 209 LqtkmQKTIVFITHD 223
Cdd:PRK11147  202 F----QGSIIFISHD 212
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
31-248 5.37e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.90  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  31 TDLLKKYkhsvgvNNVSFSVNEGEIFV-----VMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnEKItqvsSAKLREIRRK 105
Cdd:PRK13409  344 PDLTKKL------GDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI----SYKPQYIKPD 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 106 KIAMVFQnfallphrtVLENVAFGLEIQKVDVEERKKKAIEMLevvglkgYENaKPKELSGGMQQRVGLARALATDADIL 185
Cdd:PRK13409  413 YDGTVED---------LLRSITDDLGSSYYKSEIIKPLQLERL-------LDK-NVKDLSGGELQRVAIAACLSRDADLY 475

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 186 LMDEAFSALD--------PLIRKEMQNEllslqtkmQKTIVFITHDLDEALKIGDRIaimkdgnIVQIGEP 248
Cdd:PRK13409  476 LLDEPSAHLDveqrlavaKAIRRIAEER--------EATALVVDHDIYMIDYISDRL-------MVFEGEP 531
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 43-223 5.52e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.04  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdnekitqvsSAKLreirrkKIAMVFQNFALL-PHRT 121
Cdd:PRK11147  335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---------GTKL------EVAYFDQHRAELdPEKT 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 122 VLENVAFGLeiQKVDVEERKKKAIEMLEVVGLKGYENAKP-KELSGGMQQRVGLARALATDADILLMDEAFSALD--PLi 198
Cdd:PRK11147  400 VMDNLAEGK--QEVMVNGRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDveTL- 476

                         170       180
                  ....*....|....*....|....*.
gi 1577416155 199 rkemqnELL-SLQTKMQKTIVFITHD 223
Cdd:PRK11147  477 ------ELLeELLDSYQGTVLLVSHD 496
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
274-380 6.05e-09

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 57.38  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 274 SASSIMrSSESIIL-EKAGVRTAAKKMKDLE-----ISSIFVTDKHKTLLGIITIdkvSELMKENRDD-LKSVIDTDIRT 346
Cdd:COG2239   130 SAGRLM-TTEFVAVrEDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSL---RDLLLADPDTkVSDIMDTDVIS 205

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1577416155 347 VGVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGII 380
Cdd:COG2239   206 VPADDDQEEVARLFERYDLLaLPVVDEEGRLVGII 240
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 32-189 6.35e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 57.44  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIdNEKItqvssaklreirrkKIAMVF 111
Cdd:PRK11819  329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------------KLAYVD 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 112 QNF-ALLPHRTVLENVAFGLEIQKVDVEERKKKAiemleVVG---LKGYENAKP-KELSGGMQQRVGLARALATDADILL 186
Cdd:PRK11819  394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSRA-----YVGrfnFKGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLL 468


                  ...
gi 1577416155 187 MDE 189
Cdd:PRK11819  469 LDE 471
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 274-380 8.25e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 53.11  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 274 SASSIMrSSESIIL-EKAGVRTAAKKMKDLE-----ISSIFVTDKHKTLLGIITIdkvSELMKENRDD-LKSVIDTDIRT 346
Cdd:cd04606     2 SAGRLM-TTEFVAVrPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSL---RDLLLADPDTkVSDIMDTDVIS 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1577416155 347 VGVDTSIDEIIPLFLQSGYPVA-VVDDENKLKGII 380
Cdd:cd04606    78 VSADDDQEEVARLFAKYDLLALpVVDEEGRLVGII 112
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 33-246 1.42e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.04  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   33 LLKKYKHSVGVN---NVSFSVNEGEIFVVMGLSGSGKSTLIRCLnrlieptSGEIY---IDNEKITQVSSAKLREIRRKK 106
Cdd:TIGR00956   64 KLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTI-------ASNTDgfhIGVEGVITYDGITPEEIKKHY 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  107 IAMVF---QNFALLPHRTVLENVAF-------GLEIQKVDVEERKKKAIEM-LEVVGLKGYENAKP-----KELSGGMQQ 170
Cdd:TIGR00956  137 RGDVVynaETDVHFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVgndfvRGVSGGERK 216

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577416155  171 RVGLARALATDADILLMDEAFSALDPLIRKEMQNeLLSLQTKMQKTIVFIT--HDLDEALKIGDRIAIMKDGNIVQIG 246
Cdd:TIGR00956  217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIR-ALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFG 293
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 32-224 1.89e-08

