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Conserved domains on  [gi|1405942281|gb|PZX82098|]
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ABC transporter substrate-binding protein [Klebsiella variicola]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467437)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including Fe(3+) ions and polyamines such as spermidine and putrescine

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0042626|GO:0140359|GO:0005524|GO:0016887
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 7-222 4.70e-120

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 345.54  E-value: 4.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 7-222 4.70e-120

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 345.54  E-value: 4.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 7-222 2.70e-106

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: 305.21  E-value: 2.70e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT----GVPPERRNIGM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03259    77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03259   157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-220 8.70e-90

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 269.12  E-value: 8.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTP-ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPP 79
Cdd:PRK09452    8 PSSLSPlVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQRDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK09452   84 ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK09452  164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 7-219 5.17e-79

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 241.09  E-value: 5.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
7-233 5.15e-74

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 228.34  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAG-WGLPPEQ 81
Cdd:NF040933    3 VRVENVTKIFkkgkKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGkIIVPPED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:NF040933   83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT-----PTSGEVA 233
Cdd:NF040933  163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEeiydnPANIFVA 239
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-233 4.02e-67

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 210.32  E-value: 4.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGMVFQDYALWPHMSVAQ 101
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN----LPPEKRGIAYVYQNYMLFPHKTVFE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCG 181
Cdd:NF040840   92 NIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 182 EMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT-----PTSGEVA 233
Cdd:NF040840  172 EMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVRevfrrPKNEFVA 228
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 22-169 2.15e-52

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: 166.28  E-value: 2.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWGLPPEQRDIGMVFQDYALWPHMSVAQ 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD--DERKSLRKEIGYVFQDPQLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERK----PSGLSGGQQQRVALARAIVAAPRVLLFDEPLS 169
Cdd:pfam00005  79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
18-218 4.45e-47

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 154.88  E-value: 4.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRD------IGMVFQDY 91
Cdd:NF038007   17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT----NLSYSQKIilrrelIGYIFQSF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:NF038007   93 NLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 172 DSE-LRESLcgEMSRLLRQLGITAVYVTHDrREAELLADQIVYLSAGR 218
Cdd:NF038007  173 DSKnARAVL--QQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
15-214 1.77e-29

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 108.86  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  15 AFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEI-RFGDRLVA------RAGWGLPPEQRDIGMV 87
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAyvpqrsEVPDSLPLTVRDLVAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 fqdyALWPHMSvaqnvafplRMRGVSRSEReRRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040873   81 ----GRWARRG---------LWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAeLLADQIVYL 214
Cdd:NF040873  147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-167 2.27e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 92.11  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF--GDRLVARAgwglppeqRDi 84
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDMADARH--------RR- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 gMVFQDYA---------LWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERkPSG-LSGGQQQRVALARA 154
Cdd:NF033858   73 -AVCPRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAGkLSGGMKQKLGLCCA 150

                         170
                  ....*....|...
gi 1405942281 155 IVAAPRVLLFDEP 167
Cdd:NF033858  151 LIHDPDLLILDEP 163
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-222 6.98e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.57  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  23 DRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARagwGLPPEQRdIGMVFQDYALWPHMSVAQ 101
Cdd:NF033858  283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGQPVDAG---DIATRRR-VGYMSQAFSLYGELTVRQ 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCG 181
Cdd:NF033858  359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1405942281 182 EMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAAV 222
Cdd:NF033858  439 LLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLAS 478
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-218 3.23e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 82.53  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGlsvpV------SGEIRFGDRLVA----RAGwglppEQRDIGMVFQDY 91
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG----VyphgsyEGEILFDGEVCRfkdiRDS-----EALGIVIIHQEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVaF---PLRMRGV-SRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040905   88 ALIPYLSIAENI-FlgnERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 168 ---LSNLDSE-----LREslcgemsrlLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:NF040905  167 taaLNEEDSAalldlLLE---------LKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
16-221 6.74e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 6.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLlRLLAGLSVPVSGE--IRFGDRLVARAGWglppeQRDIGMVFQ-DYA 92
Cdd:NF000106   23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpWRF*TWCANRRAL-----RRTIG*HRPvR*G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  93 LWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:NF000106   97 RRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1405942281 173 SELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:NF000106  177 PRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 31-218 3.29e-09

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: 53.92  E-value: 3.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   31 PGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDrlvaragwglppeqrdigmvfqdyalwphmsvaqnvafplrmr 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  111 gvsrSERERRVSEALARVGLNGfaeRKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL-----CGEMSR 185
Cdd:smart00382  38 ----GEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLL 110

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1405942281  186 LLRQLGITAVYVTH-----DRREAELLADQIVYLSAGR 218
Cdd:smart00382 111 LKSEKNLTVILTTNdekdlGPALLRRRFDRRIVLLLIL 148
GguA NF040905
sugar ABC transporter ATP-binding protein;
110-167 5.14e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.62  E-value: 5.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 110 RGVSRSERERRVSEALaRVGLNgfaERKPS------GLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040905  372 RGVIDENEEIKVAEEY-RKKMN---IKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 7-222 4.70e-120

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 345.54  E-value: 4.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 7-219 3.30e-115

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 333.19  E-value: 3.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT----DLPPKDRNIAM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG3839    80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG3839   160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 7-222 2.70e-106

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: 305.21  E-value: 2.70e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT----GVPPERRNIGM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03259    77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03259   157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 7-219 2.93e-96

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: 280.66  E-value: 2.93e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVNT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03300    77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03300   157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 7-222 7.75e-96

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 283.58  E-value: 7.75e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwgLPPEQRDIGM 86
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN---LPPRERRVGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG1118    80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG1118   160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 7-222 1.50e-94

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: 275.67  E-value: 1.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGM 86
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT----DLPPKDRDIAM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03301    77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03301   157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 7-225 1.10e-93

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 275.04  E-value: 1.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA----ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglppeqR 82
Cdd:COG1116     8 LELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-------P 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:COG1116    81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 163 LFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSA--GRVAAVRAV 225
Cdd:COG1116   161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDV 225
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-220 8.70e-90

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 269.12  E-value: 8.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTP-ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPP 79
Cdd:PRK09452    8 PSSLSPlVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQRDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK09452   84 ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK09452  164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 7-222 5.39e-88

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: 259.33  E-value: 5.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglppeqR 82
Cdd:cd03293     1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------P 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:cd03293    74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 163 LFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSA--GRVAAV 222
Cdd:cd03293   154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
7-219 1.58e-81

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 247.45  E-value: 1.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIG 85
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----LEPADRDIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:PRK11650   80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 166 EPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11650  160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
9-219 2.11e-81

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 246.94  E-value: 2.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrF--GDRLVARAgwglpPEQRDIGM 86
Cdd:PRK11432    9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FidGEDVTHRS-----IQQRDICM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:PRK11432   83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11432  163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
4-222 4.63e-79

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 241.86  E-value: 4.63e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   4 LTPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRD 83
Cdd:PRK11000    1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:PRK11000   77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 164 FDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:PRK11000  157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 7-219 5.17e-79

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 241.09  E-value: 5.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 37-222 1.22e-78

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: 239.32  E-value: 1.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  37 LLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSE 116
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 117 RERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVY 196
Cdd:TIGR01187  77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156

                         170       180
                  ....*....|....*....|....*.
gi 1405942281 197 VTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQI 182
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-224 2.24e-78

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 234.94  E-value: 2.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLtpITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwg 76
Cdd:COG1136     1 MSPL--LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  77 LPPEQRD------IGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVA 150
Cdd:COG1136    75 LSERELArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAAVRA 224
Cdd:COG1136   155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDER 227
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 7-219 3.44e-76

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: 229.30  E-value: 3.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQR 82
Cdd:cd03255     1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK----LSEKEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 D------IGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:cd03255    77 AafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:cd03255   157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 7-222 4.53e-75

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: 227.17  E-value: 4.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVaragWGLPPEQRD--- 83
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----TGLSEKELYelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 --IGMVFQDYALWPHMSVAQNVAFPLRMRG-VSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:COG1127    82 rrIGMLFQGGALFDSLTVFENVAFPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG1127   162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 7-222 9.63e-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: 226.45  E-value: 9.63e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD----VPVQERNVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSR----SERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:cd03296    79 VFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 163 LFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03296   159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
7-233 5.15e-74

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 228.34  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAG-WGLPPEQ 81
Cdd:NF040933    3 VRVENVTKIFkkgkKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGkIIVPPED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:NF040933   83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT-----PTSGEVA 233
Cdd:NF040933  163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEeiydnPANIFVA 239
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 7-218 2.13e-72

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: 218.21  E-value: 2.13e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGM 86
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPlrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 7-221 5.05e-72

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: 219.13  E-value: 5.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwgLPPEQRDIG 85
Cdd:COG1122     1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDyalwP-----HMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:COG1122    79 LVFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 161 VLLFDEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1122   155 VLVLDEPTAGLDPRGRR----ELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 22-221 7.45e-72

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: 217.93  E-value: 7.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHID---PGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV--ARAGWGLPPEQRDIGMVFQDYALWPH 96
Cdd:cd03297    10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQQRKIGLVFQQYALFPH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFPLRmrGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELR 176
Cdd:cd03297    90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1405942281 177 ESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03297   168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 7-219 1.01e-71

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 218.71  E-value: 1.01e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGM 86
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAF-PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 166 EPLSNLDSELReslcGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG1126   162 EPTSALDPELV----GEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 7-220 1.10e-71

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 220.73  E-value: 1.10e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQ--RD 83
Cdd:COG1125     2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR----DLDPVElrRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLN--GFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:COG1125    78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:COG1125   158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-224 5.12e-70

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 213.76  E-value: 5.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARA-GWGLPPEQRDI 84
Cdd:COG2884     2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkRREIPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 165 DEPLSNLDSELRESLcgeMsRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAAVRA 224
Cdd:COG2884   162 DEPTGNLDPETSWEI---M-ELLEEInrrGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 21-233 5.35e-70

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: 214.12  E-value: 5.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGMVFQDYALWPHMSVA 100
Cdd:cd03299    14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT----NLPPEKRDISYVPQNYALFPHMTVY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLC 180
Cdd:cd03299    90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 181 GEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV---RAV--TPTSGEVA 233
Cdd:cd03299   170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVgkpEEVfkKPKNEFVA 227
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
7-221 1.07e-69

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 213.08  E-value: 1.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVldRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA----LPPAERPVSM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLR--MRgVSRSERERrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:COG3840    76 LFQENNLFPHLTVAQNIGLGLRpgLK-LTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 165 DEPLSNLDSELREslcgEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG3840   154 DEPFSALDPALRQ----EMLDLVDELcrerGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 7-222 1.69e-69

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 212.74  E-value: 1.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATR----VHARDRKIGF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR00968  77 VFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQI 212
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
7-222 2.31e-67

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 207.22  E-value: 2.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLppeQRDIGM 86
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---RRRIGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG1131    78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 167 PLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG1131   158 PTSGLDPEARR----ELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-233 4.02e-67

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 210.32  E-value: 4.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGMVFQDYALWPHMSVAQ 101
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN----LPPEKRGIAYVYQNYMLFPHKTVFE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCG 181
Cdd:NF040840   92 NIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 182 EMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT-----PTSGEVA 233
Cdd:NF040840  172 EMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVRevfrrPKNEFVA 228
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 9-218 6.66e-67

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: 205.39  E-value: 6.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAraGWGLPPEQRDIGM 86
Cdd:cd03225     2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDyalwP-HM----SVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:cd03225    80 VFQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 162 LLFDEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:cd03225   156 LLLDEPTAGLDPAGRR----ELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 7-221 3.99e-66

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: 204.27  E-value: 3.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAGWGLPPEQRDIG 85
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLiDGEDISGLSEAELYRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAFPLRMRGV-SRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 165 DEPLSNLD---SELRESLcgeMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03261   161 DEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 7-219 1.04e-65

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: 202.37  E-value: 1.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGM 86
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAF-PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 166 EPLSNLDSELReslcGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03262   161 EPTSALDPELV----GEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 7-222 1.68e-65

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: 202.92  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--RD 83
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE----QDPVElrRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGL--NGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:cd03295    77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03295   157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 22-221 2.13e-65

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: 206.49  E-value: 2.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHID----PGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV--ARAGWGLPPEQRDIGMVFQDYALWP 95
Cdd:COG4148    11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRRIGYVFQEARLFP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNVAFPlrMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSEL 175
Cdd:COG4148    91 HLSVRGNLLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1405942281 176 RESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG4148   169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 8-216 6.40e-65

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 200.40  E-value: 6.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   8 TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP---VSGEIRFGDRLVARagwgLPPEQRDI 84
Cdd:COG4136     3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA----LPAEQRRI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRmRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:COG4136    79 GILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 165 DEPLSNLDSELRE---SLCGEMsrlLRQLGITAVYVTHDRREAElLADQIVYLSA 216
Cdd:COG4136   158 DEPFSKLDAALRAqfrEFVFEQ---IRQRGIPALLVTHDEEDAP-AAGRVLDLGN 208
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 7-225 1.57e-63

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: 198.10  E-value: 1.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGlpPEQR 82
Cdd:COG1124     2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--AFRR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDY--ALWPHMSVAQNVAFPLRMRGvsRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:COG1124    80 RVQMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAV 225
Cdd:COG1124   158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
2-218 2.47e-63

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 201.60  E-value: 2.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   2 RTLTPI-TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPE 80
Cdd:PRK11607   14 KALTPLlEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 QRDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:PRK11607   90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK11607  170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-222 7.61e-63

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 196.62  E-value: 7.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTpitLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwg 76
Cdd:COG4525     1 MSMLT---VRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  77 lppeqRDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:COG4525    76 -----ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSA--GRVAAV 222
Cdd:COG4525   151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 7-219 1.03e-62

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: 195.49  E-value: 1.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET----PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAGWGLPPEQ 81
Cdd:cd03258     2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvDGTDLTLLSGKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
7-232 1.11e-62

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 199.15  E-value: 1.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHARDRKVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMrgVSRSER------ERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:PRK10851   79 VFQHYALFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 161 VLLFDEPLSNLDSELREslcgEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAG------------RVAAVRA 224
Cdd:PRK10851  157 ILLLDEPFGALDAQVRK----ELRRWLRQLheelKFTSVFVTHDQEEAMEVADRVVVMSQGnieqagtpdqvwREPATRF 232


                  ....*...
gi 1405942281 225 VTPTSGEV 232
Cdd:PRK10851  233 VLEFMGEV 240
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
7-219 7.26e-62

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 196.84  E-value: 7.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR-LVARAGWGLPPEQ 81
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdLTALSERELRAAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHD----RReaelLADQIVYLSAGRV 219
Cdd:COG1135   162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvvRR----ICDRVAVLENGRI 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 7-219 2.57e-61

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: 200.13  E-value: 2.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-----ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWG-LPPE 80
Cdd:COG1123   261 LEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRsLREL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 QRDIGMVFQD--YALWPHMSVAQNVAFPLRMRGV-SRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIV 156
Cdd:COG1123   341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 26-219 2.61e-61

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: 193.24  E-value: 2.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQR--DIGMVFQDYALWPHMSVAQNV 103
Cdd:cd03294    44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrkKISMVFQSFALLPHRTVLENV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 104 AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEM 183
Cdd:cd03294   124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 184 SRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03294   204 LRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
7-219 4.91e-61

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 191.38  E-value: 4.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-------FGDRLVARAGWGLpp 79
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPSEKAIRLL-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 eQRDIGMVFQDYALWPHMSVAQN-VAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:COG4161    81 -RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4161   160 PQVLLFDEPTAALDPEITAQVV-EIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
7-219 5.52e-61

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 190.03  E-value: 5.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQ--RDI 84
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS----AMPPPEwrRQV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPhMSVAQNVAFPLRMRGvsRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:COG4619    77 AYVPQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 164 FDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4619   154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 7-222 2.34e-60

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: 189.68  E-value: 2.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPE-QRDIG 85
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREaRRQIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:COG4555    78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 166 EPLSNLDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:COG4555   158 EPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 7-219 5.29e-60

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 188.68  E-value: 5.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-------FGDRLVARAGWGLpp 79
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIREL-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 eQRDIGMVFQDYALWPHMSVAQN-VAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:PRK11124   81 -RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11124  160 PQVLLFDEPTAALDPEITAQIV-SIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
7-220 1.25e-59

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 187.99  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGM 86
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAF-PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 166 EPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK09493  162 EPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 7-222 5.06e-59

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: 185.85  E-value: 5.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL-----SVPVSGEIRFGDRLVAraGWGLPPEQ 81
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIY--DLDVDVLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 --RDIGMVFQDYALWPhMSVAQNVAFPLRMRGV-SRSERERRVSEALARVGLNGFAERK--PSGLSGGQQQRVALARAIV 156
Cdd:cd03260    79 lrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 157 AAPRVLLFDEPLSNLDSELREslcgEMSRLLRQLG--ITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03260   158 NEPEVLLLDEPTSALDPISTA----KIEELIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 7-219 1.51e-57

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 182.56  E-value: 1.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWG-LPPEQRDI 84
Cdd:COG3638     3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRaLRRLRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNV--------AFPLRMRG-VSRSERERrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAI 155
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGlFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 156 VAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG3638   162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 7-218 3.55e-57

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 180.52  E-value: 3.55e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAR-AGWGLPPEQRDI 84
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 165 DEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 20-219 2.00e-55

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: 176.54  E-value: 2.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQR-DIGMVFQDY--ALWPH 96
Cdd:cd03257    19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkEIQMVFQDPmsSLNPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFPLRMRGVSR--SERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:cd03257    99 MTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDV 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1405942281 174 ELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03257   179 SVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 7-221 2.25e-55

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: 177.16  E-value: 2.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--RDI 84
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS----LSRRElaRRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVA---FP-LRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:COG1120    78 AYVPQEPPAPFGLTVRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1120   158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 7-221 2.99e-55

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: 177.62  E-value: 2.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FG-DRLVARAGWGLppeQR 82
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvDGlDTLDEENLWEI---RK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVA 157
Cdd:TIGR04520  78 KVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAeLLADQIVYLSAGRVAA 221
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVA 216
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-220 2.60e-54

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 174.51  E-value: 2.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglppe 80
Cdd:COG1121     1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 qRDIGMVFQDYALwphmsvaqNVAFPLR---------------MRGVSRSERERrVSEALARVGLNGFAERKPSGLSGGQ 145
Cdd:COG1121    75 -RRIGYVPQRAEV--------DWDFPITvrdvvlmgrygrrglFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQ 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 146 QQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:COG1121   145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 7-221 8.00e-54

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: 171.91  E-value: 8.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVldRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglPPEQRDIGM 86
Cdd:cd03298     1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA----PPADRPVSM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03298    75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03298   155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-221 2.69e-53

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: 178.94  E-value: 2.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL---SVPVSGEIRFGDRLVARAGWGL 77
Cdd:COG1123     1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  78 PpeQRDIGMVFQD--YALWPhMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAI 155
Cdd:COG1123    81 R--GRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 156 VAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1123   158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 22-169 2.15e-52