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 54.68  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSF----SVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEiYIDNEKITQVSSA---------- 97
Cdd:cd03236     1 ELEDEPVHRYGPNSFKLhrlpVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEfrgselqnyf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  98 -KLREiRRKKIAMVFQNFALLPhRTVLENVafGLEIQKVDVEERKKKAIEMLEvvgLKGYENAKPKELSGGMQQRVGLAR 176
Cdd:cd03236    80 tKLLE-GDVKVIVKPQYVDLIP-KAVKGKV--GELLKKKDERGKLDELVDQLE---LRHVLDRNIDQLSGGELQRVAIAA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1577416155 177 ALATDADILLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDL 224
Cdd:cd03236   153 ALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDL 199
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 44-195 2.17e-08

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 53.79  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCL-NRLIEPT-SGEIYIDNEKITQvssaklrEIRRkKIAMVFQNFALLPHRT 121
Cdd:cd03232    24 NNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLDK-------NFQR-STGYVEQQDVHSPNLT 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 122 VLENVAFGLEIQKVDVEERKkkaiemlevvglkgyenakpkelsggmqqRVGLARALATDADILLMDEAFSALD 195
Cdd:cd03232    96 VREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLD 140
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
33-251 2.26e-08

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 55.51  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  33 LLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSG--KSTLIRclnRLIEPTSGE------IYIDNEKITQVSSAKLREIRR 104
Cdd:NF000106   19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPA---HV*GPDAGRrpwrf*TWCANRRALRRTIG*HRPVR* 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 105 KKiamvFQNFAllpHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKGYENAKpkeLSGGMQQRVGLARALATDADI 184
Cdd:NF000106   96 GR----RESFS---GRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK---YSGGMRRRLDLAASMIGRPAV 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIVQIGEPEEI 251
Cdd:NF000106  166 LYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-249 2.86e-08

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 52.38  E-value: 2.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   53 GEIFVVMGLSGSGKSTLIRCLNRLIEPTSGE-IYIDNEKITQVSSAKLREIrrkkiamvfqnfallphrtvlenvafgle 131
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLI----------------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  132 iqkvdveerkkkaiemlevvglkgYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQT 211
Cdd:smart00382  53 ------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1577416155  212 KM-----QKTIVFITHDLDEalkIGDRIAIMKDGNIVQIGEPE 249
Cdd:smart00382 109 LLlksekNLTVILTTNDEKD---LGPALLRRRFDRRIVLLLIL 148
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 49-248 3.76e-08

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.18  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  49 SVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDnEKItqvsSAKLREIRRKKIAMVfqnfallphRTVLENVAf 128
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKI----SYKPQYISPDYDGTV---------EEFLRSAN- 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 129 gleiqKVDVEERKKKAiEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSALD--------PLIRK 200
Cdd:COG1245   427 -----TDDFGSSYYKT-EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 201 EMQNEllslqtkmQKTIVFITHDL---DealKIGDRIaimkdgnIVQIGEP 248
Cdd:COG1245   501 FAENR--------GKTAMVVDHDIyliD---YISDRL-------MVFEGEP 533
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 43-249 3.78e-08

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 53.88  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIRCL--NRLIEPTSGEIYIDNEKITQVSSaklREIRRKKIAMVFQNFALLPH- 119
Cdd:CHL00131   23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEP---EERAHLGIFLAFQYPIEIPGv 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 ------RTVLENVAFGLEIQKVDVEERKKKAIEMLEVVGLKG-YENAKPKE-LSGGMQQRVGLARALATDADILLMDEAF 191
Cdd:CHL00131  100 snadflRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETD 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 192 SALDPLIRKEMQNELLSLQTKmQKTIVFITH--DLDEALKiGDRIAIMKDGNIVQIGEPE 249
Cdd:CHL00131  180 SGLDIDALKIIAEGINKLMTS-ENSIILITHyqRLLDYIK-PDYVHVMQNGKIIKTGDAE 237
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 276-380 5.46e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 50.70  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 276 SSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDDLKSVIDTDIRTVGVDTSIDE 355
Cdd:cd04605     3 EDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALKKDSLEEIMTRNVITARPDEPIEL 82