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: 166.28  E-value: 2.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWGLPPEQRDIGMVFQDYALWPHMSVAQ 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD--DERKSLRKEIGYVFQDPQLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERK----PSGLSGGQQQRVALARAIVAAPRVLLFDEPLS 169
Cdd:pfam00005  79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 7-218 2.46e-52

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: 168.04  E-value: 2.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglPPEQRDIGM 86
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERerRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:COG4133    80 LGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGItAVYVTHDrrEAELLADQIVYLSAGR 218
Cdd:COG4133   158 PFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ--PLELAAARVLDLGDFK 206
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 21-227 4.98e-52

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: 168.00  E-value: 4.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLV-----ARAGWglppEQRDIGMVFQDYALW 94
Cdd:COG4181    27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlAGQDLFaldedARARL----RARHVGFVFQSFQLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRGvsRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:COG4181   103 PTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAAVRAVTP 227
Cdd:COG4181   181 TGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 19-220 1.80e-51

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: 166.97  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  19 TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD-RLVARAGWGLPPEQRDIGMVFQDYALWPHM 97
Cdd:cd03256    14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtDINKLKGKALRQLRRQIGMIFQQFNLIERL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  98 SVAQNVAFPL--RM-------RGVSRSERERrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:cd03256    94 SVLENVLSGRlgRRstwrslfGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 169 SNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:cd03256   173 ASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-219 4.60e-51

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: 165.27  E-value: 4.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAR-AGWGLPPEQRDI 84
Cdd:cd03292     1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 165 DEPLSNLDSElresLCGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03292   161 DEPTGNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
7-217 7.57e-51

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 166.03  E-value: 7.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwglPPEQRdiGM 86
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAER--GV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:PRK11248   75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAG 217
Cdd:PRK11248  155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 25-221 1.19e-50

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: 168.37  E-value: 1.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHID---PGR-IVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV--ARAGWGLPPEQRDIGMVFQDYALWPHMS 98
Cdd:TIGR02142  12 FSLDADftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIFLPPEKRRIGYVFQEARLFPHLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAFPL-RMRGVSRSERERRVSEALarvGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRE 177
Cdd:TIGR02142  92 VRGNLRYGMkRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1405942281 178 SLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 5-219 2.13e-50

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 164.85  E-value: 2.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   5 TPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglppeQRDI 84
Cdd:PRK11247   11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-------REDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAfpLRMRGVSRSERErrvsEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK11247   84 RLMFQDARLLPWKKVIDNVG--LGLKGQWRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 165 DEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11247  158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 7-220 2.64e-50

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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 164.93  E-value: 2.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-----ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR-LVARAGWGLPPE 80
Cdd:TIGR04521   1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRdITAKKKKKLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 QRDIGMVFQ--DYALWpHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVA 157
Cdd:TIGR04521  81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
16-219 4.20e-50

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 164.20  E-value: 4.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD---RLVARAGWGLPPEQRD--------I 84
Cdd:COG4598    18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeiRLKPDRDGELVPADRRqlqrirtrL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAF-PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:COG4598    98 GMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 164 FDEPLSNLDSElresLCGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4598   178 FDEPTSALDPE----LVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 7-219 6.91e-50

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 166.13  E-value: 6.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA----ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR-LVARAGWGLPPEQ 81
Cdd:PRK11153    2 IELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdLTALSEKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:PRK11153   82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 162 LLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHD----RReaelLADQIVYLSAGRV 219
Cdd:PRK11153  162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmdvvKR----ICDRVAVIDAGRL 219
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 22-222 1.21e-49

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: 161.86  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglpPEQRdigMVFQDYALWPHMSVAQ 101
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRM---VVFQNYSLLPWLTVRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAFPLR--MRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL 179
Cdd:TIGR01184  74 NIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1405942281 180 CGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANI 196
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 7-222 3.95e-49

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 160.03  E-value: 3.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVldRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQRDIGM 86
Cdd:TIGR01277   1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG----LAPYQRPVSM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR01277  75 LFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
7-221 1.56e-48

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 160.57  E-value: 1.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAG-WGLppeQRD 83
Cdd:PRK13635    6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvWDV---RRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:PRK13635   83 VGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAeLLADQIVYLSAGRVAA 221
Cdd:PRK13635  159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 14-221 2.51e-48

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: 158.05  E-value: 2.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  14 FAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwGLPPEQRDIGMVFQDYAL 93
Cdd:cd03263    10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAARQSLGYCPQFDAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 WPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:cd03263    87 FDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 174 ELRESLCGEMSRLLRQLGItaVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03263   167 ASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRC 212
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 8-221 3.41e-48

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: 156.44  E-value: 3.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   8 TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwglppeqrdigmv 87
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 fqdyalWPHMSVAQNVAFplrmrgvsrsererrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:cd03214    66 ------LSPKELARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03214   125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 7-219 3.93e-48

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: 158.84  E-value: 3.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLV---ARAGWGLPPEQR 82
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYhmpGRNGPLVPADEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 -------DIGMVFQDYALWPHMSVAQNVAF-PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARA 154
Cdd:TIGR03005  81 hlrqmrnKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRI 225
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 9-214 5.58e-48

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 157.01  E-value: 5.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPE-QRD-IGM 86
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfRREkLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 167 PLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAElLADQIVYL 214
Cdd:TIGR03608 161 PTGSLDPKNRD----EVLDLLLELndeGKTIIIVTHDPEVAK-QADRVIEL 206
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-221 5.73e-48

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: 167.70  E-value: 5.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--R 82
Cdd:COG2274   474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ----IDPASlrR 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVAFplrmrGVSRSERErRVSEALARVGLNGFAERKP-----------SGLSGGQQQRVAL 151
Cdd:COG2274   550 QIGVVLQDVFLF-SGTIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRVAA 221
Cdd:COG2274   623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAH-RLSTIRLADRIIVLDKGRIVE 689
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 7-219 2.56e-47

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 156.74  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLS--VP---VSGEIRFGDRLVARAGWGLPPEQ 81
Cdd:COG1117    12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDIYDPDVDVVELR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPhMSVAQNVAFPLRMRGV-SRSERERRVSEALARVGLngFAERK------PSGLSGGQQQRVALARA 154
Cdd:COG1117    92 RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL--WDEVKdrlkksALGLSGGQQQRLCIARA 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 155 IVAAPRVLLFDEPLSNLDS-------ELRESLCGEMsrllrqlgiTAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG1117   169 LAVEPEVLLMDEPTSALDPistakieELILELKKDY---------TIVIVTHNMQQAARVSDYTAFFYLGEL 231
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
21-228 3.62e-47

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 156.77  E-value: 3.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA---RAGWGlpPEQRDIGMVFQDY--ALWP 95
Cdd:PRK10419   27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnRAQRK--AFRRDIQMVFQDSisAVNP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNVAFPLR-MRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:PRK10419  105 RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 174 ELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPT 228
Cdd:PRK10419  185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 7-219 4.35e-47

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: 153.32  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARagwglPPE-QRDI 84
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIKKE-----PEEvKRRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAfplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:cd03230    76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 165 DEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03230   120 DEPTSGLDPESRR----EFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
18-218 4.45e-47

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 154.88  E-value: 4.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRD------IGMVFQDY 91
Cdd:NF038007   17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT----NLSYSQKIilrrelIGYIFQSF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:NF038007   93 NLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 172 DSE-LRESLcgEMSRLLRQLGITAVYVTHDrREAELLADQIVYLSAGR 218
Cdd:NF038007  173 DSKnARAVL--QQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 7-218 1.01e-46

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: 152.54  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPE--QR 82
Cdd:cd03228     1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR----DLDLEslRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVafplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVL 162
Cdd:cd03228    77 NIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 163 LFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGR 218
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAH-RLSTIRDADRIIVLDDGR 171
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 21-220 3.58e-46

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 152.87  E-value: 3.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAGWGLPPEQRDIGMVFQDYALWPHMSV 99
Cdd:TIGR02982  20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvLGQELHGASKKQLVQLRRRIGYIFQAHNLLGFLTA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVAFPLRM-RGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRES 178
Cdd:TIGR02982 100 RQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1405942281 179 LCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVA 220
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHDNRILD-VADRILQMEDGKLL 220
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 8-218 4.12e-46

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: 150.47  E-value: 4.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   8 TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWGLPPEQRDIGMV 87
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 FQdyalwphmsvaqnvafplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:cd00267    79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:cd00267   108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 7-220 4.71e-46

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: 151.96  E-value: 4.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGrIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLppeQRDIGM 86
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIGY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03264    77 LPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLcgemSRLLRQLGITAVYV--THDRREAELLADQIVYLSAGRVA 220
Cdd:cd03264   157 PTAGLDPEERIRF----RNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV 208
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 9-221 5.32e-46

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: 152.59  E-value: 5.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQR---DIG 85
Cdd:cd03219     3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT----GLPPHEIarlGIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVA--------FPLRMRGVSRSERE--RRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAI 155
Cdd:cd03219    79 RTFQIPRLFPELTVLENVMvaaqartgSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 156 VAAPRVLLFDEPLSNLDSELRESLcGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03219   159 ATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 4-219 8.01e-46

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 152.98  E-value: 8.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   4 LTPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDrLVARAGWGLPPEQRD 83
Cdd:PRK11264    1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD-ITIDTARSLSQQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 I-------GMVFQDYALWPHMSVAQNV-AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAI 155
Cdd:PRK11264   80 IrqlrqhvGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 156 VAAPRVLLFDEPLSNLDSElresLCGEMSRLLRQLG---ITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11264  160 AMRPEVILFDEPTSALDPE----LVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFMDQGRI 222
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 21-219 1.11e-45

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: 152.07  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARA-GWGLPPEQRDIGMVFQDYALWPHMSV 99
Cdd:TIGR02315  17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrGKKLRKLRRRIGMIFQHYNLIERLTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNV---------AFPLRMRGVSRSERERRVSeALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:TIGR02315  97 LENVlhgrlgykpTWRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIAS 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1405942281 171 LDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR02315 176 LDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 18-205 3.94e-45

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 150.19  E-value: 3.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDI--GMVFQDYALWP 95
Cdd:TIGR02211  17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKklGFIYQFHHLLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSEL 175
Cdd:TIGR02211  97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 1405942281 176 RESLCGEMSRLLRQLGITAVYVTHDRREAE 205
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAK 206
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
7-221 4.41e-45

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 158.40  E-value: 4.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--RD 83
Cdd:COG1132   340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD----LTLESlrRQ 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWpHMSVAQNVAFPLrmRGVSRSErerrVSEALARVGLNGFAERKPSG-----------LSGGQQQRVALA 152
Cdd:COG1132   416 IGVVPQDTFLF-SGTIRENIRYGR--PDATDEE----VEEAAKAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIA 488

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 153 RAIVAAPRVLLFDEPLSNLDSE----LRESLcgemSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRVAA 221
Cdd:COG1132   489 RALLKDPPILILDEATSALDTEtealIQEAL----ERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVE 554
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 9-221 7.11e-45

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: 150.57  E-value: 7.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQR-DIGMV 87
Cdd:COG0411     7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT----GLPPHRIaRLGIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 --FQDYALWPHMSVAQNV-------------AFPLRMRGVSRSERE--RRVSEALARVGLNGFAERKPSGLSGGQQQRVA 150
Cdd:COG0411    83 rtFQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQQRRLE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG0411   163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 20-226 1.07e-44

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 150.34  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLPPEQRDIGMVFQDY--ALWPH 96
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDRKQRRAFRRDVQLVFQDSpsAVNPR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFPLR-MRGVSRSERERRVSEALARVGLNG-FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT 226
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 9-220 1.26e-44

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: 148.45  E-value: 1.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGdrlvaragwGLPPEQ--RDIGM 86
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF---------GKPLEKerKRIGY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQ-DYALW--PhMSVAQNVAFPLR-----MRGVSRSEReRRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:cd03235    73 VPQrRSIDRdfP-ISVRDVVLMGLYghkglFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:cd03235   151 PDLLLLDEPFAGVDPKTQEDIY-ELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
7-220 1.82e-44

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 148.58  E-value: 1.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVldRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglPPEQRDIGM 86
Cdd:PRK10771    2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT----PPSRRPVSM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRmRGVSRSERERRVSEALA-RVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:PRK10771   76 LFQENNLFSHLTVAQNIGLGLN-PGLKLNAAQREKLHAIArQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 166 EPLSNLDSELREslcgEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK10771  155 EPFSALDPALRQ----EMLTLVSQVcqerQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 22-200 2.07e-44

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 151.42  E-value: 2.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLPPEQRDIGMVFQD-YA-LWPHMS 98
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdGQDITGLSGRELRPLRRRMQMVFQDpYAsLNPRMT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAFPLRMRGV-SRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELR 176
Cdd:COG4608   114 VGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193

                         170       180
                  ....*....|....*....|....
gi 1405942281 177 ESLCGEMSRLLRQLGITAVYVTHD 200
Cdd:COG4608   194 AQVLNLLEDLQDELGLTYLFISHD 217
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 12-219 2.26e-44

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: 150.97  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFAFAETPV--LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL---SVPVSGEIRFGDRLVARagwgLPPEQ----- 81
Cdd:COG0444     9 VYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLK----LSEKElrkir 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 -RDIGMVFQD-Y-ALWPHMSVAQNVAFPLRM-RGVSRSERERRVSEALARVGLNG---FAERKPSGLSGGQQQRVALARA 154
Cdd:COG0444    85 gREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG0444   165 LALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 7-219 2.10e-43

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 146.67  E-value: 2.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL-----SVPVSGEIRFGDRLVARAGWGLPPEQ 81
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDKKIDVVELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPhMSVAQNVAFPLRMRGV-SRSERERRVSEALARVGLngFAERK------PSGLSGGQQQRVALARA 154
Cdd:TIGR00972  82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAAL--WDEVKdrlhdsALGLSGGQQQRLCIARA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSElresLCGEMSRLLRQL--GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPI----ATGKIEELIQELkkKYTIVIVTHNMQQAARISDRTAFFYDGEL 221
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
7-221 2.56e-42

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 144.10  E-value: 2.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--RDI 84
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA----WSPWElaRRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV-------A 157
Cdd:COG4559    78 AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 158 APRVLLFDEPLSNLDseLRESLCgeMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG4559   158 GPRWLFLDEPTSALD--LAHQHA--VLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 7-221 7.07e-42

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: 149.14  E-value: 7.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPE--QRD 83
Cdd:COG4988   337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD----LDPAswRRQ 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDyALWPHMSVAQNvafpLRMRGVSRSERErrVSEALARVGLNGFAERKP-----------SGLSGGQQQRVALA 152
Cdd:COG4988   413 IAWVPQN-PYLFAGTIREN----LRLGRPDASDEE--LEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 153 RAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRVAA 221
Cdd:COG4988   486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITH-RLALLAQADRILVLDDGRIVE 551
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
7-229 7.10e-42

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 148.24  E-value: 7.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglpP---EQRD 83
Cdd:COG1129     5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS----PrdaQAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAF---PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:COG1129    81 IAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPTS 229
Cdd:COG1129   161 VLILDEPTASLTEREVERLFRII-RRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELT 228
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 7-222 8.45e-42

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: 141.26  E-value: 8.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglppeQRDIGM 86
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03269    75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03269   155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 21-222 8.75e-42

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: 141.35  E-value: 8.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglPPE-QRDIGMVFQDYALWPHMSV 99
Cdd:cd03266    20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE----PAEaRRRLGFVSDSTGLYDRLTA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL 179
Cdd:cd03266    96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1405942281 180 CgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03266   176 R-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
cbiO PRK13650
energy-coupling factor transporter ATPase;
7-219 1.04e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 142.95  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLppeQR 82
Cdd:PRK13650    5 IEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDI---RH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVA 157
Cdd:PRK13650   82 KIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:PRK13650  158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 22-219 2.00e-41

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: 147.52  E-value: 2.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVPVSGEIRF-GDRLVARAGWGLPPEQRDIGMVFQD-YA-LWPHMS 98
Cdd:COG4172   302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFdGQDLDGLSRRALRPLRRRMQVVFQDpFGsLSPRMT 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAFPLR--MRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDsel 175
Cdd:COG4172   381 VGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--- 457

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 176 reslcgeMS------RLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4172   458 -------VSvqaqilDLLRDLqrehGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
7-219 2.40e-41

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 140.40  E-value: 2.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAR-AGWGLPPEQRDI 84
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK10908   82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 165 DEPLSNLDSELRESLCGEMSRLLRqLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK10908  162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
34-221 3.64e-41

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 143.48  E-value: 3.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  34 IVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV--ARAGWGLPPEQRDIGMVFQDYALWPHMSVAQNvafpLR--M 109
Cdd:PRK11144   26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN----LRygM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 110 RGVSRSERERRVSealaRVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQ 189
Cdd:PRK11144  102 AKSMVAQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1405942281 190 LGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK11144  178 INIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 16-222 4.50e-41

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: 139.81  E-value: 4.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAGwglpPEQRDIGMVFQDYALW 94
Cdd:cd03265    10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvAGHDVVREPR----EVRRRIGIVFQDLSVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:cd03265    86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03265   166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 7-221 6.33e-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: 146.83  E-value: 6.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--R 82
Cdd:COG4987   334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD----LDEDDlrR 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNvafpLRM--RGVSrserERRVSEALARVGLNGFAERKPSGL-----------SGGQQQRV 149
Cdd:COG4987   410 RIAVVPQRPHLF-DTTLREN----LRLarPDAT----DEELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRL 480

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 150 ALARAIVAAPRVLLFDEPLSNLDSELRESLcgeMSRLLRQL-GITAVYVTHDRREAElLADQIVYLSAGRVAA 221
Cdd:COG4987   481 ALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLAGLE-RMDRILVLEDGRIVE 549
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
19-211 7.22e-40

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 136.87  E-value: 7.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  19 TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFG----DRLVARAGWGLppEQRDIGMVFQDYALW 94
Cdd:PRK11629   22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmSKLSSAAKAEL--RNQKLGFIYQFHHLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:PRK11629  100 PDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQI 211
Cdd:PRK11629  180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
16-219 2.75e-39

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 136.25  E-value: 2.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD---RLVARAGWGLPPEQRD--------I 84
Cdd:PRK10619   15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLKVADKNqlrllrtrL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNV-AFPLRMRGVSRSERERRVSEALARVGLNGFAERK-PSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:PRK10619   95 TMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVL 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 163 LFDEPLSNLDSElresLCGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK10619  175 LFDEPTSALDPE----LVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 7-219 8.35e-39

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: 133.50  E-value: 8.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLppeqRDIGM 86
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVsrseRERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03268    77 LIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 167 PLSNLD----SELRESLcgemsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03268   153 PTNGLDpdgiKELRELI-----LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 8-219 1.15e-38

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: 133.15  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   8 TLQEVSFAFAETP-VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglpPEQRDIGM 86
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-----ERRKSIGY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQD--YALWPHmSVAQNVAfpLRMRGVSrsERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:cd03226    76 VMQDvdYQLFTD-SVREELL--LGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 165 DEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03226   151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
7-221 3.12e-38