                          90       100
                  ....*....|....*....|....*...
gi 1577416155 356 IIPLFLQ---SGYPvaVVDDENKLKGII 380
Cdd:cd04605    83 AARKMEKhniSALP--VVDDDRRVIGII 108
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
272-386 2.21e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 49.53  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 272 IVSASSIMRSSESIIL-EKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVseLMKENRDDLKSVIDTDIRTVGVD 350
Cdd:COG4109    15 ILLVEDIMTLEDVATLsEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDI--LGKDDDTPIEDVMTKNPITVTPD 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1577416155 351 TSIDEIIPLFLQSGYPVA-VVDDENKLKGIIFKSTVL 386
Cdd:COG4109    93 TSLASAAHKMIWEGIELLpVVDDDGRLLGIISRQDVL 129
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 45-223 5.74e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 51.43  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYID-NEKItqvssAKLREIRrkkiaMVFQNFallphrTVL 123
Cdd:PRK15064   19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERL-----GKLRQDQ-----FAFEEF------TVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 124 ENVAFG-LEIQKVDVEerkKKAI----EMLEVVGLK------------GYE-NAKPKEL-----------SGGMQQ---- 170
Cdd:PRK15064   83 DTVIMGhTELWEVKQE---RDRIyalpEMSEEDGMKvadlevkfaemdGYTaEARAGELllgvgipeeqhYGLMSEvapg 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 171 ---RVGLARALATDADILLMDEAFSALDPLIRKEMQNELlslqTKMQKTIVFITHD 223
Cdd:PRK15064  160 wklRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
GguA NF040905
sugar ABC transporter ATP-binding protein;
43-243 7.49e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.94  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLI-----RCLNRLIeptSGEIYIDNEKItQVSSAKlREIR---------RKKIA 108
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgRSYGRNI---SGTVFKDGKEV-DVSTVS-DAIDaglayvtedRKGYG 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 109 MVF-----QNFAL-----LPHRTVLENVAfglEIqKVDVEERKK---KAIEMLEVVGlkgyenakpkELSGGMQQRVGLA 175
Cdd:NF040905  351 LNLiddikRNITLanlgkVSRRGVIDENE---EI-KVAEEYRKKmniKTPSVFQKVG----------NLSGGNQQKVVLS 416

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 176 RALATDADILLMDEAFSALDPLIRKEMQ---NELlslqTKMQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:NF040905  417 KWLFTDPDVLILDEPTRGIDVGAKYEIYtiiNEL----AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 164-250 1.15e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 50.50  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 164 LSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSLQTKmQKTIVFITHDLDEALKIGDRIAIMKDGNIV 243
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470


                  ....*..
gi 1577416155 244 QIGEPEE 250
Cdd:PRK10982  471 GIVDTKT 477
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 58-223 1.21e-06

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 50.32  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  58 VMGLSGSGKSTLIRCLNRLIEPTSGEiyidnekitqvssAKLREIRrkKIAMVFQNFALLPHRTVLENVAFGL-EIQKV- 135
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPGI--KVGYLPQEPQLDPTKTVRENVEEGVaEIKDAl 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 136 -------------DVE-----ERKKKAIEMLEVVGLKGYEN---------------AKPKELSGGMQQRVGLARALATDA 182
Cdd:TIGR03719 101 drfneisakyaepDADfdklaAEQAELQEIIDAADAWDLDSqleiamdalrcppwdADVTKLSGGERRRVALCRLLLSKP 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1577416155 183 DILLMDEAFSALDPLIRKEMQNELlslqTKMQKTIVFITHD 223
Cdd:TIGR03719 181 DMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 309-388 1.71e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 46.79  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 309 VTDKHKTLLGIITidkVSELMKENRDD----------------------LKSVIDTDIRTVGVDTSIDEIIPLFLQSGYP 366
Cdd:cd04600    31 VVDRARRLVGIVT---LADLLKHADLDpprglrgrlrrtlglrrdrpetVGDIMTRPVVTVRPDTPIAELVPLFSDGGLH 107