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 133.74  E-value: 3.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLPPEQRDIG 85
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAFPLRmrgvsrseRERRVSEALAR---------VGLNGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:PRK11831   88 MLFQSGALFTDMNVFDNVAYPLR--------EHTQLPAPLLHstvmmkleaVGLRGAAKLMPSELSGGMARRAALARAIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK11831  160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-221 4.31e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 134.08  E-value: 4.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV---ARAGWGLPPEQRd 83
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpeDRRRIGYLPEER- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 igmvfqdyALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:COG4152    81 --------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 164 FDEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG4152   153 LDEPFSGLDPVNVE----LLKDVIRELaakGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 7-221 6.39e-38

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 132.59  E-value: 6.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--RDI 84
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD----WSPAElaRRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMvfqdyalwphMSVAQNVAFPLRMRGV----------SRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARA 154
Cdd:PRK13548   79 AV----------LPQHSSLSFPFTVEEVvamgraphglSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IV------AAPRVLLFDEPLSNLDseLRESLcgEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13548  149 LAqlwepdGPPRWLLLDEPTSALD--LAHQH--HVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 7-219 2.08e-37

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: 128.87  E-value: 2.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET--PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGlppEQRD- 83
Cdd:cd03246     1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELGDh 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHmSVAQNVafplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLL 163
Cdd:cd03246    78 VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 164 FDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:cd03246   120 LDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 7-221 2.08e-37

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: 130.02  E-value: 2.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVaragWGLPPE--QR 82
Cdd:cd03245     3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI----RQLDPAdlRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVAfpLRMRGVSrserERRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:cd03245    79 NIGYVPQDVTLF-YGTLRDNIT--LGAPLAD----DERILRAAELAGVTDFVNKHPNGldlqigergrgLSGGQRQAVAL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdrREAEL-LADQIVYLSAGRVAA 221
Cdd:cd03245   152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH--RPSLLdLVDRIIVMDSGRIVA 218
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
5-221 2.84e-37

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 130.90  E-value: 2.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   5 TPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVaragWGLPPEQ--R 82
Cdd:PRK11231    1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI----SMLSSRQlaR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHMSVAQNVAF---P-LRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:PRK11231   77 RLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK11231  157 TPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 7-221 3.43e-37

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: 130.59  E-value: 3.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSG-EIR-FGDRlvaRAGWGLPPEQRDI 84
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGER---RGGEDVWELRKRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALW--PHMSVAQNV-----AFPLRMRGVSRSERERrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVA 157
Cdd:COG1119    81 GLVSPALQLRfpRDETVLDVVlsgffDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHdrREAELLA--DQIVYLSAGRVAA 221
Cdd:COG1119   160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH--HVEEIPPgiTHVLLLKDGRVVA 223
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 7-222 3.71e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 130.88  E-value: 3.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwgLPPEQRDI 84
Cdd:PRK13632    8 IKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN--LKEIRKKI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK13632   86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAeLLADQIVYLSAGRVAAV 222
Cdd:PRK13632  162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 7-221 4.01e-37

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 130.20  E-value: 4.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglPPEQ--RDI 84
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT----PSRElaKRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAF---PlRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:COG4604    78 AILRQENHINSRLTVRELVAFgrfP-YSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 162 LLFDEPLSNLDseLRESLcgEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG4604   157 VLLDEPLNNLD--MKHSV--QMMKLLRRLadelGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
cbiO PRK13637
energy-coupling factor transporter ATPase;
4-220 4.83e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 131.32  E-value: 4.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   4 LTPITLQEVSFafaETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRD 83
Cdd:PRK13637    8 LTHIYMEGTPF---EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQ--DYALWPHmSVAQNVAFPLRMRGVSRSERERRVSEALARVGL--NGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK13637   85 VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK13637  164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 7-221 9.18e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 130.53  E-value: 9.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPvLDRFSLH-----IDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA--RAGWGLP 78
Cdd:PRK13634    3 ITFQKVEHRYqYKTP-FERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagKKNKKLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  79 PEQRDIGMVFQ--DYALWPHmSVAQNVAF-PLRMrGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARA 154
Cdd:PRK13634   82 PLRKKVGIVFQfpEHQLFEE-TVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13634  160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
25-219 1.04e-36

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 129.57  E-value: 1.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLhiDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA------RAgwglppeqRDIGMVFQD--YALWPH 96
Cdd:COG4167    34 FTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygdykyRC--------KHIRMIFQDpnTSLNPR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFPLRMR-GVSRSERERRVSEALARVGLNG-FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:COG4167   104 LNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4167   184 VRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 7-222 1.20e-36

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: 126.39  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglPPEQRD--I 84
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRagI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQdyalwphmsvaqnvafplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:cd03216    78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 165 DEPLSNLDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:cd03216   107 DEPTAALTPAEVERLFKVI-RRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 19-219 1.46e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 129.43  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  19 TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGMVFQ---DYALWP 95
Cdd:PRK13639   15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQnpdDQLFAP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 hmSVAQNVAF-PLRMrGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:PRK13639   95 --TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 175 LRESLcgemSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13639  172 GASQI----MKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKI 215
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 5-219 2.47e-36

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 133.65  E-value: 2.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   5 TPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVaragwglppeqrdI 84
Cdd:COG0488   314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK-------------I 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYA-LWPHMSVAQNvafplrMRGVSRSERERRVSEALARVGLNGFAERKP-SGLSGGQQQRVALARAIVAAPRVL 162
Cdd:COG0488   381 GYFDQHQEeLDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVL 454

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 163 LFDEPLSNLDSELRESLcgEMsrLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG0488   455 LLDEPTNHLDIETLEAL--EE--ALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
21-221 3.48e-36

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 134.47  E-value: 3.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARA-GWGLPPEQRD-IGMVFQDYALWPHMS 98
Cdd:PRK10535   23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdADALAQLRREhFGFIFQRYHLLSHLT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRES 178
Cdd:PRK10535  103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1405942281 179 LcgeMSRL--LRQLGITAVYVTHDRREAElLADQIVYLSAGRVAA 221
Cdd:PRK10535  183 V---MAILhqLRDRGHTVIIVTHDPQVAA-QAERVIEIRDGEIVR 223
cbiO PRK13640
energy-coupling factor transporter ATPase;
7-221 3.90e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 128.76  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET--PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGE----IRFGDRLVARAGWglppE 80
Cdd:PRK13640    6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskiTVDGITLTAKTVW----D 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 QRD-IGMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARA 154
Cdd:PRK13640   82 IREkVGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAA 221
Cdd:PRK13640  158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLA 223
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 7-221 4.83e-36

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: 126.78  E-value: 4.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQR---D 83
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GLPPHERaraG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNvafpLRMRGVSRSERERRvsEALARVgLNGF---AERK--PSG-LSGGQQQRVALARAIVA 157
Cdd:cd03224    77 IGYVPEGRRIFPELTVEEN----LLLGAYARRRAKRK--ARLERV-YELFprlKERRkqLAGtLSGGEQQMLAIARALMS 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLcGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03224   150 RPKLLLLDEPSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
26-222 8.40e-36

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 130.54  E-value: 8.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQR--DIGMVFQDYALWPHMSVAQNV 103
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrkKIAMVFQSFALMPHMTVLDNT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 104 AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEM 183
Cdd:PRK10070  128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1405942281 184 SRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:PRK10070  208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 7-219 9.30e-36

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: 126.19  E-value: 9.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVarAGWGLPPEQRDI 84
Cdd:cd03251     1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWpHMSVAQNVAFplrmrGVSRSERErRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVALAR 153
Cdd:cd03251    79 GLVSQDVFLF-NDTVAENIAY-----GRPGATRE-EVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIAR 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:cd03251   152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKI 214
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 7-220 1.06e-35

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: 126.19  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD---RLVAragwgLPPEQR 82
Cdd:cd03253     1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVT-----LDSLRR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVAFplrmrG-VSRSERErrVSEALARVGLNGFAERKPSG-----------LSGGQQQRVA 150
Cdd:cd03253    76 AIGVVPQDTVLF-NDTIGYNIRY-----GrPDATDEE--VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVA 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHDRREAeLLADQIVYLSAGRVA 220
Cdd:cd03253   148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIV 214
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 7-221 1.15e-35

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 133.07  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFgDRLVARAgwgLPPE--QR 82
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLL-DGVDIRQ---IDPAdlRR 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVAfpLRMRGVSrserERRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIA--LGAPYAD----DEEILRAAELAGVTEFVRRHPDGldmqigergrsLSGGQRQAVAL 612

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdrREAEL-LADQIVYLSAGRVAA 221
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTH--RTSLLdLVDRIIVMDNGRIVA 679
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 7-221 1.15e-35

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: 132.18  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWglPPEQ--R 82
Cdd:COG4618   331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ--W--DREElgR 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHmSVAQNVAfplRMRGVSRsereRRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:COG4618   407 HIGYLPQDVELFDG-TIAENIA---RFGDADP----EKVVAAAKLAGVHEMILRLPDGydtrigeggarLSGGQRQRIGL 478

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLcGEMSRLLRQLGITAVYVTHdRREAELLADQIVYLSAGRVAA 221
Cdd:COG4618   479 ARALYGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKARGATVVVITH-RPSLLAAVDKLLVLRDGRVQA 546
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 7-221 1.35e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 127.16  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAG--WglppEQRD 83
Cdd:PRK13647    5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekW----VRSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDyalwPH-----MSVAQNVAF-PLRMrGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVA 157
Cdd:PRK13647   81 VGLVFQD----PDdqvfsSTVWDDVAFgPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13647  156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-216 2.54e-35

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 124.83  E-value: 2.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTPI-TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPP 79
Cdd:PRK10247    1 MQENSPLlQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST----LKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQ--RDIGMVFQDYALWPHmSVAQNVAFPLRMRGvsRSERERRVSEALARVGL-NGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:PRK10247   77 EIyrQQVSYCAQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQ 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSA 216
Cdd:PRK10247  154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEIN-HADKVITLQP 212
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 22-220 1.80e-34

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 125.46  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglPPEQ-----RDIGMVFQD-YA-LW 94
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA----DPEAqkllrQKIQIVFQNpYGsLN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMR-GVSRSERERRVSEALARVGLNG-FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PRK11308  107 PRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 173 SELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK11308  187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 6-214 1.97e-34

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: 128.56  E-value: 1.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA---RAGWglppeQ 81
Cdd:TIGR02857 321 SLEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdadADSW-----R 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDyalwPHM---SVAQNVAfpLRMRGVSRSErerrVSEALARVGLNGFAERKP-----------SGLSGGQQQ 147
Cdd:TIGR02857 396 DQIAWVPQH----PFLfagTIAENIR--LARPDASDAE----IREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQ 465

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 148 RVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHDRREAElLADQIVYL 214
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 7-219 2.68e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 123.71  E-value: 2.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA--ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwgLPPEQRDI 84
Cdd:PRK13648    8 IVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN--FEKLRKHI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDyalwPH-----MSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK13648   86 GIVFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAeLLADQIVYLSAGRV 219
Cdd:PRK13648  162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTV 220
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 12-219 7.43e-34

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: 127.11  E-value: 7.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFA--FAETPVLDRFSLHIDPGRIVALLGPSGCGKS----TLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQ---- 81
Cdd:COG4172    14 VAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL----GLSERElrri 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 --RDIGMVFQD--YALWPHMSVAQNVAFPLRM-RGVSRSERERRVSEALARVGLNGfAERK----PSGLSGGQQQRVALA 152
Cdd:COG4172    90 rgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRldayPHQLSGGQRQRVMIA 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 153 RAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHD----RReaelLADQIVYLSAGRV 219
Cdd:COG4172   169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRR----FADRVAVMRQGEI 235
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 18-221 7.85e-34

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: 121.24  E-value: 7.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQR---DIGMVFQDYALW 94
Cdd:COG0410    15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT----GLPPHRIarlGIGYVPEGRRIF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNvafpLRMRGVSRSEReRRVSEALARVgLNGF---AERK--PSG-LSGGQQQRVALARAIVAAPRVLLFDEPl 168
Cdd:COG0410    91 PSLTVEEN----LLLGAYARRDR-AEVRADLERV-YELFprlKERRrqRAGtLSGGEQQMLAIGRALMSRPKLLLLDEP- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 169 snldSE-LRESLCGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG0410   164 ----SLgLAPLIVEEIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVL 216
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 17-220 9.54e-34

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: 119.96  E-value: 9.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  17 AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL--SVPVSGEIRFGDRLVARAGWglppeQRDIGMVFQDYALW 94
Cdd:cd03213    20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF-----RKIIGYVPQDDILH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRgvsrsererrvsealarvglngfaerkpsGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSe 174
Cdd:cd03213    95 PTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1405942281 175 lreSLCGEMSRLLRQL---GITAVYVTHD-RREAELLADQIVYLSAGRVA 220
Cdd:cd03213   145 ---SSALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 22-229 2.04e-33

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 125.52  E-value: 2.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA--------RAGwglppeqrdIGMVFQDYAL 93
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdaiALG---------IGMVHQHFML 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 WPHMSVAQNVAF---PLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:COG3845    92 VPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 171 LDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPTS 229
Cdd:COG3845   172 LTPQEADELFEIL-RRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETS 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
7-219 2.95e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 121.00  E-value: 2.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDR----FSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWG--LPP 79
Cdd:PRK13649    3 INLQNVSYTYqAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQRDIGMVFQdyalWPHM-----SVAQNVAFPLRMRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALAR 153
Cdd:PRK13649   83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13649  159 ILAMEPKILVLDEPTAGLDPKGRKELM-TLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 16-221 3.08e-33

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: 119.57  E-value: 3.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQR---DIGMVFQDYA 92
Cdd:cd03218    10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK----LPMHKRarlGIGYLPQEAS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  93 LWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:cd03218    86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 173 ----SELReslcgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03218   166 piavQDIQ-----KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 21-204 3.41e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 119.50  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRfgdrLVARAGWGLPPEQR------DIGMVFQDYALW 94
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS----LVGQPLHQMDEEARaklrakHVGFVFQSFMLI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:PRK10584  101 PTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180

                         170       180       190
                  ....*....|....*....|....*....|
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREA 204
Cdd:PRK10584  181 TGDKIADLLFSLNREHGTTLILVTHDLQLA 210
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 7-219 5.09e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 120.72  E-value: 5.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIG 85
Cdd:PRK13636    6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQ--DYALWPhMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:PRK13636   86 MVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 164 FDEPLSNLD----SELRESLcgemSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13636  165 LDEPTAGLDpmgvSEIMKLL----VEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 20-221 6.50e-33

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 118.98  E-value: 6.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV--------ARAGWG-LPPEQRdigmVFQD 90
Cdd:COG1137    17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrARLGIGyLPQEAS----IFRK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  91 yalwphMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:COG1137    93 ------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 171 LD----SELReslcgEMSRLLRQLGItAVYVT-HDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1137   167 VDpiavADIQ-----KIIRHLKERGI-GVLITdHNVRETLGICDRAYIISEGKVLA 216
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 20-218 7.48e-33

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: 118.69  E-value: 7.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF--GDRLV--ARAgwglPPEQ------RDIGMVFQ 89
Cdd:COG4778    25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQA----SPREilalrrRTIGYVSQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  90 DYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLngfAER----KPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:COG4778   101 FLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL---PERlwdlPPATFSGGEQQRVNIARGFIADPPLLLLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 166 EPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:COG4778   178 EPTASLDAANRAVVV-ELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
5-219 5.95e-32

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 117.42  E-value: 5.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   5 TPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL----SVPVSgEIRFGDRLVARAGwglpPE 80
Cdd:PRK09984    3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREG----RL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 QRDI-------GMVFQDYALWPHMSVAQNV------AFPLR---MRGVSRSERERRVsEALARVGLNGFAERKPSGLSGG 144
Cdd:PRK09984   78 ARDIrksrantGYIFQQFNLVNRLSVLENVligalgSTPFWrtcFSWFTREQKQRAL-QALTRVGMVHFAHQRVSTLSGG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 145 QQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK09984  157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 6-221 8.33e-32

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 119.95  E-value: 8.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwGLPPEQRDIG 85
Cdd:PRK09536    3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL--SARAASRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAF---PLRMRGVSRSERERR-VSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:PRK09536   81 SVPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 162 LLFDEPLSNLDSElRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK09536  161 LLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 7-225 1.61e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 115.78  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL-----SVPVSGEIRFGDRLVARAGwgLPPEQ 81
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VIELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERE--RRVSEALARVGLngFAERK-----PSG-LSGGQQQRVALAR 153
Cdd:PRK14247   82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQL--WDEVKdrldaPAGkLSGGQQQRLCIAR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGItaVYVTHDRREAELLADQIVYLSAGRVAAVRAV 225
Cdd:PRK14247  160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
26-219 1.85e-31

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 116.04  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPpEQRdIGMVFQD--YALWPHMSVAQNV 103
Cdd:PRK15112   33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYR-SQR-IRMIFQDpsTSLNPRQRISQIL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 104 AFPLRMR-GVSRSERERRVSEALARVGL-NGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCG 181
Cdd:PRK15112  111 DFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1405942281 182 EMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK15112  191 LMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 7-199 2.12e-31

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: 113.99  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwGLPPEQRDIGM 86
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---QRDEPHENILY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFplrMRGVSRSEReRRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR01189  78 LGHLPGLKPELSALENLHF---WAAIHGGAQ-RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGItAVYVTH 199
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGI-VLLTTH 185
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 18-219 3.24e-31

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 115.18  E-value: 3.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQR--DIGMVFQDYAL-- 93
Cdd:COG1101    18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK----LPEYKRakYIGRVFQDPMMgt 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 WPHMSVAQNVA--------FPLRmRGVSRSERErRVSEALARVGLnGFAER--KPSG-LSGGQQQRVALARAIVAAPRVL 162
Cdd:COG1101    94 APSMTIEENLAlayrrgkrRGLR-RGLTKKRRE-LFRELLATLGL-GLENRldTKVGlLSGGQRQALSLLMATLTKPKLL 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 163 LFDEPLSNLD---SELRESLcgeMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG1101   171 LLDEHTAALDpktAALVLEL---TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 7-219 4.10e-31

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: 114.24  E-value: 4.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET-PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD---RLVARAGWglppeQR 82
Cdd:cd03254     3 IEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSL-----RS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHmSVAQNVAFplrmrgvSRSE-RERRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVA 150
Cdd:cd03254    78 MIGVVLQDTFLFSG-TIMENIRL-------GRPNaTDEEVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:cd03254   150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKI 215
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 9-219 7.77e-31

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 118.63  E-value: 7.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRfgdrlvaragwgLPPEQRdIGMVF 88
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLR-IGYLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  89 QDYALWPHMSVAQNV--AFPLRMRGVSRSER------------------------------ERRVSEALARVGLNGF-AE 135
Cdd:COG0488    68 QEPPLDDDLTVLDTVldGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEdLD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 136 RKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLcgEmsRLLRQLGITAVYVTHDRreaELL---ADQIV 212
Cdd:COG0488   148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWL--E--EFLKNYPGTVLVVSHDR---YFLdrvATRIL 220


                  ....*..
gi 1405942281 213 YLSAGRV 219
Cdd:COG0488   221 ELDRGKL 227
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 16-222 2.01e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 113.01  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL-----SVPVSGEIRFGDRLVARAGWGLPPEQRDIGMVFQD 90
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  91 YALWPHMSVAQNVAFPLRMRGVSRSERE--RRVSEALARVGL-NGFAER---KPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 165 DEPLSNLD---SELRESLCGEMSRLLrqlgiTAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:PRK14267  174 DEPTANIDpvgTAKIEELLFELKKEY-----TIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 18-199 2.90e-30

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 111.12  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRlvaRAGWGLPPEQ------RDigmvfqdy 91
Cdd:PRK13539   14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEAchylghRN-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVAFPLRMRGvsrsERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PRK13539   83 AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158

                         170       180
                  ....*....|....*....|....*...
gi 1405942281 172 DSELRESLCGEMSRLLRQLGItAVYVTH 199
Cdd:PRK13539  159 DAAAVALFAELIRAHLAQGGI-VIAATH 185
cbiO PRK13642
energy-coupling factor transporter ATPase;
22-228 3.06e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 113.26  E-value: 3.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLppeQRDIGMVFQDY-ALWPHMSV 99
Cdd:PRK13642   23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNL---RRKIGMVFQNPdNQFVGATV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL 179
Cdd:PRK13642  100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1405942281 180 CGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVaaVRAVTPT 228
Cdd:PRK13642  180 MRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEI--IKEAAPS 225
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 7-219 3.85e-30

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: 111.86  E-value: 3.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ-- 81
Cdd:cd03249     1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD----LNLRWlr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPhMSVAQNVAFPLrmRGVSRSERERRVSEALA-------------RVGLNGfaerkpSGLSGGQQQR 148
Cdd:cd03249    77 SQIGLVSQEPVLFD-GTIAENIRYGK--PDATDEEVEEAAKKANIhdfimslpdgydtLVGERG------SQLSGGQKQR 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 149 VALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:cd03249   148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQV 215
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 7-217 4.55e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 112.18  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLS-----VPVSGEIRFGDRLVARAGWGLPPEQ 81
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNIYSPRTDTVDLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPhMSVAQNVAFPLRMRGVSRSER-ERRVSEALarVGLNGFAERKPS------GLSGGQQQRVALARA 154
Cdd:PRK14239   86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSL--KGASIWDEVKDRlhdsalGLSGGQQQRVCIARV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IVAAPRVLLFDEPLSNLD----SELRESLCGemsrlLRQlGITAVYVTHDRREAELLADQIVYLSAG 217
Cdd:PRK14239  163 LATSPKIILLDEPTSALDpisaGKIEETLLG-----LKD-DYTMLLVTRSMQQASRISDRTGFFLDG 223
cbiO PRK13643
energy-coupling factor transporter ATPase;
16-219 7.63e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 112.52  E-value: 7.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDrFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWG--LPPEQRDIGMVFQ--DY 91
Cdd:PRK13643   17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeIKPVRKKVGVVFQfpES 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHmSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNG-FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:PRK13643   96 QLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 171 LDSELREslcgEMSRL---LRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13643  175 LDPKARI----EMMQLfesIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 7-218 8.02e-30

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: 108.30  E-value: 8.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLvaragwglppeqrDIGM 86
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------KIGY 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQdyalwphmsvaqnvafplrmrgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:cd03221    68 FEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 167 PLSNLDSELRESLcgemSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:cd03221    97 PTNHLDLESIEAL----EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 7-220 1.06e-29

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 116.21  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET--PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAraGWGLPPEQRDI 84
Cdd:TIGR03797 452 IEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA--GLDVQAVRRQL 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHmSVAQNVA--FPLRMRgvsrsererRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENIAggAPLTLD---------EAWEAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLI 599

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHdRREAELLADQIVYLSAGRVA 220
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIV----SESLERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVV 663
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
15-214 1.77e-29

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 108.86  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  15 AFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEI-RFGDRLVA------RAGWGLPPEQRDIGMV 87
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAyvpqrsEVPDSLPLTVRDLVAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 fqdyALWPHMSvaqnvafplRMRGVSRSEReRRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040873   81 ----GRWARRG---------LWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAeLLADQIVYL 214
Cdd:NF040873  147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
6-221 1.84e-29

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 111.82  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAgwglPPEQRDI 84
Cdd:PRK13537    7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRA----RHARQRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK13537   83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 165 DEPLSNLDSELREsLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13537  163 DEPTTGLDPQARH-LMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIA 218
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
14-221 2.54e-29

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 110.48  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  14 FAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGMVFQDyal 93
Cdd:PRK13638    9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 wP-----HMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK13638   86 -PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 169 SNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13638  165 AGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 21-219 3.07e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 110.14  E-value: 3.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL------SVPVSGEI-RFGDRLVARAGWGLppeQRDIGMVFQDYAL 93
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVlYFGKDIFQIDAIKL---RKEVGMVFQQPNP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 WPHMSVAQNVAFPLRMRGVS-RSERERRVSEALARVGL----NGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK14246  102 FPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 169 SNLD---SELRESLCGEMSRllrqlGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK14246  182 SMIDivnSQAIEKLITELKN-----EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
7-219 3.09e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 110.56  E-value: 3.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA------ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFG--DRLVARAGWGLp 78
Cdd:PRK13633    5 IKCKNVSYKYEsneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDI- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  79 peQRDIGMVFQ--DYALWPHMsVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:PRK13633   84 --RNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAeLLADQIVYLSAGRV 219
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 7-221 6.75e-29

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 113.60  E-value: 6.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFA--FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWGLPPEQRDI 84
Cdd:TIGR01842 317 LSVENVTIVppGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ--WDRETFGKHI 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHmSVAQNVAfplRMRGVSRSERerrVSEALARVGLNGFAERKPSG-----------LSGGQQQRVALAR 153
Cdd:TIGR01842 395 GYLPQDVELFPG-TVAENIA---RFGENADPEK---IIEAAKLAGVHELILRLPDGydtvigpggatLSGGQRQRIALAR 467

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHdRREAELLADQIVYLSAGRVAA 221
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITH-RPSLLGCVDKILVLQDGRIAR 533
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 7-220 1.68e-28

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: 107.57  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETP-VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFG--DRLVARAGWglppEQR 82
Cdd:cd03252     1 ITFEHVRFRYkPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPAW----LRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWpHMSVAQNVAfpLRMRGVSRsereRRVSEALARVGLNGFAERKP-----------SGLSGGQQQRVAL 151
Cdd:cd03252    77 QVGVVLQENVLF-NRSIRDNIA--LADPGMSM----ERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAI 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRVA 220
Cdd:cd03252   150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIV 215
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 23-200 2.95e-28

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 109.03  E-value: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  23 DRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVaragwGLPPEQR-----DIGMVFQD--YALW 94
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLL-----GMKDDEWravrsDIQMIFQDplASLN 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMR--GVSRSERERRVSEALARVGL-NGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PRK15079  113 PRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192

                         170       180
                  ....*....|....*....|....*....
gi 1405942281 172 DSELRESLCGEMSRLLRQLGITAVYVTHD 200
Cdd:PRK15079  193 DVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
7-219 6.36e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 107.00  E-value: 6.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrfgdrLVARAGWG----LPPEQ 81
Cdd:PRK13644    2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-----LVSGIDTGdfskLQGIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQD-YALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:PRK13644   77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:PRK13644  157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVMDRGKI 213
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
18-199 1.11e-27

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 104.50  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwglppeQRDigmVFQDYALW--- 94
Cdd:PRK13538   13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR--------QRD---EYHQDLLYlgh 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 -----PHMSVAQNVAFPLRMRGVSRSErerRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLS 169
Cdd:PRK13538   82 qpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1405942281 170 NLDSELRESLCGEMSRLLRQLGItAVYVTH 199
Cdd:PRK13538  159 AIDKQGVARLEALLAQHAEQGGM-VILTTH 187
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 18-225 2.10e-27

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 109.56  E-value: 2.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAGWGLPPEQRDIGMVFQD-YA-LW 94
Cdd:PRK10261  336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIDTLSPGKLQALRRDIQFIFQDpYAsLD 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAFPLRMRGVSRSER-ERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PRK10261  416 PRQTVGDSIMEPLRVHGLLPGKAaAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 173 SELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAV---RAV 225
Cdd:PRK10261  496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIgprRAV 551
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 26-216 2.18e-27

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 105.25  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGL-----SVPVSGEIRFGDRLVARAGWGLPPEQRDIGMVFQDYALWPHmSVA 100
Cdd:PRK14243   30 WLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPFPK-SIY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRG--------VSRSERER----RVSEALARVGLNgfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK14243  109 DNIAYGARINGykgdmdelVERSLRQAalwdEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEPC 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 169 SNLD--SELReslcgeMSRLLRQLG--ITAVYVTHDRREAELLADQIVYLSA 216
Cdd:PRK14243  180 SALDpiSTLR------IEELMHELKeqYTIIIVTHNMQQAARVSDMTAFFNV 225
cbiO PRK13645
energy-coupling factor transporter ATPase;
7-219 2.65e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 105.86  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TP----VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVArAGWGLPPE- 80
Cdd:PRK13645    7 IILDNVSYTYAKkTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP-ANLKKIKEv 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 ---QRDIGMVFQ--DYALWPHmSVAQNVAF-PLRMrGVSRSERERRVSEALARVGL-NGFAERKPSGLSGGQQQRVALAR 153
Cdd:PRK13645   86 krlRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13645  164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 35-221 2.96e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 105.27  E-value: 2.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  35 VALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwgLPPEQRDIGMVFQ---DYALWPhmSVAQNVAF-PLRMr 110
Cdd:PRK13652   33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKFVGLVFQnpdDQIFSP--TVEQDIAFgPINL- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 111 GVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQL 190
Cdd:PRK13652  108 GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1405942281 191 GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13652  188 GMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 19-225 4.25e-27

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.36  E-value: 4.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  19 TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF--GDRLVAragwgLPpeQRdigmvfqdyalwPH 96
Cdd:COG4178   376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLF-----LP--QR------------PY 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 M---SVAQNVAFPLRMRGVSRSErerrVSEALARVGLNGFAER------KPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:COG4178   437 LplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 168 LSNLDSELRESLcgeMSRLLRQL-GITAVYVTHdRREAELLADQIVYLSAGRVAAVRAV 225
Cdd:COG4178   513 TSALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGDGSWQLLPA 567
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
7-218 7.87e-27

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 105.30  E-value: 7.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAGWGlppeQRDIG 85
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPARARLA----RARIG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:PRK13536  118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 166 EPLSNLDSELREsLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK13536  198 EPTTGLDPHARH-LIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
5-221 3.46e-26

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 102.17  E-value: 3.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   5 TPITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAraGWGLPPEQRDI 84
Cdd:PRK10575   10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE--SWSSKAFARKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVA---FPLR-MRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:PRK10575   88 AYLPQQLPAAEGMTVRELVAigrYPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK10575  168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 1-209 4.17e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 102.04  E-value: 4.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTP-ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLS-----VPVSGEIRFGDRLVARAG 74
Cdd:PRK14258    1 MSKLIPaIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  75 WGLPPEQRDIGMVFQDYALWPhMSVAQNVAFPLRMRG-VSRSERERRVSEALARVGLNGFAERK----PSGLSGGQQQRV 149
Cdd:PRK14258   81 VNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 150 ALARAIVAAPRVLLFDEPLSNLD---SELRESLCGEMsRLLRQLgiTAVYVTHDRREAELLAD 209
Cdd:PRK14258  160 CIARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSL-RLRSEL--TMVIVSHNLHQVSRLSD 219
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 16-219 5.88e-26

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: 100.87  E-value: 5.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRlvaragwgLPPEQRD-----IGMVF-Q 89
Cdd:cd03267    31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--------VPWKRRKkflrrIGVVFgQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  90 DYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLS 169
Cdd:cd03267   103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1405942281 170 NLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03267   183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 8-221 6.02e-26

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 100.68  E-value: 6.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   8 TLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQR---DI 84
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK----LPPHERaraGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNvafpLRMRGVSRSERERRVSE---ALARVgLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:TIGR03410  78 AYVPQGREIFPRLTVEEN----LLTGLAALPRRSRKIPDeiyELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 162 LLFDEPlsnldSE-LRESLCGEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:TIGR03410 153 LLLDEP-----TEgIQPSIIKDIGRVIRRLraegGMAILLVEQYLDFARELADRYYVMERGRVVA 212
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 7-219 6.94e-26

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 105.03  E-value: 6.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARagwgL---PPeqR 82
Cdd:PRK11147    4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVAR----LqqdPP--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DI-GMVFqDY----------ALWPHMSVAQNVAFPLRMRGVSRSER-------------ERRVSEALARVGLNgfAERKP 138
Cdd:PRK11147   78 NVeGTVY-DFvaegieeqaeYLKRYHDISHLVETDPSEKNLNELAKlqeqldhhnlwqlENRINEVLAQLGLD--PDAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 139 SGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGemsrLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEG----FLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230


                  .
gi 1405942281 219 V 219
Cdd:PRK11147  231 L 231
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-219 8.09e-26

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: 105.48  E-value: 8.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwgLPPEQRDIGMVFQDYALWPHMSV 99
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFHHLTV 1020

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  100 AQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL 179
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1405942281  180 CGEMsrLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 18-227 2.01e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 101.47  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV----ARAGWGLPPEQRDI--------- 84
Cdd:PRK13631   38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkkNNHELITNPYSKKIknfkelrrr 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 -GMVFQ--DYALWPHmSVAQNVAF-PLRMrGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK13631  118 vSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQP 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELREslcgEMSRLL---RQLGITAVYVTHDRREAELLADQIVYLSAGRVaaVRAVTP 227
Cdd:PRK13631  196 EILIFDEPTAGLDPKGEH----EMMQLIldaKANNKTVFVITHTMEHVLEVADEVIVMDKGKI--LKTGTP 260
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 25-219 2.19e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 103.25  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHidPGRIVALLGPSGCGKST----LLRLLAGlsvpvSGEIRFGDR-LVARAGWGLPPEQRDIGMVFQD--YALWPHM 97
Cdd:PRK15134  307 FTLR--PGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQpLHNLNRRQLLPVRHRIQVVFQDpnSSLNPRL 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  98 SVAQNVAFPLRM--RGVSRSERERRVSEALARVGLNGFA-ERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE 174
Cdd:PRK15134  380 NVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1405942281 175 LRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK15134  460 VQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 7-218 3.73e-25

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: 97.93  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-----TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRL--VARAGWGLPp 79
Cdd:cd03250     1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQEPWIQN- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 eqrdigmvfqdyalwphMSVAQNVAFPLRMRgvsrSERERRVSEA--------------LARVGLNGFAerkpsgLSGGQ 145
Cdd:cd03250    80 -----------------GTIRENILFGKPFD----EERYEKVIKAcalepdleilpdgdLTEIGEKGIN------LSGGQ 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 146 QQRVALARAIVAAPRVLLFDEPLSNLDSE-----LRESLCGEMsrllrQLGITAVYVTHdrrEAELL--ADQIVYLSAGR 218
Cdd:cd03250   133 KQRISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILGLL-----LNNKTRILVTH---QLQLLphADQIVVLDNGR 204
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 16-221 4.92e-25

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 98.76  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSvPVSGEIRFGDRLVARagWGLPPEQRDIGMVFQDYALWP 95
Cdd:COG4138     6 VAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSD--WSAAELARHRAYLSQQQSPPF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNVAFPLRmRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV-------AAPRVLLFDEPL 168
Cdd:COG4138    83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 169 SNLDSELRESLcgemSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG4138   162 NSLDVAQQAAL----DRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 26-219 5.49e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 98.84  E-value: 5.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR-LVARAGWGLP-PEQR-----DIGMVFQDYA--LWPH 96
Cdd:PRK11701   26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdGQLRDLYALSeAERRrllrtEWGFVHQHPRdgLRMQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFPLRMRGVSRSERERRV-SEALARVGLNgfAER---KPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PRK11701  106 VSAGGNIGERLMAVGARHYGDIRATaGDWLERVEID--AARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405942281 173 SELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11701  184 VSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 22-220 5.74e-25

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 102.43  E-value: 5.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPvsGEIRFGDRLVAragwGLP---PEQRDI-GMVFQDYALWPHM 97
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLN----GMPidaKEMRAIsAYVQQDDLFIPTL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  98 SVAQNVAFP--LRM-RGVSRSERERRVSEALARVGLNGFA------ERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:TIGR00955 115 TVREHLMFQahLRMpRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 169 SNLDSelreSLCGEMSRLLRQL---GITAVYVTHdRREAEL--LADQIVYLSAGRVA 220
Cdd:TIGR00955 195 SGLDS----FMAYSVVQVLKGLaqkGKTIICTIH-QPSSELfeLFDKIILMAEGRVA 246
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 7-220 9.46e-25

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 102.13  E-value: 9.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE--TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARA--GWglppEQR 82
Cdd:TIGR01846 456 ITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdpAW----LRR 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDYALWPHmSVAQNVAfpLRMRGVSrserERRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:TIGR01846 532 QMGVVLQENVLFSR-SIRDNIA--LCNPGAP----FEHVIHAAKLAGAHDFISELPQGyntevgekganLSGGQRQRIAI 604

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRVA 220
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIA 670
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 21-199 9.60e-25

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: 96.79  E-value: 9.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglPPEQRDIGMVFQDYALWPHMSVA 100
Cdd:cd03231    15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLYLGHAPGIKTTLSVL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRsererrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLC 180
Cdd:cd03231    92 ENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165

                         170
                  ....*....|....*....
gi 1405942281 181 GEMSRLLRQLGItAVYVTH 199
Cdd:cd03231   166 EAMAGHCARGGM-VVLTTH 183
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 15-224 1.01e-24

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 101.54  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  15 AFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVPV---SGEIRF-GDRLVARagwGL-PPEQRDIGMVFQ 89
Cdd:PRK13549   14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQAS---NIrDTERAGIAIIHQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  90 DYALWPHMSVAQNV---AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:PRK13549   90 ELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 167 PLSNL-DSELRESLcgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRA 224
Cdd:PRK13549  170 PTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRP 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 7-200 1.12e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 99.00  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETP----VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF------GDRLVARAGW 75
Cdd:PRK13651    3 IKVKNIVKIFnKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  76 GL------PPE----------QRDIGMVFQ--DYALWpHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLN-GFAER 136
Cdd:PRK13651   83 VLeklviqKTRfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 137 KPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHD 200
Cdd:PRK13651  162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVK----EILEIFDNLnkqGKTIILVTHD 224
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-200 1.44e-24

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 97.49  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLtpITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLvaragwglppe 80
Cdd:PRK09544    1 MTSL--VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 qrDIGMVFQDYALWPHMSVAqnVAFPLRMR-GVSRSErerrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK09544   68 --RIGYVPQKLYLDTTLPLT--VNRFLRLRpGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHD 200
Cdd:PRK09544  140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 7-220 1.62e-24

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: 101.05  E-value: 1.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPE--QRD 83
Cdd:COG5265   358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR----DVTQAslRAA 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWpHMSVAQNVAF--PlrmrGVSRSErerrVSEALARVGLNGFAERKPSG-----------LSGGQQQRVA 150
Cdd:COG5265   434 IGIVPQDTVLF-NDTIAYNIAYgrP----DASEEE----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVA 504