                          90       100
                  ....*....|....*....|...
gi 1577416155 367 -VAVVDDENKLKGIIFKSTVLAG 388
Cdd:cd04600   108 hIPVVDADGRLVGIVTQSDLIAA 130
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 52-224 1.73e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 50.17  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  52 EGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIyiDNE----KITQVSSAK-----LREIRRKKI--AMVFQNFALLPH- 119
Cdd:COG1245    98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEpswdEVLKRFRGTelqdyFKKLANGEIkvAHKPQYVDLIPKv 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 120 -----RTVLEnvafgleiqKVDveERKKkAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEAFSAL 194
Cdd:COG1245   176 fkgtvRELLE---------KVD--ERGK-LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1577416155 195 DplIRKEMQ-----NELlslqTKMQKTIVFITHDL 224
Cdd:COG1245   244 D--IYQRLNvarliREL----AEEGKYVLVVEHDL 272
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
116-252 1.85e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 50.12  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 116 LLPHRTVLENVAF-----GLeiqkvDVEERKKKAIEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDADILLMDEA 190
Cdd:NF033858   89 LYPTLSVFENLDFfgrlfGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 191 FSALDPLIRK---EMQNELLSLQTKMqkTIVFITHDLDEALKIgDRIAIMKDGNIVQIGEPEEIL 252
Cdd:NF033858  164 TTGVDPLSRRqfwELIDRIRAERPGM--SVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 279-380 1.92e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 46.36  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 279 MRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKENRDDLKSVID---TDIRTVGVDTSIDE 355
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVEEimtKNLVTVSPDESIYE 80

                          90       100
                  ....*....|....*....|....*.
gi 1577416155 356 IIPLFLQSGYP-VAVVDDENKLKGII 380
Cdd:cd09836    81 AAELMREHNIRhLPVVDGGGKLVGVI 106
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 50-248 2.01e-06

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 47.57  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  50 VNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEIYIDNEKITqvssaklreirrkkiamvfqnfallphrtvlenvafg 129
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 130 LEIQKVDveerkkkaiemlevvglkgyenakpkeLSGGMQQRVGLARALATDADILLMDEAFSALDPLIRKEMQNELLSL 209
Cdd:cd03222    65 YKPQYID---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1577416155 210 QTKMQKTIVFITHDLDEALKIGDRIaimkdgnIVQIGEP 248
Cdd:cd03222   118 SEEGKKTALVVEHDLAVLDYLSDRI-------HVFEGEP 149
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 292-380 4.64e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 45.23  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTLLGIIT-IDKVSELMKENRD--DLK--SVIDTDIRTVGVDTSIDEIIPLFLQSG-- 364
Cdd:cd17775    14 VLEAARLMRDHHVGSVVVVEEDGKPVGIVTdRDIVVEVVAKGLDpkDVTvgDIMSADLITAREDDGLFEALERMREKGvr 93

                          90
                  ....*....|....*..
gi 1577416155 365 -YPvaVVDDENKLKGII 380
Cdd:cd17775    94 rLP--VVDDDGELVGIV 108
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
39-224 7.51e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.88  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  39 HSVGVNnvSFS------VNEGEIFVVMGLSGSGKSTLIRCL--------NRLIEPTSGEIYIDNEKITQVSS--AKLREi 102
Cdd:PRK13409   81 HRYGVN--GFKlyglpiPKEGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDEVLKRFRGTELQNyfKKLYN- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 103 RRKKIAMVFQNFALLPhRTVLENVAFGLEiqKVDveERKKKAiEMLEVVGLKGYENAKPKELSGGMQQRVGLARALATDA 182
Cdd:PRK13409  158 GEIKVVHKPQYVDLIP-KVFKGKVRELLK--KVD--ERGKLD-EVVERLGLENILDRDISELSGGELQRVAIAAALLRDA 231

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 183 DILLMDEAFSALD--------PLIRKEMQNellslqtkmqKTIVFITHDL 224
Cdd:PRK13409  232 DFYFFDEPTSYLDirqrlnvaRLIRELAEG----------KYVLVVEHDL 271
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 36-195 8.52e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 48.18  E-value: 8.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155   36 KYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLircLNRLIEPTSGEIYIDNEKItqVSSAKLREIRRKKIAMVFQNFA 115
Cdd:TIGR00956  772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTL---LNVLAERVTTGVITGGDRL--VNGRPLDSSFQRSIGYVQQQDL 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  116 LLPHRTVLENVAFGLEI---QKVDVEERKKKAIEMLEVVGLKGYENA---KPKE-LSGGMQQRVGLARALATDADILL-M 187
Cdd:TIGR00956  847 HLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfL 926