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTH------DrreaellADQIVYLSAGRVA 220
Cdd:COG5265   505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIV 571
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 23-218 1.66e-24

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 97.37  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  23 DRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQ-RDIGMV--FQDYALWPHMSV 99
Cdd:PRK11300   22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE----GLPGHQiARMGVVrtFQHVRLFREMTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQN--VA---------FP--LRMRGVSRSERE--RRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK11300   98 IENllVAqhqqlktglFSglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 165 DEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK11300  178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
cbiO PRK13641
energy-coupling factor transporter ATPase;
7-219 2.04e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 97.98  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-ETPV----LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF-GDRLVARAG-WGLPP 79
Cdd:PRK13641    3 IKFENVDYIYSpGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGnKNLKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQRDIGMVFQ--DYALWPHmSVAQNVAFPLRMRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALARAIV 156
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 157 AAPRVLLFDEPLSNLDSELREslcgEMSRLL---RQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13641  162 YEPEILCLDEPAAGLDPEGRK----EMMQLFkdyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 21-221 3.22e-24

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: 96.06  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVaragWGLppeqrDIGMVFQdyalwPHMSVA 100
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----SLL-----GLGGGFN-----PELTGR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESlC 180
Cdd:cd03220   103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK-C 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1405942281 181 GEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:cd03220   182 QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 3-219 8.81e-24

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: 94.85  E-value: 8.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   3 TLTPITL------QEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGdrlvara 73
Cdd:cd03248     2 SLAPDHLkgivkfQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  74 gwGLPPEQ-------RDIGMVFQDYALWPHmSVAQNVAFplrmrGVSRSERERrVSEALARVGLNGFAERKPSG------ 140
Cdd:cd03248    75 --GKPISQyehkylhSKVSLVGQEPVLFAR-SLQDNIAY-----GLQSCSFEC-VKEAAQKAHAHSFISELASGydtevg 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 141 -----LSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSElreslcgemSRLLRQlgiTAVYVTHDRREAELL-------- 207
Cdd:cd03248   146 ekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAE---------SEQQVQ---QALYDWPERRTVLVIahrlstve 213

                         250
                  ....*....|...
gi 1405942281 208 -ADQIVYLSAGRV 219
Cdd:cd03248   214 rADQILVLDGGRI 226
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 6-200 1.13e-23

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: 98.59  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPpeQRDI 84
Cdd:TIGR02868 334 TLELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV--RRRV 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWpHMSVAQNVAfplrmrgVSRSE-RERRVSEALARVGLNGFAERKPSGL-----------SGGQQQRVALA 152
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLR-------LARPDaTDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALA 483

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942281 153 RAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHD 200
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 7-219 1.20e-23

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: 93.15  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE--TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLppeQRDI 84
Cdd:cd03247     1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDyalwPHM---SVAQNVAfplrmrgvsrsereRRvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRV 161
Cdd:cd03247    78 SVLNQR----PYLfdtTLRNNLG--------------RR--------------------FSGGERQRLALARILLQDAPI 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 162 LLFDEPLSNLDSELRESLcgeMSRLLRQL-GITAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:cd03247   120 VLLDEPTVGLDPITERQL---LSLIFEVLkDKTLIWITHHLTGIE-HMDKILFLENGKI 174
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 26-220 1.75e-23

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: 94.26  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVP----VSGEIRFGDRLVARAGWglppeQRDIGMVFQDYALWPHMSVAQ 101
Cdd:cd03234    27 SLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKPDQF-----QKCVAYVRQDDILLPGLTVRE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAF--PLRMRGVSRSE--RERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRE 177
Cdd:cd03234   101 TLTYtaILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1405942281 178 SLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:cd03234   181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 21-221 1.99e-23

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 94.38  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrfgdRLVARAGWGLppeqrDIGMVFQdyalwPHMSVA 100
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV----EVNGRVSALL-----ELGAGFH-----PELTGR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLC 180
Cdd:COG1134   107 ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1405942281 181 GEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1134   187 ARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 7-220 3.75e-23

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 97.04  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLD--RFSLHidPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLpPEQRDI 84
Cdd:PRK15439   12 LCARSISKQYSGVEVLKgiDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWPHMSVAQNVAFPLrmrgVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK15439   89 YLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 165 DEPLSNLDSELRESLCGEMsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK15439  165 DEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 26-219 4.23e-23

nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 93.20  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKST----LLRLLAGLSVPVSGEIRFGDRLVAragwGLPPEQRDIGMVFQD--YALWPHMSV 99
Cdd:TIGR02770   6 NLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLL----PLSIRGRHIATIMQNprTAFNPLFTM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAE---RKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELR 176
Cdd:TIGR02770  82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1405942281 177 ESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-221 6.51e-23

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 96.13  E-value: 6.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA--------RAGwglppeqrdIGMVFQDYAL 93
Cdd:PRK11288   20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaalAAG---------VAIIYQELHL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  94 WPHMSVAQNV---AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:PRK11288   91 VPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 171 LDSelRESlcGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK11288  171 LSA--REI--EQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 12-219 6.98e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 93.62  E-value: 6.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA-RAGWG---LPPEQRDIGMV 87
Cdd:PRK14271   27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgRSIFNyrdVLEFRRRVGML 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 FQDYALWPhMSVAQNVAFPLRMRGVSRSERERRVSEA-LARVGL-NGFAER---KPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:PRK14271  107 FQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQArLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVL 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 163 LFDEPLSNLDSELREslcgEMSRLLRQLG--ITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK14271  186 LLDEPTSALDPTTTE----KIEEFIRSLAdrLTVIIVTHNLAQAARISDRAALFFDGRL 240
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 26-219 7.51e-23

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: 92.97  E-value: 7.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR----------------LVARAGWGLPPEQRDIGMVFQ 89
Cdd:TIGR02323  23 SFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelelyqlseaerrRLMRTEWGFVHQNPRDGLRMR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  90 dyalwphMSVAQNVAFPLRMRGVSRSERERRVSEA-LARVGLN-GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:TIGR02323 103 -------VSAGANIGERLMAIGARHYGNIRATAQDwLEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 7-219 8.25e-23

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 96.33  E-value: 8.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGdrlvaragwGLPPEQ-- 81
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD---------GVPLVQyd 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 -----RDIGMVFQDYALWPHmSVAQNVAFplrmrGVSRSERERRVSEALA----------RVGLNGFAERKPSGLSGGQQ 146
Cdd:TIGR00958 550 hhylhRQVALVGQEPVLFSG-SVRENIAY-----GLTDTPDEEIMAAAKAanahdfimefPNGYDTEVGEKGSQLSGGQK 623

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 147 QRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlgiTAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASR----TVLLIAHRLSTVE-RADQILVLKKGSV 691
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
10-221 8.84e-23

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 93.13  E-value: 8.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  10 QEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEI--------RFGDRLVARAgwglppeq 81
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASKEVARR-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 rdIGMVFQDYALWPHMSVAQNVAF------PLRMRGvsRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAI 155
Cdd:PRK10253   83 --IGLLAQNATTPGDITVQELVARgryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 156 VAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK10253  159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 22-200 1.90e-22

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: 94.87  E-value: 1.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGE--IRFGDRLVARAGWGLPPEQRD---IGMVFQDYALWPH 96
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRGRAkryIGILHQEYDLYPH 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNV--AFPLRMrgvsrsERERRVSEALARVGLNGFAERK--------PSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:TIGR03269 380 RTVLDNLteAIGLEL------PDELARMKAVITLKMVGFDEEKaeeildkyPDELSEGERHRVALAQVLIKEPRIVILDE 453

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1405942281 167 PLSNLDSELRESLCGEMSRLLRQLGITAVYVTHD 200
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 7-215 3.76e-22

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: 89.14  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFgdrlvaragwglpPEQRDIG 85
Cdd:cd03223     1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------PEGEDLL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDyalwPHM---SVAQNVAFPLRMRgvsrsererrvsealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVL 162
Cdd:cd03223    68 FLPQR----PYLplgTLREQLIYPWDDV------------------------------LSGGEQQRLAFARLLLHKPKFV 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 163 LFDEPLSNLDSELRESLCgemsRLLRQLGITAVYVTHdRREAELLADQIVYLS 215
Cdd:cd03223   114 FLDEATSALDEESEDRLY----QLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
7-219 4.15e-22

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 94.01  E-value: 4.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF-AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLppEQRDIG 85
Cdd:PRK10790  341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHmSVAQNVAfplrmrgVSRSERERRVSEALARVGLNGFAERKPSG-----------LSGGQQQRVALARA 154
Cdd:PRK10790  419 MVQQDPVVLAD-TFLANVT-------LGRDISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARV 490

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMsRLLRQlGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:PRK10790  491 LVQTPQILILDEATANIDSGTEQAIQQAL-AAVRE-HTTLVVIAH-RLSTIVEADTILVLHRGQA 552
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 21-220 4.51e-22

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: 89.51  E-value: 4.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLS--VPVSGEIRFGDRLVARagwgLPPEQR---DIGMVFQDyalwp 95
Cdd:cd03217    15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITD----LPPEERarlGIFLAFQY----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 hmsvaqnvafPLRMRGVSRSERERRVSEalarvglngfaerkpsGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSEL 175
Cdd:cd03217    86 ----------PPEIPGVKNADFLRYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1405942281 176 RESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVY-LSAGRVA 220
Cdd:cd03217   140 LRLVAEVINKLREE-GKSVLIITHYQRLLDYIKPDRVHvLYDGRIV 184
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
25-221 4.79e-22

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 93.54  E-value: 4.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHidPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA--------RAGWGLPPEQRdigmvfQDYALWPH 96
Cdd:COG1129   273 FSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdaiRAGIAYVPEDR------KGEGLVLD 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNVAFP----LRMRGVSRSERERRVSEALARvGLN---GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLS 169
Cdd:COG1129   345 LSIRENITLAsldrLSRGGLLDRRRERALAEEYIK-RLRiktPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 170 NLD----SELReslcgemsRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:COG1129   424 GIDvgakAEIY--------RLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVG 474
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 7-224 1.40e-21

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: 92.58  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSV--PVSGEIRF-GDRLVARAgwGLPPEQRD 83
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWsGSPLKASN--IRDTERAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAF--PLRMRG--VSRSERERRVSEALARVGLNGFAERKPSG-LSGGQQQRVALARAIVAA 158
Cdd:TIGR02633  80 IVIIHQELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRA 224
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILL-DIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 7-219 2.07e-21

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 92.20  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwglppeqrdi 84
Cdd:PRK11160  339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD------------ 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 gmvFQDYALWPHMS-VAQNV---AFPLR--MRGVSRSERERRVSEALARVGLNGFAERKPS----------GLSGGQQQR 148
Cdd:PRK11160  407 ---YSEAALRQAISvVSQRVhlfSATLRdnLLLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 149 VALARAIVA-APRVLLfDEPLSNLDSELREslcgEMSRLLRQL--GITAVYVTHDRREAELLaDQIVYLSAGRV 219
Cdd:PRK11160  484 LGIARALLHdAPLLLL-DEPTEGLDAETER----QILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-167 2.27e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 92.11  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF--GDRLVARAgwglppeqRDi 84
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDMADARH--------RR- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 gMVFQDYA---------LWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERkPSG-LSGGQQQRVALARA 154
Cdd:NF033858   73 -AVCPRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAGkLSGGMKQKLGLCCA 150

                         170
                  ....*....|...
gi 1405942281 155 IVAAPRVLLFDEP 167
Cdd:NF033858  151 LIHDPDLLILDEP 163
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 21-219 2.44e-21

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: 87.10  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVA--------RAGWGLPPEQRdigmvfQDYA 92
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdaiRAGIAYVPEDR------KREG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  93 LWPHMSVAQNVAFPlrmrgvsrsererrvsealarvglngfaerkpSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:cd03215    89 LVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1405942281 173 SELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:cd03215   137 VGAKA----EIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-222 6.98e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.57  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  23 DRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARagwGLPPEQRdIGMVFQDYALWPHMSVAQ 101
Cdd:NF033858  283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGQPVDAG---DIATRRR-VGYMSQAFSLYGELTVRQ 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 102 NVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCG 181
Cdd:NF033858  359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1405942281 182 EMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAAV 222
Cdd:NF033858  439 LLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLAS 478
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
7-231 7.78e-21

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 90.23  E-value: 7.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPE---QRD 83
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK----LDHKlaaQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNV---AFPLR----MRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIV 156
Cdd:PRK09700   82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPTSGE 231
Cdd:PRK09700  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 9-219 1.27e-20

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 86.55  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFA------ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAG--LSVPVSGEIRFgdrlvaragwglppe 80
Cdd:COG2401    27 VAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV--------------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 qrdigmvfQDYALWPHMSVAQNVAfplrmRGVSRSErerrVSEALARVGLNG--FAERKPSGLSGGQQQRVALARAIVAA 158
Cdd:COG2401    92 --------PDNQFGREASLIDAIG-----RKGDFKD----AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAER 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVT-HDRREAELLADQIVYLSAGRV 219
Cdd:COG2401   155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAThHYDVIDDLQPDLLIFVGYGGV 216
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 7-219 2.60e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.99  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF----AETPVLDRFSLHIDPGRIVALLGPSGCGKS----TLLRLLAglSVPV---SGEIRFGDRLVARAgw 75
Cdd:PRK15134    6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGESLLHA-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  76 glpPEQR-------DIGMVFQD--YALWPHMSVAQNVAFPLRM-RGVSRSERERRVSEALARVGLNGFAER---KPSGLS 142
Cdd:PRK15134   82 ---SEQTlrgvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 143 GGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK15134  159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 22-219 3.50e-20

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 87.06  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRlvaragwgLPPEQR-----DIGMVF-QDYALWP 95
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY--------VPFKRRkefarRIGVVFgQRSQLWW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNvaFPL--RMRGVSRSERERRVSEALARVGLNGFAE---RKpsgLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:COG4586   110 DLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDtpvRQ---LSLGQRMRCELAAALLHRPKILFLDEPTIG 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 171 LD----SELRESLcgemSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:COG4586   185 LDvvskEAIREFL----KEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
12-174 4.39e-20

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 84.90  E-value: 4.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglpPEQRDIGMVFQDY 91
Cdd:PRK13543   17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-----DRSRFMAYLGHLP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVAFplrMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PRK13543   92 GLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168


                  ...
gi 1405942281 172 DSE 174
Cdd:PRK13543  169 DLE 171
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
7-219 6.25e-20

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 87.71  E-value: 6.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD---RLVARAGWglppeQR 82
Cdd:PRK13657  335 VEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASL-----RR 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDyALWPHMSVAQNvafpLRMRGVSRSERERRvsEALARVGLNGFAERKPSG-----------LSGGQQQRVAL 151
Cdd:PRK13657  410 NIAVVFQD-AGLFNRSIEDN----IRVGRPDATDEEMR--AAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAI 482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRqlGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:PRK13657  483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRV 547
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 1-173 1.09e-19

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: 83.47  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTPITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP---VSGEIRFGdrlvaragwG 76
Cdd:cd03233     1 ASTLSWRNISFTTGKGRsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYN---------G 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  77 LPPE------QRDIGMVFQDYALWPHMSVAQNVAFPLRMRGvsrsererrvsealarvglNGFAerkpSGLSGGQQQRVA 150
Cdd:cd03233    72 IPYKefaekyPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-------------------NEFV----RGISGGERKRVS 128

                         170       180
                  ....*....|....*....|...
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDS 173
Cdd:cd03233   129 IAEALVSRASVLCWDNSTRGLDS 151
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
7-219 2.01e-19

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 83.39  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVarAGWGLPPEQR-DIG 85
Cdd:PRK11614    6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI--TDWQTAKIMReAVA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHMSVAQNVAfplrMRG--VSRS---ERERRVSEALARVglngfAERK---PSGLSGGQQQRVALARAIVA 157
Cdd:PRK11614   84 IVPEGRRVFSRMTVEENLA----MGGffAERDqfqERIKWVYELFPRL-----HERRiqrAGTMSGGEQQMLAIGRALMS 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11614  155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
PLN03211 PLN03211
ABC transporter G-25; Provisional
 6-218 2.03e-19

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 86.47  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGL--SVPVSGEIRFGDRLVARagwglpPEQRD 83
Cdd:PLN03211   68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK------QILKR 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQDYALWPHMSVAQNVAFP--LRM-RGVSRSERERRVSEALARVGL---------NGFAErkpsGLSGGQQQRVAL 151
Cdd:PLN03211  142 TGFVTQDDILYPHLTVRETLVFCslLRLpKSLTKQEKILVAESVISELGLtkcentiigNSFIR----GISGGERKRVSI 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 152 ARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTH--DRREAELLaDQIVYLSAGR 218
Cdd:PLN03211  218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS-LAQKGKTIVTSMHqpSSRVYQMF-DSVLVLSEGR 284
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-219 2.58e-19

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: 86.01  E-value: 2.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSV--PVSGEIRFGDRLVARAGWGLPPE---- 80
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALCEKCGYVERPSkvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  81 ---------------------------QRDIGMVFQ-DYALWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNG 132
Cdd:TIGR03269  81 pcpvcggtlepeevdfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 133 FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIV 212
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240


                  ....*..
gi 1405942281 213 YLSAGRV 219
Cdd:TIGR03269 241 WLENGEI 247
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 9-226 2.92e-19

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.83  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglPPEQRD--IGM 86
Cdd:PRK10762    7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNG---PKSSQEagIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNV----AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:PRK10762   84 IHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 163 LFDEPLSNL-DSElRESLCgEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVT 226
Cdd:PRK10762  164 IMDEPTDALtDTE-TESLF-RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVA 226
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 7-219 5.75e-19

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 85.18  E-value: 5.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFA-ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGdrlvaragwGLPPEQRDIG 85
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN---------GFSLKDIDRH 544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQDYALWPHM------SVAQNVAFPLRmRGVSRSERERRVSEALAR-------VGLNGFAERKPSGLSGGQQQRVALA 152
Cdd:TIGR01193 545 TLRQFINYLPQEpyifsgSILENLLLGAK-ENVSQDEIWAACEIAEIKddienmpLGYQTELSEEGSSISGGQKQRIALA 623

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 153 RAIVAAPRVLLFDEPLSNLDSELRESLcgeMSRLLRQLGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-221 6.07e-19

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 82.95  E-value: 6.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAG--------LSVPVSGEIRFGDRLVARagwgLPPEQ--RDIGMVFQD 90
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAA----IDAPRlaRLRAVLPQA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  91 YALWPHMSVAQNVA---FPLRMRGVSRSERERRV-SEALARVGLNGFAERKPSGLSGGQQQRVALARAI---------VA 157
Cdd:PRK13547   92 AQPAFAFSAREIVLlgrYPHARRAGALTHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 158 APRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13547  172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 14-217 2.18e-18

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: 83.91  E-value: 2.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   14 FAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwgLPPEQRDIGMVFQDYAL 93
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---ISDVHQNMGYCPQFDAI 2023