                   ....*...
gi 1577416155  188 DEAFSALD 195
Cdd:TIGR00956  927 DEPTSGLD 934
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 44-242 1.19e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 47.32  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  44 NNVSFSVNEGEIFVVMGLSGSGKSTLIRCL---------NRLI----EPTSGEIYID-NEKITQVSSAKLREIRRKKIAm 109
Cdd:PRK10938  277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTlfgrRRGSGETIWDiKKHIGYVSSSLHLDYRVSTSV- 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 110 vfqnfallphRTVLENVAF---GLeIQKVDvEERKKKAIEMLEVVGLKGYENAKP-KELSGGmQQRVGL-ARALATDADI 184
Cdd:PRK10938  356 ----------RNVILSGFFdsiGI-YQAVS-DRQQKLAQQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTL 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577416155 185 LLMDEAFSALDPLIRKEMQNELLSLQTKMQKTIVFITHDLDEALK-IGDRIAIMKDGNI 242
Cdd:PRK10938  423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 292-380 2.22e-05

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 43.18  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDkHKTLLGIIT-----IDKVSELMKENRDDLKSVIDTDIRTVGVDTSIDEIIPLFlqSGYP 366
Cdd:cd04622    14 LREAARLMRDLDIGALPVCE-GDRLVGMVTdrdivVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARLM--AEHQ 90

                          90
                  ....*....|....*..
gi 1577416155 367 V---AVVDDENKLKGII 380
Cdd:cd04622    91 VrrlPVVDDDGRLVGIV 107
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 292-381 4.24e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 42.40  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTLLGIIT---ID-------KVSELM-KENRddlksvidtdIRTVGVDTSIDEIIPLF 360
Cdd:cd04601    13 VADVLELKAEYGISGVPVTEDGGKLVGIVTsrdIRfetdlstPVSEVMtPDER----------LVTAPEGITLEEAKEIL 82

                          90       100
                  ....*....|....*....|...
gi 1577416155 361 LQS--GYpVAVVDDENKLKGIIF 381
Cdd:cd04601    83 HKHkiEK-LPIVDDNGELVGLIT 104
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 288-387 7.29e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 41.65  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 288 EKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIIT-----------------IDKVSELMKenrddlksvidTDIRTVGVD 350
Cdd:cd04629    10 PDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSeqdclkalleasyhcepGGTVADYMS-----------TEVLTVSPD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1577416155 351 TSIDEIIPLFLQSG---YPvaVVDDeNKLKGIIFKSTVLA 387
Cdd:cd04629    79 TSIVDLAQLFLKNKprrYP--VVED-GKLVGQISRRDVLR 115
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 292-381 1.50e-04

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 43.53  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKhKTLLGIIT----------IDKVSELMKenRDDLKsvidtdirTVGVDTSIDEIIPLFL 361
Cdd:pfam00478  99 VADALALMERYGISGVPVVDD-GKLVGIVTnrdlrfetdlSQPVSEVMT--KENLV--------TAPEGTTLEEAKEILH 167

                          90       100
                  ....*....|....*....|...
gi 1577416155 362 QSG---YPVavVDDENKLKGIIF 381
Cdd:pfam00478 168 KHKiekLPV--VDDNGRLVGLIT 188
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 275-331 2.05e-04

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 39.12  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 275 ASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMKE 331
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 32-254 3.61e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 42.57  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  32 DLLKKYKHSVGVNNVSFSVNEGEIFVVMGLSGSGKSTLIRCLNRLIEPTSGEI-YIDNEKI---TQVSSAK--------- 98
Cdd:PRK15064  324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIgyyAQDHAYDfendltlfd 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  99 -LREIRRKK--IAMVfqnfallphRTVLENVAFGleiqkvdVEERKKKAiemlevvglkgyenakpKELSGGMQQRVGLA 175
Cdd:PRK15064  404 wMSQWRQEGddEQAV---------RGTLGRLLFS-------QDDIKKSV-----------------KVLSGGEKGRMLFG 450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 176 RALATDADILLMDEAFSALDplirkeMQN-ELLSLQTKM-QKTIVFITHDLDEALKIGDRIAIMKDGNIVQI-GEPEEIL 252
Cdd:PRK15064  451 KLMMQKPNVLVMDEPTNHMD------MESiESLNMALEKyEGTLIFVSHDREFVSSLATRIIEITPDGVVDFsGTYEEYL 524