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   94 WPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:TIGR01257 2024 DDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1405942281  174 ELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAG 217
Cdd:TIGR01257 2104 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-218 3.23e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 82.53  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGlsvpV------SGEIRFGDRLVA----RAGwglppEQRDIGMVFQDY 91
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG----VyphgsyEGEILFDGEVCRfkdiRDS-----EALGIVIIHQEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVaF---PLRMRGV-SRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040905   88 ALIPYLSIAENI-FlgnERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 168 ---LSNLDSE-----LREslcgemsrlLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:NF040905  167 taaLNEEDSAalldlLLE---------LKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-221 4.16e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 79.94  E-value: 4.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTPITLQEvsfAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDR------LVARAg 74
Cdd:PRK10895    1 MATLTAKNLAK---AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllpLHARA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  75 wglppeQRDIGMVFQDYALWPHMSVAQNVAFPLRMR-GVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALAR 153
Cdd:PRK10895   77 ------RRGIGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIAR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSeLRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK10895  151 ALAANPKFILLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
7-174 5.35e-18

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 82.37  E-value: 5.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAF--AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrFGDRLVARAgWGLPPEQRDI 84
Cdd:PRK11176  342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDGHDLRD-YTLASLRNQV 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  85 GMVFQDYALWpHMSVAQNVAFPlRMRGVSRSERERRVSEALARvglnGFAERKPSG-----------LSGGQQQRVALAR 153
Cdd:PRK11176  420 ALVSQNVHLF-NDTIANNIAYA-RTEQYSREQIEEAARMAYAM----DFINKMDNGldtvigengvlLSGGQRQRIAIAR 493

                         170       180
                  ....*....|....*....|.
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSE 174
Cdd:PRK11176  494 ALLRDSPILILDEATSALDTE 514
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 21-190 7.63e-18

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 82.08  E-value: 7.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSvpVSGEIRFGDRLVaragwGLPPE----QRDIGMVFQDYALWPH 96
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLV-----NGRPLdssfQRSIGYVQQQDLHLPT 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   97 MSVAQNVAFPLRMR---GVSRSERERRVSE----------ALARVGLNGfaerkpSGLSGGQQQRVALARAIVAAPRVLL 163
Cdd:TIGR00956  851 STVRESLRFSAYLRqpkSVSKSEKMEYVEEvikllemesyADAVVGVPG------EGLNVEQRKRLTIGVELVAKPKLLL 924

                          170       180
                   ....*....|....*....|....*...
gi 1405942281  164 F-DEPLSNLDSELRESLCgemsRLLRQL 190
Cdd:TIGR00956  925 FlDEPTSGLDSQTAWSIC----KLMRKL 948
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 23-230 7.81e-18

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: 79.72  E-value: 7.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  23 DRFSLH----IDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGeiRFGDrlvaragwglPPEQRDI-----GMVFQDY-- 91
Cdd:cd03236    13 NSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDD----------PPDWDEIldefrGSELQNYft 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 -ALWPHMSVA---QNV-AFPLRMRG-----VSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRV 161
Cdd:cd03236    81 kLLEGDVKVIvkpQYVdLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 162 LLFDEPLSNLDSELRESlcgeMSRLLRQL---GITAVYVTHDRREAELLADqIVYLSAGRVAAVRAVTPTSG 230
Cdd:cd03236   161 YFFDEPSSYLDIKQRLN----AARLIRELaedDNYVLVVEHDLAVLDYLSD-YIHCLYGEPGAYGVVTLPKS 227
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 17-221 1.05e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 79.21  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  17 AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSvPVSGEIRFGDRLVA---------RAGWgLPPEQRD-IGM 86
Cdd:PRK03695    7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaaelarHRAY-LSQQQTPpFAM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 -VFQDYALwpHMSVAQNVAfplrmrgvsrsERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALA-------RAIVAA 158
Cdd:PRK03695   85 pVFQYLTL--HQPDKTRTE-----------AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 159 PRVLLFDEPLSNLDSELRESLcgemSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK03695  152 GQLLLLDEPMNSLDVAQQAAL----DRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 7-201 1.26e-17

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: 81.13  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLvaragwglppeqrDIGM 86
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-------------KLAY 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDY-ALWPHMSVAQNVAFPLRMRGVSRSERERRVSeaLARVGLNGFAERKPSG-LSGGQQQRVALARAIVAAPRVLLF 164
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAY--VGRFNFKGSDQQKKVGqLSGGERNRVHLAKTLKSGGNVLLL 467

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1405942281 165 DEPLSNLDSELRESLcgeMSRLLRQLGiTAVYVTHDR 201
Cdd:TIGR03719 468 DEPTNDLDVETLRAL---EEALLNFAG-CAVVISHDR 500
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 9-221 1.69e-17

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 78.57  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSV--PVSGEIRF-GDRLVAragwgLPPEQR--- 82
Cdd:COG0396     3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLdGEDILE-----LSPDERara 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDyalwphmsvaqnvafPLRMRGVS-----------RSERE-------RRVSEALARVGLN-GFAERkP--SGL 141
Cdd:COG0396    78 GIFLAFQY---------------PVEIPGVSvsnflrtalnaRRGEElsareflKLLKEKMKELGLDeDFLDR-YvnEGF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 142 SGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE-LResLCGEMSRLLRQLGITAVYVTHDRReaeLL----ADQIVYLSA 216
Cdd:COG0396   142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDaLR--IVAEGVNKLRSPDRGILIITHYQR---ILdyikPDFVHVLVD 216


                  ....*
gi 1405942281 217 GRVAA 221
Cdd:COG0396   217 GRIVK 221
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 26-219 2.27e-17

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 80.27  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVPVSGEIRFGD---RLVARAGWglppeQRDIGMVFQDYALwPHMSVAQN 102
Cdd:PRK11174  370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGielRELDPESW-----RKHLSWVGQNPQL-PHGTLRDN 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 103 VAfplrMRGVSRSERErrVSEALARVGLNGFAERKP-----------SGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PRK11174  443 VL----LGNPDASDEQ--LQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 172 D--SELR--ESLCGEMSRLlrqlgiTAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:PRK11174  517 DahSEQLvmQALNAASRRQ------TTLMVTH-QLEDLAQWDQIWVMQDGQI 561
cbiO PRK13646
energy-coupling factor transporter ATPase;
7-227 2.28e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 78.67  E-value: 2.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE-TP----VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWG--LPP 79
Cdd:PRK13646    3 IRFDNVSYTYQKgTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  80 EQRDIGMVFQdyalWPHM-----SVAQNVAFPLRMRGVSRSERERRVSEALARVGLN-GFAERKPSGLSGGQQQRVALAR 153
Cdd:PRK13646   83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELREslcgEMSRLLRQLGI----TAVYVTHDRREAELLADQIVYLSAGRVaaVRAVTP 227
Cdd:PRK13646  159 ILAMNPDIIVLDEPTAGLDPQSKR----QVMRLLKSLQTdenkTIILVSHDMNEVARYADEVIVMKEGSI--VSQTSP 230
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 20-229 2.53e-17

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 80.07  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwglPPEQRDIGMVF-----QDYALW 94
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYipedrLGRGLV 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNVAF------PLRMRGVSRSERERRVSEALARvglnGFAERKPS------GLSGGQQQRVALARAIVAAPRVL 162
Cdd:COG3845   349 PDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIE----EFDVRTPGpdtparSLSGGNQQKVILARELSRDPKLL 424

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 163 LFDEPLSNLD----SELRESLcgemsRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPTS 229
Cdd:COG3845   425 IAAQPTRGLDvgaiEFIHQRL-----LELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEAT 490
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 7-227 3.13e-17

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: 79.84  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRF-----SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWglpPEQ 81
Cdd:COG4615   328 LELRGVTYRYPGEDGDEGFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR---EAY 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RD-IGMVFQDYALwphmsvaqnvaFPlRMRGVSRSERERRVSEALARVGL--------NGFAERKpsgLSGGQQQRVALa 152
Cdd:COG4615   405 RQlFSAVFSDFHL-----------FD-RLLGLDGEADPARARELLERLELdhkvsvedGRFSTTD---LSQGQRKRLAL- 468

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 153 raIVA----APrVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRVAAVRAVTP 227
Cdd:COG4615   469 --LVAlledRP-ILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFD-LADRVLKMDYGKLVELTGPAA 543
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 20-201 4.22e-17

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: 79.59  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRfgdrlvaragwglPPEQRDIGMVFQDYALWPHMSV 99
Cdd:TIGR03719  19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-------------PQPGIKVGYLPQEPQLDPTKTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVafplrMRGVSRS----ERERRVSEALA------------------------------RVGLNGFAERKPSG----- 140
Cdd:TIGR03719  86 RENV-----EEGVAEIkdalDRFNEISAKYAepdadfdklaaeqaelqeiidaadawdldsQLEIAMDALRCPPWdadvt 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 141 -LSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDR 201
Cdd:TIGR03719 161 kLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERHLQEYPGTVVAVTHDR 218
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
 11-219 5.75e-17

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 79.23  E-value: 5.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  11 EVSFAFAETPVldrfSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGlppEQRDI-GMVFQ 89
Cdd:TIGR01194 351 EGSEGFALGPI----DLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRD---DYRDLfSAIFA 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  90 DYALW---------PHMSVAQNVAFplrmrgVSRSERERRVSealarvgLNGFAERKPSGLSGGQQQRVALARAIVAAPR 160
Cdd:TIGR01194 424 DFHLFddligpdegEHASLDNAQQY------LQRLEIADKVK-------IEDGGFSTTTALSTGQQKRLALICAWLEDRP 490

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 161 VLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGRV 219
Cdd:TIGR01194 491 ILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFE-LADQIIKLAAGCI 548
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 12-219 9.52e-17

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 77.47  E-value: 9.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFAFAETP--VLDRFSLHIDPGRIVALLGPSGCGKSTLlrllaglSVPVSGEIRFGDRLVA-------RAGWGLPPEQR 82
Cdd:PRK11022   11 VHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVS-------SLAIMGLIDYPGRVMAeklefngQDLQRISEKER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 ------DIGMVFQD--YALWPHMSVAQNVAFPLRM-RGVSRSERERRVSEALARVGLNGFAER---KPSGLSGGQQQRVA 150
Cdd:PRK11022   84 rnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 151 LARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK11022  164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 7-220 1.66e-16

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: 75.22  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAET--PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwgLPPEQ--R 82
Cdd:cd03244     3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK----IGLHDlrS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 DIGMVFQDyalwPHM---SVAQNVAfPLrmrGVSRSERerrVSEALARVGLNGFAERKPSGL-----------SGGQQQR 148
Cdd:cd03244    79 RISIIPQD----PVLfsgTIRSNLD-PF---GEYSDEE---LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 149 VALARAIVAAPRVLLFDEPLSNLDSELREslcgEMSRLLRQL--GITAVYVTHdRREAELLADQIVYLSAGRVA 220
Cdd:cd03244   148 LCLARALLRKSKILVLDEATASVDPETDA----LIQKTIREAfkDCTVLTIAH-RLDTIIDSDRILVLDKGRVV 216
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 11-172 2.90e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 74.22  E-value: 2.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  11 EVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwGLPPEQRDIGMVFQD 90
Cdd:PRK13540    6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLCTYQKQLCFVGHR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  91 YALWPHMSVAQNVAFPLRMrgvsrSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:PRK13540   83 SGINPYLTLRENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157


                  ..
gi 1405942281 171 LD 172
Cdd:PRK13540  158 LD 159
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 7-219 5.86e-16

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 76.08  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRfgdrlvaragWGlppEQRDIGM 86
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----------WS---ENANIGY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYA--------LWPHMSVAqnvafplrmrgvsRSER--ERRVSEALARVGLNGFAERKP-SGLSGGQQQRVALARAI 155
Cdd:PRK15064  387 YAQDHAydfendltLFDWMSQW-------------RQEGddEQAVRGTLGRLLFSQDDIKKSvKVLSGGEKGRMLFGKLM 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 156 VAAPRVLLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK15064  454 MQKPNVLVMDEPTNHMDMESIESL----NMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 31-212 1.34e-15

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: 75.21  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  31 PGRIVALLGPSGCGKSTLLRLLAGLSVPvsgeiRFGDrlvaragWGLPPEQRDI-----GMVFQDY-----------ALW 94
Cdd:COG1245    98 KGKVTGILGPNGIGKSTALKILSGELKP-----NLGD-------YDEEPSWDEVlkrfrGTELQDYfkklangeikvAHK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PhmsvaQNVAF-PLRMRGVSRS--ER--ERRVSEALA-RVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:COG1245   166 P-----QYVDLiPKVFKGTVREllEKvdERGKLDELAeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405942281 169 SNLDseLRESLcgEMSRLLRQL---GITAVYVTHDRREAELLADQIV 212
Cdd:COG1245   241 SYLD--IYQRL--NVARLIRELaeeGKYVLVVEHDLAILDYLADYVH 283
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 7-220 1.49e-15

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: 75.37  E-value: 1.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281    7 ITLQEVSFAFA--ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFgdrlvaRAGWGLPPEQrdi 84
Cdd:TIGR00957  637 ITVHNATFTWArdLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------KGSVAYVPQQ--- 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   85 gmvfqdyALWPHMSVAQNVAFPLRMRgvsrSERERRVSEALArvgLNGFAERKPSG-----------LSGGQQQRVALAR 153
Cdd:TIGR00957  708 -------AWIQNDSLRENILFGKALN----EKYYQQVLEACA---LLPDLEILPSGdrteigekgvnLSGGQKQRVSLAR 773

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281  154 AIVAAPRVLLFDEPLSNLDSELR----ESLCGEMSRLlrqLGITAVYVTHDRREAELLaDQIVYLSAGRVA 220
Cdd:TIGR00957  774 AVYSNADIYLFDDPLSAVDAHVGkhifEHVIGPEGVL---KNKTRILVTHGISYLPQV-DVIIVMSGGKIS 840
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
26-200 2.73e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 72.99  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARA---------------GWGLPPEQRDIGMVfqd 90
Cdd:PRK15056   27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvpqseevDWSFPVLVEDVVMM--- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  91 yALWPHMSVaqnvafplrMRGVSRSERERrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:PRK15056  104 -GRYGHMGW---------LRRAKKRDRQI-VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 1405942281 171 LDSElRESLCGEMSRLLRQLGITAVYVTHD 200
Cdd:PRK15056  173 VDVK-TEARIISLLRELRDEGKTMLVSTHN 201
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 7-218 9.60e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 72.70  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFA-----FAETPVldrfSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGlpPEQ 81
Cdd:PRK10522  323 LELRNVTFAyqdngFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE--DYR 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWPHMsvaqnvafplrMRGVSRSERERRVSEALARVGLNG---FAERKPSG--LSGGQQQRVALARAIV 156
Cdd:PRK10522  397 KLFSAVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALA 465

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 157 AAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAElLADQIVYLSAGR 218
Cdd:PRK10522  466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ 526
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 22-212 1.17e-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: 70.90  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPG-----RIVALLGPSGCGKSTLLRLLAGlsvpvsgeirfgdrlvaragwGLPPEQRDIGMVFQDYALWPH 96
Cdd:cd03237    10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAG---------------------VLKPDEGDIEIELDTVSYKPQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQnvaFPLRMRGVSRSERERRV------SEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSN 170
Cdd:cd03237    69 YIKAD---YEGTVRDLLSSITKDFYthpyfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1405942281 171 LDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIV 212
Cdd:cd03237   146 LDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 26-220 1.30e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 72.39  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLV------ARAGWGLP--PEQRDIGMVFQDYAL-WPH 96
Cdd:PRK15439  283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalstaQRLARGLVylPEDRQSSGLYLDAPLaWNV 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNvafplRMRGVSRSERERRVSEALAR---VGLNGfAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:PRK15439  363 CALTHN-----RRGFWIKPARENAVLERYRRalnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1405942281 174 ELReslcGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK15439  437 SAR----NDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 29-218 1.33e-14

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 72.45  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   29 IDPGRIVALLGPSGCGKSTLLRLLA----GLSVPVSGEIRFGdrlvaragwGLPPEqrDIGMVFQDYALW--------PH 96
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYD---------GITPE--EIKKHYRGDVVYnaetdvhfPH 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   97 MSVAQNVAFPLRMR-------GVSRSERERRVSEALARV-GL---------NGFAErkpsGLSGGQQQRVALARAIVAAP 159
Cdd:TIGR00956  153 LTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATyGLshtrntkvgNDFVR----GVSGGERKRVSIAEASLGGA 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281  160 RVLLFDEPLSNLDS----ELRESLcGEMSRLLRQLGITAVYvtHDRREAELLADQIVYLSAGR 218
Cdd:TIGR00956  229 KIQCWDNATRGLDSatalEFIRAL-KTSANILDTTPLVAIY--QCSQDAYELFDKVIVLYEGY 288
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
18-217 2.24e-14

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 71.09  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETP-----VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP---VSGE-IRFGDR-LVAragwgLPPEQR----- 82
Cdd:COG4170    14 DTPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhVTADrFRWNGIdLLK-----LSPRERrkiig 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 -DIGMVFQD--YALWPHMSVAQNV--AFPLRMRGVS----RSERERRVSEALARVG-------LNGFaerkPSGLSGGQQ 146
Cdd:COG4170    89 rEIAMIFQEpsSCLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGikdhkdiMNSY----PHELTEGEC 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 147 QRVALARAIVAAPRVLLFDEPLSNLDSELReslcGEMSRLLRQL----GITAVYVTHDRREAELLADQIVYLSAG 217
Cdd:COG4170   165 QKVMIAMAIANQPRLLIADEPTNAMESTTQ----AQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCG 235
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 20-199 6.21e-14

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: 68.51  E-value: 6.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDIGMVFQDYALWP-HMS 98
Cdd:cd03290    15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLlNAT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAF--PLRmrgvsrSERERRVSEALA---RVGLNGFAERKPSG-----LSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:cd03290    95 VEENITFgsPFN------KQRYKAVTDACSlqpDIDLLPFGDQTEIGerginLSGGQRQRICVARALYQNTNIVFLDDPF 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1405942281 169 SNLDSELRESLCGE-MSRLLRQLGITAVYVTH 199
Cdd:cd03290   169 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTH 200
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 25-218 6.27e-14

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 69.75  E-value: 6.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHidPGRIVALLGPSGCGKS----TLLRLLAGLSVpVSGEIRFGDRLVAragwGLPPEQ------RDIGMVFQD--YA 92
Cdd:PRK09473   37 FSLR--AGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREIL----NLPEKElnklraEQISMIFQDpmTS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  93 LWPHMSVAQNVAFPLRM-RGVSRSER-ERRVS--------EALARVGLngfaerKPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:PRK09473  110 LNPYMRVGEQLMEVLMLhKGMSKAEAfEESVRmldavkmpEARKRMKM------YPHEFSGGMRQRVMIAMALLCRPKLL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942281 163 LFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK09473  184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 9-201 6.41e-14