                  ..
gi 1577416155 253 NS 254
Cdd:PRK15064  525 RS 526
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 292-356 3.67e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 39.72  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKtLLGIITidkvselmkenrddlksviDTDIRT------VGVDTSIDEI 356
Cdd:cd04587    15 IQEAAQLMSEERVSSLLVVDDGR-LVGIVT-------------------DRDLRNrvvaegLDPDTPVSEI 65
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 292-380 7.64e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 39.13  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTlLGIITidkvselmkeNRDDLK--------------SVIDTDIRTVGVDTSIDEII 357
Cdd:cd09833    16 LADAAARMAERRCSSILIVENGEI-VGIWT----------ERDALKldfsdpdafrrpisEVMSSPVLTIPQDTTLGEAA 84

                          90       100
                  ....*....|....*....|....
gi 1577416155 358 PLFLQSGYP-VAVVDDENKLKGII 380
Cdd:cd09833    85 VRFRQEGVRhLLVVDDDGRPVGIV 108
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 336-391 7.66e-04

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.19  E-value: 7.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577416155 336 LKSVIDTDIRTVGVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGIIFKSTVLAGIAG 391
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISrLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 342-380 7.92e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 39.34  E-value: 7.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1577416155 342 TDIRTVGVDTSIDEIIPLFLQ---SGYPVavVDDENKLKGII 380
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEhriSGLPV--VDDDGKLVGIV 42
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
52-224 9.30e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 39.99  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  52 EGEIFVVMGLSGSGKSTLIRCL---------------NRLIEPTSGEIYI----------------DNEKITQVSSAklR 100
Cdd:COG0419    22 DDGLNLIVGPNGAGKSTILEAIryalygkarsrsklrSDLINVGSEEASVelefehggkryrierrQGEFAEFLEAK--P 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 101 EIRRKKIAMVFQNFALLPHRTVLENVAFGLEIQKVDVEERKKKAIEMLEVvgLKGYENakPKELSGGMQQRVGLARALAt 180
Cdd:COG0419   100 SERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQ--LSGLDP--IETLSGGERLRLALADLLS- 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1577416155 181 dadiLLMDeaFSALDPLIRKEMQNELLSLQtkmqktivFITHDL 224
Cdd:COG0419   175 ----LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 288-380 9.56e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 38.94  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 288 EKAGVRTAAKKMKDLEISSIFVTDKHKtLLGIIT--------IDKVSELMKENRDDL------KSVIDTDIRTVGVDTSI 353
Cdd:cd04584    15 PDTSLAEARELMKEHKIRHLPVVDDGK-LVGIVTdrdllrasPSKATSLSIYELNYLlskipvKDIMTKDVITVSPDDTV 93

                          90       100
                  ....*....|....*....|....*..
gi 1577416155 354 DEIIPLFLQSGYPVAVVDDENKLKGII 380
Cdd:cd04584    94 EEAALLMLENKIGCLPVVDGGKLVGII 120
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 292-387 1.02e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 38.67  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTLLGIIT----IDKVSELMKENRDDLKSVIDTDIRTVGVDTSIDEIIPLFlQSGYPV 367
Cdd:cd04608    21 LGEAIEIMREYGVDQLPVVDEDGRVVGMVTegnlLSSLLAGRAQPSDPVSKAMYKQFKQVDLDTPLGALSRIL-ERDHFA 99

                          90       100
                  ....*....|....*....|
gi 1577416155 368 AVVDDENKLKGIIFKSTVLA 387
Cdd:cd04608   100 LVVDGQGKVLGIVTRIDLLN 119
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
251-380 1.13e-03

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 39.87  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 251 ILNSPADAYVREFIQDVNRTKIVSASSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSELMK 330
Cdd:COG2524     3 VLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577416155 331 ENRDDLKSVIDTDIRTVGVDTSIDEIIPLFLQSGYPVAVVDDENKLKGII 380
Cdd:COG2524    83 VLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGII 132
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
262-347 1.65e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 40.59  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 262 EFIQDVnRTKIvsaSSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSE-LMKENRDDLKSVI 340
Cdd:PRK14869   61 ELIEDV-KPQV---RDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARaYMDILDPEILSKS 136


                  ....*..
gi 1577416155 341 DTDIRTV 347
Cdd:PRK14869  137 PTSLENI 143
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 43-234 1.77e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 38.84  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  43 VNNVSFSVNEGEIFVVMGLSGSGKSTLIrclnrlieptsgeiyidnekitqvsSAKLREIRRKKIAMVFQNFAllPHRTV 122
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------------NEGLYASGKARLISFLPKFS--RNKLI 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 123 LenvafgleiqkVDveerkkkAIEMLEVVGLkGY--ENAKPKELSGGMQQRVGLARALA--TDADILLMDEAFSALDPLI 198
Cdd:cd03238    64 F-----------ID-------QLQFLIDVGL-GYltLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQD 124

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1577416155 199 RKEMQNELLSLQTKmQKTIVFITHDLDeALKIGDRI 234
Cdd:cd03238   125 INQLLEVIKGLIDL-GNTVILIEHNLD-VLSSADWI 158
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 305-389 1.83e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 38.25  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 305 SSIFVTDKHKTLLGIITIDKVSELMKENRD---------DLKSVIDTDIRTVGVDTSIDEIIPL-----FLqsgypvAVV 370
Cdd:cd04643    31 SRIPVLDKDYKLVGLISLSMILDAILGLERiefeklselKVEEVMNTDVPTVSPDDDLEEVLHLlvdhpFL------CVV 104

                          90
                  ....*....|....*....
gi 1577416155 371 DDENKLKGIIFKSTVLAGI 389
Cdd:cd04643   105 DEDGYFLGIITRREILKAV 123
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 257-385 1.92e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 37.94  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 257 DAYVREFiqdvnrtKIVSASSIMRS-SESIILEKAgvrtaakkmkdlEISSIFVTDKHKTLLGIITIDKVSELMKENRDD 335
Cdd:cd04639     1 DAMVTEF-------PIVDADLTLREfADDYLIGKK------------SWREFLVTDEAGRLVGLITVDDLRAIPTSQWPD 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577416155 336 --LKSVI--DTDIRTVGVDTSIDEIIPLFLQSGYP-VAVVDDENKLKGIIFKSTV 385
Cdd:cd04639    62 tpVRELMkpLEEIPTVAADQSLLEVVKLLEEQQLPaLAVVSENGTLVGLIEKEDI 116
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 292-380 2.17e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 37.40  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTLLGIIT----IDKVSELMKENRDDL-KSVIDTDIRTVGVDTSIDEI---------- 356
Cdd:cd04623    13 VAEALRLLAEKNIGALVVVDDGGRLVGILSerdyVRKLALRGASSLDTPvSEIMTRDVVTCTPDDTVEECmalmterrir 92

                          90       100
                  ....*....|....*....|....*
gi 1577416155 357 -IPlflqsgypvaVVDDeNKLKGII 380
Cdd:cd04623    93 hLP----------VVED-GKLVGIV 106
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
250-321 2.86e-03

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.54  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 250 EILNSPADAYVREFIQDVNRTKIvsaSSIMRSSESIILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIIT 321
Cdd:COG3448    53 DLLRALLPDRLDELEERLLDLPV---EDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVT 121
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 45-251 3.44e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.61  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  45 NVSFSVNEGEIFVVMGLSGSGKSTLI-----RCLNRLI-----EPTSGE-----------IYIDNEKI--TQVSS----- 96
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLIndtlyPALANRLngaktVPGRYTsieglehldkvIHIDQSPIgrTPRSNpatyt 705

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  97 ----------AKLREIRRK-------------------------KIAMVFQNFALLP---------HRTVLE------NV 126
Cdd:TIGR00630 706 gvfdeirelfAETPEAKVRgytpgrfsfnvkggrceacqgdgviKIEMHFLPDVYVPcevckgkryNRETLEvkykgkNI 785

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 127 AfglEIQKVDVEERKK---------KAIEMLEVVGLkGY----ENAKpkELSGGMQQRVGLARAL---ATDADILLMDEA 190
Cdd:TIGR00630 786 A---DVLDMTVEEAYEffeavpsisRKLQTLCDVGL-GYirlgQPAT--TLSGGEAQRIKLAKELskrSTGRTLYILDEP 859