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 70.20  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRF--GDRLVARAgwglppeQRDIGM 86
Cdd:PRK10636  315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakGIKLGYFA-------QHQLEF 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSvaqnvafplrmrGVSRSERERRVSEALARVGLNGFAERKPSG-LSGGQQQRVALARAIVAAPRVLLFD 165
Cdd:PRK10636  388 LRADESPLQHLA------------RLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLD 455

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 166 EPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDR 201
Cdd:PRK10636  456 EPTNHLDLDMRQAL----TEALIDFEGALVVVSHDR 487
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 9-201 6.79e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 70.36  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   9 LQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRL-VAragwglppeqrdigmV 87
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLeVA---------------Y 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  88 FQDY--ALWPHMSVAQNVAfplrmRG---VSRSERERRVSEALARVGLNGFAERKP-SGLSGGQQQRVALARAIVAAPRV 161
Cdd:PRK11147  387 FDQHraELDPEKTVMDNLA-----EGkqeVMVNGRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNL 461

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1405942281 162 LLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDR 201
Cdd:PRK11147  462 LILDEPTNDLDVETLELL----EELLDSYQGTVLLVSHDR 497
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
26-222 1.15e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 69.43  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAgwglPPEQRDIGMVF-----QDYALWPHMSV 99
Cdd:PRK09700  283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlNGKDISPRS----PLDAVKKGMAYitesrRDNGFFPNFSI 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVAFPLRMR--------GVSRSERERRVSEAlARVGLN---GFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK09700  359 AQNMAISRSLKdggykgamGLFHEVDEQRTAEN-QRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 169 SNLDSELReslcGEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAAV 222
Cdd:PRK09700  438 RGIDVGAK----AEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 20-201 1.60e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 68.99  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEirfgdrlvARAGWGLppeqrDIGMVFQDYALWPHMSV 99
Cdd:PRK11819   21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGI-----KVGYLPQEPQLDPEKTV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 AQNVafplrMRGVSRS----ERERRVSEALA-----------RVG--------LNGF-----------AERKPSG----- 140
Cdd:PRK11819   88 RENV-----EEGVAEVkaalDRFNEIYAAYAepdadfdalaaEQGelqeiidaADAWdldsqleiamdALRCPPWdakvt 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 141 -LSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDR 201
Cdd:PRK11819  163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL----EQFLHDYPGTVVAVTHDR 220
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
31-212 2.63e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 68.30  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  31 PGRIVALLGPSGCGKSTLLRLLAGLSVPvsgeiRFGDrlvaragWGLPPEQRDI-----GMVFQDY-----------ALW 94
Cdd:PRK13409   98 EGKVTGILGPNGIGKTTAVKILSGELIP-----NLGD-------YEEEPSWDEVlkrfrGTELQNYfkklyngeikvVHK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PhmsvaQNV-AFPLRMRGVSRS--ER--ERRVSEALA-RVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK13409  166 P-----QYVdLIPKVFKGKVREllKKvdERGKLDEVVeRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1405942281 169 SNLDseLRESLcgEMSRLLRQL--GITAVYVTHDRREAELLADQIV 212
Cdd:PRK13409  241 SYLD--IRQRL--NVARLIRELaeGKYVLVVEHDLAVLDYLADNVH 282
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 14-217 3.15e-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: 67.19  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  14 FAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRL--VARAGWGLPPEQRD---IGMVF 88
Cdd:cd03291    45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfSSQFSWIMPGTIKEniiFGVSY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  89 QDYAlwpHMSVAQnvAFPLRMRGVSRSERERRVseaLARVGLNgfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:cd03291   125 DEYR---YKSVVK--ACQLEEDITKFPEKDNTV---LGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPF 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 169 SNLD----SELRES-LCGEMSRLLRQLgITAvYVTHDRReaellADQIVYLSAG 217
Cdd:cd03291   188 GYLDvfteKEIFEScVCKLMANKTRIL-VTS-KMEHLKK-----ADKILILHEG 234
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 22-212 3.29e-13

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: 68.27  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRI-----VALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglppeQRdigmVFQDYalwpH 96
Cdd:COG1245   351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKP-------QY----ISPDY----D 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNvafpLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELR 176
Cdd:COG1245   416 GTVEEF----LRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 177 ESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIV 212
Cdd:COG1245   492 LAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 12-229 4.12e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 67.83  E-value: 4.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  12 VSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGWGLPPEQrDIGMVFQDY 91
Cdd:PRK10982    4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN-GISMVHQEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNV---AFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK10982   83 NLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 169 SNLdSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRVAAVRAVTPTS 229
Cdd:PRK10982  163 SSL-TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 13-217 4.23e-13

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: 68.01  E-value: 4.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   13 SFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRL--VARAGWGLPPEQRDigmvfqd 90
Cdd:TIGR01271  433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIsfSPQTSWIMPGTIKD------- 505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   91 yalwphmsvaqNVAFplrmrGVSRSE-RERRVSEALA-RVGLNGFAERKPS-------GLSGGQQQRVALARAIVAAPRV 161
Cdd:TIGR01271  506 -----------NIIF-----GLSYDEyRYTSVIKACQlEEDIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADL 569

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281  162 LLFDEPLSNLD----SELRES-LCGEMSRLLRQLgITAvYVTHDRReaellADQIVYLSAG 217
Cdd:TIGR01271  570 YLLDSPFTHLDvvteKEIFEScLCKLMSNKTRIL-VTS-KLEHLKK-----ADKILLLHEG 623
PLN03073 PLN03073
ABC transporter F family; Provisional
 7-220 4.59e-13

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 67.96  E-value: 4.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDR-FSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrFGDRLVARAgwglppeqrdig 85
Cdd:PLN03073  509 ISFSDASFGYPGGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMA------------ 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 mVFQDYalwpHMSVAQNVAFPL--RMR---GVSrserERRVSEALARVGLNGFAERKPS-GLSGGQQQRVALARAIVAAP 159
Cdd:PLN03073  576 -VFSQH----HVDGLDLSSNPLlyMMRcfpGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKP 646

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMsrLLRQLGItaVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PLN03073  647 HILLLDEPSNHLDLDAVEALIQGL--VLFQGGV--LMVSHDEHLISGSVDELWVVSEGKVT 703
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 7-201 5.00e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.45  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLvaragwglppeqrDIGM 86
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-------------KLAY 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDY-ALWPHMSVAQNVAFPLRMRGVSRSERERRvseA-LARVGLNGFAERKPSG-LSGGQQQRVALARAIVAAPRVLL 163
Cdd:PRK11819  392 VDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR---AyVGRFNFKGGDQQKKVGvLSGGERNRLHLAKTLKQGGNVLL 468

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1405942281 164 FDEPLSNLDSELRESLcgEmSRLLRQLGiTAVYVTHDR 201
Cdd:PRK11819  469 LDEPTNDLDVETLRAL--E-EALLEFPG-CAVVISHDR 502
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
16-221 6.74e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 6.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  16 FAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLlRLLAGLSVPVSGE--IRFGDRLVARAGWglppeQRDIGMVFQ-DYA 92
Cdd:NF000106   23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpWRF*TWCANRRAL-----RRTIG*HRPvR*G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  93 LWPHMSVAQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:NF000106   97 RRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1405942281 173 SELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:NF000106  177 PRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 20-220 8.23e-13

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: 65.13  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDrlVARAGWGLPPEQRDIGMVFQDyalwphmsv 99
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIPLEDLRSSLTIIPQD--------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 aqnvafPLRMRGVSRSE-------RERRVSEALaRVGLNGfaerkpSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:cd03369    91 ------PTLFSGTIRSNldpfdeySDEEIYGAL-RVSEGG------LNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1405942281 173 SELReslcGEMSRLLRQL--GITAVYVTHdRREAELLADQIVYLSAGRVA 220
Cdd:cd03369   158 YATD----ALIQKTIREEftNSTILTIAH-RLRTIIDYDKILVMDAGEVK 202
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
25-221 1.04e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 66.47  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVA-------RAGWGLPPEQRDI-GMVfqdyalwP 95
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDGKPIDIrsprdaiRAGIMLCPEDRKAeGII-------P 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  96 HMSVAQNVA-----FPLRMRGVSRSERERRvseaLARVGLNGFAERKPSG------LSGGQQQRVALARAIVAAPRVLLF 164
Cdd:PRK11288  345 VHSVADNINisarrHHLRAGCLINNRWEAE----NADRFIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILL 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 165 DEPLSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK11288  421 DEPTRGIDVGAKH----EIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 18-218 1.28e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.42  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKS----TLLRLLAGLSVPVSGE---IRFGDRLVARAGWGLPPEQR-----DIG 85
Cdd:PRK10261   28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDkmlLRRRSRQVIELSEQSAAQMRhvrgaDMA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  86 MVFQD--YALWPHMSVAQNVAFPLRM-RGVSRSERERRVSEALARVGL---NGFAERKPSGLSGGQQQRVALARAIVAAP 159
Cdd:PRK10261  108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRP 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1405942281 160 RVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGR 218
Cdd:PRK10261  188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 21-199 1.54e-12

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 66.31  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSvPVsgeirFGDRLVaragwgLPPEQRdIGMVFQDyalwPHMSVA 100
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PV-----YGGRLT------KPAKGK-LFYVPQR----PYMTLG 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 ---QNVAFP-----LRMRGVSRSERErrvsEALARVGLNGFAERKPSG---------LSGGQQQRVALARAIVAAPRVLL 163
Cdd:TIGR00954 530 tlrDQIIYPdssedMKRRGLSDKDLE----QILDNVQLTHILEREGGWsavqdwmdvLSGGEKQRIAMARLFYHKPQFAI 605

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 164 FDEPLSNLDSELReslcGEMSRLLRQLGITAVYVTH 199
Cdd:TIGR00954 606 LDECTSAVSVDVE----GYMYRLCREFGITLFSVSH 637
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-218 1.83e-12

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 65.59  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   1 MRTLTpitlqeVSFAFAETPV--LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP----VSGEIRFGDRLVARag 74
Cdd:PRK15093    6 IRNLT------IEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLR-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  75 wgLPPEQR------DIGMVFQD--YALWPHMSVAQNV--AFP---LRMRGVSRSE-RERRVSEALARVGL---NGFAERK 137
Cdd:PRK15093   78 --LSPRERrklvghNVSMIFQEpqSCLDPSERVGRQLmqNIPgwtYKGRWWQRFGwRKRRAIELLHRVGIkdhKDAMRSF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 138 PSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAG 217
Cdd:PRK15093  156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235


                  .
gi 1405942281 218 R 218
Cdd:PRK15093  236 Q 236
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 17-219 4.30e-12

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 63.57  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  17 AETPVLDRFSLHIDPGRIVALLGPSGCGKStlLRLLAGLSVPVSGEIRFGDRLVARaGWGLPPEQ---RDIGMVFQD--Y 91
Cdd:PRK10418   14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLD-GKPVAPCAlrgRKIATIMQNprS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 ALWPHMSVAQNVAFPLRMRGvsRSERERRVSEALARVGLNG---FAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:PRK10418   91 AFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405942281 169 SNLDSELRESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK10418  169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 22-190 5.11e-12

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: 62.65  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSvpVSGEIRfGDRLVarAGWGLPPE-QRDIGMVFQDYALWPHMSVA 100
Cdd:cd03232    23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT-GEILI--NGRPLDKNfQRSTGYVEQQDVHSPNLTVR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRSERerrvsealarvglngfaerkpsglsggqqQRVALARAIVAAPRVLLFDEPLSNLDSELRESLC 180
Cdd:cd03232    98 EALRFSALLRGLSVEQR-----------------------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148

                         170
                  ....*....|
gi 1405942281 181 gemsRLLRQL 190
Cdd:cd03232   149 ----RFLKKL 154
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
7-220 8.22e-12

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 63.96  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwGLPPEQRDIGM 86
Cdd:PRK10789  316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--QLDSWRSRLAV 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHmSVAQNVAfpLRMRGVSRSERER-----RVSEALAR--------VGLNGFAerkpsgLSGGQQQRVALAR 153
Cdd:PRK10789  394 VSQTPFLFSD-TVANNIA--LGRPDATQQEIEHvarlaSVHDDILRlpqgydteVGERGVM------LSGGQKQRISIAR 464

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 154 AIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQlgiTAVYVTHDRREAELLADQIVYLSAGRVA 220
Cdd:PRK10789  465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIA 528
PLN03140 PLN03140
ABC transporter G family member; Provisional
 31-173 1.21e-11

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 63.71  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   31 PGRIVALLGPSGCGKSTLLRLLAGLSVP--VSGEIRFGdrlvaragwGLPPEQ----RDIGMVFQDYALWPHMSVAQNVA 104
Cdd:PLN03140   905 PGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRIS---------GFPKKQetfaRISGYCEQNDIHSPQVTVRESLI 975

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  105 FP--LRM-RGVSRSERERRVSEAL----------ARVGLNGFaerkpSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PLN03140   976 YSafLRLpKEVSKEEKMMFVDEVMelveldnlkdAIVGLPGV-----TGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050


                   ..
gi 1405942281  172 DS 173
Cdd:PLN03140  1051 DA 1052
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 7-179 3.19e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 60.27  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDrFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAgwglppEQRDIGM 86
Cdd:PRK13541    2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI------AKPYCTY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVAFPLRMRGVSRSererrVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDE 166
Cdd:PRK13541   75 IGHNLGLKLEMTVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149

                         170
                  ....*....|...
gi 1405942281 167 PLSNLDSELRESL 179
Cdd:PRK13541  150 VETNLSKENRDLL 162
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 25-221 3.56e-11

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: 62.15  E-value: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHidPGRIVALLGPSGCGKSTLLRLLAGlSVP--VSGEIRFGDRLVA--------RAGWGLPPEQRdigmvfQDYALW 94
Cdd:TIGR02633 281 FSLR--RGEILGVAGLVGAGRTELVQALFG-AYPgkFEGNVFINGKPVDirnpaqaiRAGIAMVPEDR------KRHGIV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  95 PHMSVAQNV------AFPLRMRgVSRSERERRVSEALARVGLNGFAERKP-SGLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:TIGR02633 352 PILGVGKNItlsvlkSFCFKMR-IDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 168 LSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 1-174 1.00e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 61.20  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281    1 MRTLTPITLQEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD----RLVARA 73
Cdd:PTZ00265   377 LKDIKKIQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLK 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   74 GWglppeQRDIGMVFQDYALWPHmSVAQNVAFPL---------------------------------------------- 107
Cdd:PTZ00265   457 WW-----RSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttd 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  108 -----RMRGVSRSERERRVSEALARVGLNGFAERKP-----------SGLSGGQQQRVALARAIVAAPRVLLFDEPLSNL 171
Cdd:PTZ00265   531 sneliEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL 610


                   ...
gi 1405942281  172 DSE 174
Cdd:PTZ00265   611 DNK 613
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 6-172 1.12e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 60.80  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   6 PITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAG-----LSVPVsgeIRFGDRlvaRAG----WG 76
Cdd:PRK10938  260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgYSNDL---TLFGRR---RGSgetiWD 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  77 LppeQRDIGMV----FQDYALwphMSVAQNVAFP--LRMRGVSR--SERERR-VSEALARVGLNGFAERKP-SGLSGGQQ 146
Cdd:PRK10938  334 I---KKHIGYVssslHLDYRV---STSVRNVILSgfFDSIGIYQavSDRQQKlAQQWLDILGIDKRTADAPfHSLSWGQQ 407

                         170       180
                  ....*....|....*....|....*.
gi 1405942281 147 QRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PRK10938  408 RLALIVRALVKHPTLLILDEPLQGLD 433
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
22-212 1.14e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.59  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRI-----VALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagwglPpeQRdigmVFQDYalwpH 96
Cdd:PRK13409  350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYK-----P--QY----IKPDY----D 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  97 MSVAQNvafpLRMRGVSRSERERRvSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELR 176
Cdd:PRK13409  415 GTVEDL----LRSITDDLGSSYYK-SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 177 ESLCGEMSRLLRQLGITAVYVTHDRREAELLADQIV 212
Cdd:PRK13409  490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
PTZ00243 PTZ00243
ABC transporter; Provisional
 26-220 4.15e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 59.41  E-value: 4.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   26 SLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrfgdrlvaragWGlppeQRDIGMVFQDyALWPHMSVAQNVAF 105
Cdd:PTZ00243   680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WA----ERSIAYVPQQ-AWIMNATVRGNILF 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  106 pLRMRGVSRSERERRVSEALARV-----GLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSE-----L 175
Cdd:PTZ00243   744 -FDEEDAARLADAVRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvgervV 822

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1405942281  176 RESLCGEMSrllrqlGITAVYVTHdrrEAELL--ADQIVYLSAGRVA 220
Cdd:PTZ00243   823 EECFLGALA------GKTRVLATH---QVHVVprADYVVALGDGRVE 860
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 7-172 8.09e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 57.11  E-value: 8.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLS--VPVSGEIRF-GDRLVAragwgLPPEQR- 82
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkGKDLLE-----LSPEDRa 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  83 --DIGMVFQdyalwphmsvaqnvaFPLRMRGVS---------RSERERRVSEALARVGLNGFAERK------PS------ 139
Cdd:PRK09580   77 geGIFMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQEPLDRFDFQDLMEEKiallkmPEdlltrs 141

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1405942281 140 ---GLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PRK09580  142 vnvGFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
PLN03130 PLN03130
ABC transporter C family member; Provisional
 4-173 1.30e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 57.83  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281    4 LTPITLQEVSFAF---AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGE---IRFGDRLVARAGWgl 77
Cdd:PLN03130   612 LPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvvIRGTVAYVPQVSW-- 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   78 ppeqrdigmVFqdyalwpHMSVAQNVAFPLRMRGvSRSERERRVS------EALARVGLNGFAERKPSgLSGGQQQRVAL 151
Cdd:PLN03130   690 ---------IF-------NATVRDNILFGSPFDP-ERYERAIDVTalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSM 751

                          170       180
                   ....*....|....*....|..
gi 1405942281  152 ARAIVAAPRVLLFDEPLSNLDS 173
Cdd:PLN03130   752 ARAVYSNSDVYIFDDPLSALDA 773
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 18-202 1.65e-09

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 56.19  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAG---LSVpVSGEIRFGDRLVARagwgLPPEQRD---IGMVFQdy 91
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILD----LEPEERAhlgIFLAFQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  92 alwphmsvaqnvaFPLRMRGVSRSE------RERR----------------VSEALARVGLN-GFAERKPS-GLSGGQQQ 147
Cdd:CHL00131   92 -------------YPIEIPGVSNADflrlayNSKRkfqglpeldplefleiINEKLKLVGMDpSFLSRNVNeGFSGGEKK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1405942281 148 RVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRR 202
Cdd:CHL00131  159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR 212
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 31-218 3.29e-09

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: 53.92  E-value: 3.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   31 PGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDrlvaragwglppeqrdigmvfqdyalwphmsvaqnvafplrmr 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  111 gvsrSERERRVSEALARVGLNGfaeRKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL-----CGEMSR 185
Cdd:smart00382  38 ----GEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLL 110

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1405942281  186 LLRQLGITAVYVTH-----DRREAELLADQIVYLSAGR 218
Cdd:smart00382 111 LKSEKNLTVILTTNdekdlGPALLRRRFDRRIVLLLIL 148
PLN03232 PLN03232
ABC transporter C family member; Provisional
 18-219 3.75e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 56.52  E-value: 3.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   18 ETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAG-------LSVPVSGEIRFgdrlVARAGWglppeqrdigmVFqd 90
Cdd:PLN03232   629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGelshaetSSVVIRGSVAY----VPQVSW-----------IF-- 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   91 yalwpHMSVAQNVAFPLRMRgvsrSERERRVSEALA-RVGLNGFAER-------KPSGLSGGQQQRVALARAIVAAPRVL 162
Cdd:PLN03232   692 -----NATVRENILFGSDFE----SERYWRAIDVTAlQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIY 762

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281  163 LFDEPLSNLDSEL-RESLCGEMSRLLRqlGITAVYVTHDRREAELLaDQIVYLSAGRV 219
Cdd:PLN03232   763 IFDDPLSALDAHVaHQVFDSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 29-212 3.80e-09

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: 54.12  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  29 IDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRfgdrlvaragwglppeqrdigmvfqdyalWPhmsvaqnvafplr 108
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-----------------------------WD------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 109 mrGVSRSERERRVSealarvglngfaerkpsgLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLR 188
Cdd:cd03222    60 --GITPVYKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119

                         170       180
                  ....*....|....*....|....
gi 1405942281 189 QLGITAVYVTHDRREAELLADQIV 212
Cdd:cd03222   120 EGKKTALVVEHDLAVLDYLSDRIH 143
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 96-173 1.89e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 54.26  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   96 HMSVAQNVAFplrmrGVSRSERE--RRVSEALArvgLNGFAERKPS-----------GLSGGQQQRVALARAIVAAPRVL 162
Cdd:PTZ00265  1309 NMSIYENIKF-----GKEDATREdvKRACKFAA---IDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKIL 1380

                           90
                   ....*....|.
gi 1405942281  163 LFDEPLSNLDS 173
Cdd:PTZ00265  1381 LLDEATSSLDS 1391
PLN03232 PLN03232
ABC transporter C family member; Provisional
 20-219 3.18e-08

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 53.83  E-value: 3.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   20 PVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARagWGLPPEQRDIGMVFQDYALWphmsv 99
Cdd:PLN03232  1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK--FGLTDLRRVLSIIPQSPVLF----- 1322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  100 AQNVAFPLRmrgvSRSER-ERRVSEALARVGLNGFAERKPSGL-----------SGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:PLN03232  1323 SGTVRFNID----PFSEHnDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEA 1398

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1405942281  168 LSNLDSELrESLcgeMSRLLRQ--LGITAVYVTHdRREAELLADQIVYLSAGRV 219
Cdd:PLN03232  1399 TASVDVRT-DSL---IQRTIREefKSCTMLVIAH-RLNTIIDCDKILVLSSGQV 1447
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 26-217 3.39e-08

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: 51.55  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLrlLAGLSVpvSGEIRFGDRLvaragwglppeqrdigmvfQDYALWPHMSVAQnvaf 105
Cdd:cd03238    15 DVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--SGKARLISFL-------------------PKFSRNKLIFIDQ---- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 106 pLRmrgvsrsererrvseALARVGLNGFA-ERKPSGLSGGQQQRVALARAIVAAPR--VLLFDEPLSNLDSELRESLCGE 182
Cdd:cd03238    68 -LQ---------------FLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1405942281 183 MSRlLRQLGITAVYVTHDRREAElLADQIVYLSAG 217
Cdd:cd03238   132 IKG-LIDLGNTVILIEHNLDVLS-SADWIIDFGPG 164
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 7-172 3.66e-08

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: 52.55  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQEVSFAFAE--TPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVPVSGEIRfgdrlVARAGWGLPPEQ--- 81
Cdd:cd03289     3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQ-----IDGVSWNSVPLQkwr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  82 RDIGMVFQDYALWphmsvaqnvAFPLRMR----GVSRSERERRVSEalaRVGLNGFAERKPSG-----------LSGGQQ 146
Cdd:cd03289    77 KAFGVIPQKVFIF---------SGTFRKNldpyGKWSDEEIWKVAE---EVGLKSVIEQFPGQldfvlvdggcvLSHGHK 144

                         170       180
                  ....*....|....*....|....*.
gi 1405942281 147 QRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:cd03289   145 QLMCLARSVLSKAKILLLDEPSAHLD 170
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 21-174 4.10e-08

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: 53.41  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVARAGwgLPPEQRDIGMVFQDYALWphmsva 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG--LHDLRFKITIIPQDPVLF------ 1372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  101 qnvAFPLRMRGVSRSE-RERRVSEALARVGLNGFAERKPSGL-----------SGGQQQRVALARAIVAAPRVLLFDEPL 168
Cdd:TIGR00957 1373 ---SGSLRMNLDPFSQySDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1449


                   ....*.
gi 1405942281  169 SNLDSE 174
Cdd:TIGR00957 1450 AAVDLE 1455
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 25-221 7.88e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 52.31  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  25 FSLHidPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR-FGDRLVARAgwglPPEQRDIGMVF--QDY---ALWPHMS 98
Cdd:PRK10762  273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTlDGHEVVTRS----PQDGLANGIVYisEDRkrdGLVLGMS 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  99 VAQNVAFPL-----RMRGVSRSERERRVSEALARVglngFAERKPS------GLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:PRK10762  347 VKENMSLTAlryfsRAGGSLKHADEQQAVSDFIRL----FNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEP 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 168 LSNLDSELREslcgEMSRLLRQL---GITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK10762  423 TRGVDVGAKK----EIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
22-219 1.14e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 50.97  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEI-RFGDRLVARAGWGLPPEqrdigmvfqdyalwphMSVA 100
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAGLSGQ----------------LTGI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLC 180
Cdd:PRK13546  104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1405942281 181 GEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13546  184 DKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 7-201 1.46e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 51.43  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   7 ITLQevsfaFAETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIrfgdrlvaragwGLPPEQRdIGM 86
Cdd:PRK15064    7 ITMQ-----FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV------------SLDPNER-LGK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  87 VFQDYALWPHMSVAQNVafplrMRGVS-----RSERER-------------RVSE------------ALARVG---LN-G 132
Cdd:PRK15064   69 LRQDQFAFEEFTVLDTV-----IMGHTelwevKQERDRiyalpemseedgmKVADlevkfaemdgytAEARAGellLGvG 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942281 133 FAERKPSGL----SGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLCGEmsrlLRQLGITAVYVTHDR 201
Cdd:PRK15064  144 IPEEQHYGLmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV----LNERNSTMIIISHDR 212
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 21-172 2.20e-07

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: 51.06  E-value: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLsVPVSGEIRFG----DRLVA---RAGWGLPPEQRDI-----GMVF 88
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDgvswNSVTLqtwRKAFGVIPQKVFIfsgtfRKNL 1312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   89 QDYALWphmsvaqnvafplrmrgvsrSERER-RVSEalaRVGLNGFAERKPSGL-----------SGGQQQRVALARAIV 156
Cdd:TIGR01271 1313 DPYEQW--------------------SDEEIwKVAE---EVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369

                          170
                   ....*....|....*.
gi 1405942281  157 AAPRVLLFDEPLSNLD 172
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD 1385
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 84-221 4.86e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 49.93  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  84 IGMVFQD---YALWPHMSVAQNVAFPL--RMRGVSR---SERERRVSEALARVGLNGFAERKPSG-LSGGQQQRVALARA 154
Cdd:PRK13549  340 IAMVPEDrkrDGIVPVMGVGKNITLAAldRFTGGSRiddAAELKTILESIQRLKVKTASPELAIArLSGGNQQKAVLAKC 419

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 155 IVAAPRVLLFDEPLSNLDSELRESLCGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRVAA 221
Cdd:PRK13549  420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
PLN03140 PLN03140
ABC transporter G family member; Provisional
 29-173 1.02e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.07  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   29 IDPGRIVALLGPSGCGKSTLLRLLAGL---SVPVSGEIRFGdrlvaraGWGLPP--EQRDIGMVFQDYALWPHMSVAQNV 103
Cdd:PLN03140   188 IKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYN-------GYRLNEfvPRKTSAYISQNDVHVGVMTVKETL 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  104 AFPLRMRGVSR-----SERERRVSEA-----------------------------LARVGLN-----GFAERKPSGLSGG 144
Cdd:PLN03140   261 DFSARCQGVGTrydllSELARREKDAgifpeaevdlfmkatamegvksslitdytLKILGLDickdtIVGDEMIRGISGG 340

                          170       180
                   ....*....|....*....|....*....
gi 1405942281  145 QQQRVALARAIVAAPRVLLFDEPLSNLDS 173
Cdd:PLN03140   341 QKKRVTTGEMIVGPTKTLFMDEISTGLDS 369
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 22-219 1.13e-06

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 48.73  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSG--EIRFGDRLVArAGWGLPPEQRDIgmvfqdyalwphmsv 99
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGtvDIKGSAALIA-ISSGLNGQLTGI--------------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 100 aQNVAFPLRMRGVSRSERERRVSEALARVGLNGFAERKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESL 179
Cdd:PRK13545  104 -ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1405942281 180 CGEMSRLLRQlGITAVYVTHDRREAELLADQIVYLSAGRV 219
Cdd:PRK13545  183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQV 221
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-175 2.17e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 48.24  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281   21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGDRLVarAGWGLPPEQRDIGMVFQDYALWPHmSVA 100
Cdd:PTZ00243  1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG-TVR 1401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  101 QNV-----AFP------LRMRGVsrseRERRVSEAlarVGLNGFAERKPSGLSGGQQQRVALARAIVA-APRVLLFDEPL 168
Cdd:PTZ00243  1402 QNVdpfleASSaevwaaLELVGL----RERVASES---EGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEAT 1474


                   ....*..
gi 1405942281  169 SNLDSEL 175
Cdd:PTZ00243  1475 ANIDPAL 1481
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 34-202 2.19e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.83  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  34 IVALLGPSGCGKSTLLR-LLAGL--SVPVSGEIRFGDRLVARAGwglppEQR-DIGMVFQ-----DYALWPHMSVAQNVA 104
Cdd:cd03240    24 LTLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREG-----EVRaQVKLAFEnangkKYTITRSLAILENVI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 105 FplrmrgvSRSErerrvsealarvGLNGFAERKPSGLSGGQQQ------RVALARAIVAAPRVLLFDEPLSNLDSE-LRE 177
Cdd:cd03240    99 F-------CHQG------------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEE 159

                         170       180
                  ....*....|....*....|....*
gi 1405942281 178 SLCGEMSRLLRQLGITAVYVTHDRR 202
Cdd:cd03240   160 SLAEIIEERKSQKNFQLIVITHDEE 184
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 21-214 3.28e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 47.47  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGlsvpvsgeirfgdRLVARAGWGLPPEQRDIGMVFQDYalwPHMSVA 100
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------------EISADGGSYTFPGNWQLAWVNQET---PALPQP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 101 QnvafplrMRGVSRSERERRVSE-------------ALARV---------------------GLnGFA----ERKPSGLS 142
Cdd:PRK10636   80 A-------LEYVIDGDREYRQLEaqlhdanerndghAIATIhgkldaidawtirsraasllhGL-GFSneqlERPVSDFS 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942281 143 GGQQQRVALARAIVAAPRVLLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYVTHDRREAELLADQIVYL 214
Cdd:PRK10636  152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL----EKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
PRK01889 PRK01889
GTPase RsgA; Reviewed
 22-67 6.30e-06

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 46.08  E-value: 6.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIRFGD 67
Cdd:PRK01889  185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDD 230
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 26-212 1.24e-05

ATP-binding cassette domain I 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: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 44.94  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLlrllAGLSVPVSGEIRFGDRLVARAGWGLPPEQRDigMVFQDYALWPHMSVAQNVAF 105
Cdd:cd03270    15 DVDIPRNKLVVITGVSGSGKSSL----AFDTIYAEGQRRYVESLSAYARQFLGQMDKP--DVDSIEGLSPAIAIDQKTTS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 106 P---------------LRMRgVSRSERERRVsEALARVGLNGFA-ERKPSGLSGGQQQRVALARAIVAAPRVLL--FDEP 167
Cdd:cd03270    89 RnprstvgtvteiydyLRLL-FARVGIRERL-GFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEP 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1405942281 168 LSNL----DSELRESLcgemsRLLRQLGITAVYVTHDrREAELLADQIV 212
Cdd:cd03270   167 SIGLhprdNDRLIETL-----KRLRDLGNTVLVVEHD-EDTIRAADHVI 209
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 17-52 4.83e-05

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 43.96  E-value: 4.83e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1405942281   17 AETPVLDRFSLHIDPGRIVALLGPSGCGKSTLLRLL 52
Cdd:COG5192     54 LHVPMVDRTPKDLPPPFIVAVVGPPGTGKSTLIRSL 89
GguA NF040905
sugar ABC transporter ATP-binding protein;
110-167 5.14e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.62  E-value: 5.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405942281 110 RGVSRSERERRVSEALaRVGLNgfaERKPS------GLSGGQQQRVALARAIVAAPRVLLFDEP 167
Cdd:NF040905  372 RGVIDENEEIKVAEEY-RKKMN---IKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
PLN03073 PLN03073
ABC transporter F family; Provisional
 118-172 1.26e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.54  E-value: 1.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1405942281 118 ERRVSEALArvGLNGFAE---RKPSGLSGGQQQRVALARAIVAAPRVLLFDEPLSNLD 172
Cdd:PLN03073  321 EARAASILA--GLSFTPEmqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 32-64 1.59e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 41.23  E-value: 1.59e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1405942281  32 GRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR 64
Cdd:cd01854    85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 125-212 1.78e-04

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: 42.31  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 125 LARVGLNGFA-ERKPSGLSGGQQQRVALARAIVAAPRVLLF--DEPLSNLDSELRESLCGEMSRlLRQLGITAVYVTHDr 201
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKR-LRDLGNTLIVVEHD- 549

                          90
                  ....*....|.
gi 1405942281 202 REAELLADQIV 212
Cdd:TIGR00630 550 EDTIRAADYVI 560
AAA_29 pfam13555
P-loop containing region of AAA domain;
23-65 2.02e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 38.35  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1405942281  23 DRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVPvSGEIRF 65
Cdd:pfam13555  13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARF 54
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 141-231 3.50e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 41.25  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 141 LSGGQQQRVALARAIVAAPRVLLFDEPLSNLDSELREslcgEMSRLLRQL-----GItaVYVTHDRREAELLADQIVYLS 215
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF----EIYQLIAELakkdkGI--IIISSEMPELLGITDRILVMS 465

                          90
                  ....*....|....*.
gi 1405942281 216 AGRVAAVRAVTPTSGE 231
Cdd:PRK10982  466 NGLVAGIVDTKTTTQN 481
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 32-64 9.72e-04

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.68  E-value: 9.72e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1405942281  32 GRIVALLGPSGCGKSTLLRLLAGLSVPVSGEIR 64
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 34-71 1.39e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 36.16  E-value: 1.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1405942281  34 IVALLGPSGCGKSTLLRLLA----GLSVPVSGEIRFGDRLVA 71
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAeqlgGRSVVVLDEIVILEGLYA 42
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 22-58 1.53e-03

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 39.17  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP 58
Cdd:TIGR00602 100 LKAQVLENAPKRILLITGPSGCGKSTTIKILSKELGI 136
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 34-65 1.92e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.47  E-value: 1.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1405942281  34 IVALLGPSGCGKSTLLRLLA---GLSVPVSGEIRF 65
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAkklGLPYLDTGGIRT 35
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 26-212 2.18e-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: 37.72  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281  26 SLHIDPGRIVALLGPSGCGKSTLLRllaglsvpvsgeirfgdrlvaragwglppeqrDIGmvfqdYALWPHMSvaqnvaf 105
Cdd:cd03227    15 DVTFGEGSLTIITGPNGSGKSTILD--------------------------------AIG-----LALGGAQS------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 106 plrmRGVSRSERERRVSEALARVGLNGFAerkpSGLSGGQQQRVALArAIVA----APRVL-LFDEPLSNLDSELRESLc 180
Cdd:cd03227    51 ----ATRRRSGVKAGCIVAAVSAELIFTR----LQLSGGEKELSALA-LILAlaslKPRPLyILDEIDRGLDPRDGQAL- 120

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1405942281 181 GEMSRLLRQLGITAVYVTHDRREAElLADQIV 212
Cdd:cd03227   121 AEAILEHLVKGAQVIVITHLPELAE-LADKLI 151
Rad17 pfam03215
Rad17 P-loop domain;
22-58 2.40e-03

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 37.63  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1405942281  22 LDRFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSVP 58
Cdd:pfam03215  35 LDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGP 71
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 141-211 3.80e-03

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 37.62  E-value: 3.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942281 141 LSGGQQQRVALArAIVAAPRV-----LLFDEPLSNLDSELRESLcgemSRLLRQLGITAVYV-THDRREAELLADQI 211
Cdd:cd03272   159 LSGGQKSLVALA-LIFAIQKCdpapfYLFDEIDAALDAQYRTAV----ANMIKELSDGAQFItTTFRPELLEVADKF 230
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
21-53 3.82e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 38.00  E-value: 3.82e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1405942281  21 VLDRFSLHIDPGRIVALLGPSGCGKSTLLRLLA 53
Cdd:COG1373     9 ILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLA 41
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
134-225 4.80e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942281 134 AERKPSGLSGGQqqRVALARAIVAAPRV--------LLFDEPLSNLDSELRESLCGEMSRLLRQlgITAV-YVTHDrREA 204
Cdd:PRK03918  782 KERPLTFLSGGE--RIALGLAFRLALSLylagniplLILDEPTPFLDEERRRKLVDIMERYLRK--IPQViIVSHD-EEL 856

                          90       100
                  ....*....|....*....|..
gi 1405942281 205 ELLADQIVYLSA-GRVAAVRAV 225
Cdd:PRK03918  857 KDAADYVIRVSLeGGVSKVEVV 878
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
 20-52 6.56e-03

Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.


Pssm-ID: 206669 [Multi-domain]  Cd Length: 231  Bit Score: 36.55  E-value: 6.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1405942281  20 PVLDRfSLHIDPGRIVALLGPSGCGKSTLLRLL 52
Cdd:cd01882    28 PVVDR-TPEEPPPLVVVVVGPPGVGKSTLIRSL 59
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
34-74 6.77e-03

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 36.38  E-value: 6.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1405942281   34 IVALLGPSGCGKSTLLRLLA--------GLSVPV-SGEIRFGDRLVARAG 74
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVAlivimaqiGSFVPAeSAELPVFDRIFTRIG 50
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 24-57 8.12e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 35.58  E-value: 8.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1405942281  24 RFSLHIDPGRIVALLGPSGCGKSTLLRLLAGLSV 57
Cdd:cd00009    11 REALELPPPKNLLLYGPPGTGKTTLARAIANELF 44
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 25-58 9.46e-03

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 35.84  E-value: 9.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1405942281  25 FSLHIDPGRIVALLGPSGCGKSTLLRLLAG-LSVP 58
Cdd:cd19518    27 QHLGVEPPRGVLLHGPPGCGKTMLANAIAGeLKVP 61
 
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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