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577416155 191 FSAL---DplIRKEMQnellSLQTKMQK--TIVFITHDLDeALKIGDRIAIM------KDGNIVQIGEPEEI 251
Cdd:TIGR00630 860 TTGLhfdD--IKKLLE----VLQRLVDKgnTVVVIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
PLN03073 PLN03073
ABC transporter F family; Provisional
 160-222 4.10e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 39.46  E-value: 4.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577416155 160 KPKELSGGMQQRVGLARALATDADILLMDEAFSALDplirkemQNELLSLQT---KMQKTIVFITH 222
Cdd:PLN03073  341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-------LHAVLWLETyllKWPKTFIVVSH 399
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 285-380 4.36e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 36.80  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 285 IILEKAGVRTAAKKMKDLEISSIFVTDKHKTLLGIITiDK------VSELMKENRDDLKSVIDTDIRTVGVDTSIDEIIP 358
Cdd:cd17781     6 TVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFT-DKdlarrvVASGLDPRSTLVSSVMTPNPLCVTMDTSATDALD 84

                          90       100
                  ....*....|....*....|....*
gi 1577416155 359 LFLQSGY---PvaVVDDENKLKGII 380
Cdd:cd17781    85 LMVEGKFrhlP--VVDDDGDVVGVL 107
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 286-386 4.55e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.71  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 286 ILEKAGVRTAAKKMKDLEISSIFVTDKHKtLLGIIT---IDKV--SELMKEnrdDLKSVIDTDIRTVGVDTSIDEIIPLF 360
Cdd:cd04595     7 VSPDTTIEEARKIMLRYGHTGLPVVEDGK-LVGIISrrdVDKAkhHGLGHA---PVKGYMSTNVITIDPDTSLEEAQELM 82

                          90       100
                  ....*....|....*....|....*.
gi 1577416155 361 LQSGYPVAVVDDENKLKGIIFKSTVL 386
Cdd:cd04595    83 VEHDIGRLPVVEEGKLVGIVTRSDVL 108
CBS_pair_KefB_assoc cd04603
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 292-386 5.27e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain which is involved in inorganic ion transport and metabolism. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341377 [Multi-domain]  Cd Length: 112  Bit Score: 36.67  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 292 VRTAAKKMKDLEISSIFVTDKHKTLLGIITIDKVSElMKENRDDLKSVIDTDIR---TVGVDTSIDEIIPLFLQSGYP-V 367
Cdd:cd04603    13 LREIIKKITELNARAIVIVNNNMSVLGQITVSDLLE-IGPSQYETLTAYDLILVpliRVNCDAPITDLLRKFRETDPPiI 91

                          90
                  ....*....|....*....
gi 1577416155 368 AVVDDENKLKGIIFKSTVL 386
Cdd:cd04603    92 AVIDDESKFIGTIYERELL 110
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 305-389 5.46e-03

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 37.04  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 305 SSIFVTDKHKTLLGIITIDKVSELMKENRD---------DLKSVIDTDIRTVGVDTSIDEIIPL-----FLqsgypvAVV 370
Cdd:NF041630   43 SKIPVLDKDKKFVGLISLSDITDYMLGLERiefeklselKVADVMNTDVPTITDDYDLEEILHLlvdhpFL------PVV 116

                          90
                  ....*....|....*....
gi 1577416155 371 DDENKLKGIIFKSTVLAGI 389
Cdd:NF041630  117 DEDGIFLGIITRREILKAV 135
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 55-69 6.22e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 37.03  E-value: 6.22e-03
                          10
                  ....*....|....*
gi 1577416155  55 IFVVMGLSGSGKSTL 69
Cdd:COG3265     3 VIVVMGVSGSGKSTV 17
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 34-238 7.93e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 36.95  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155  34 LKKYKHSVGVNNVSFSvnEGEIFVVMGLSGSGKSTLIRCLnrlieptsgeIYIdnekitqVSSAKLREIRRKKIAmvfqn 113
Cdd:cd03227     4 LGRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAI----------GLA-------LGGAQSATRRRSGVK----- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577416155 114 fallphrtVLENVAfgleiqkvdveerkkkAIEMLEVVGLKGyenakpkeLSGGMQQRVGLARALA----TDADILLMDE 189
Cdd:cd03227    60 --------AGCIVA----------------AVSAELIFTRLQ--------LSGGEKELSALALILAlaslKPRPLYILDE 107

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577416155 190 AFSALDPlirkemQN-----ELLSLQTKMQKTIVFITHDLDEALKIgDRIAIMK 238
Cdd:cd03227   108 IDRGLDP------RDgqalaEAILEHLVKGAQVIVITHLPELAELA-DKLIHIK 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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