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Conserved domains on  [gi|514971686|ref|WP_016659967|]
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MULTISPECIES: ABC transporter ATP-binding protein [Acinetobacter]

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.-.-.-
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 ...
12-354 1.02e-144

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 413.72  E-value: 1.02e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:COG3842    6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAQRVAQQLQ--TCFGAH---PISEALAhHQEPIRCCFRPHQVQVFSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3842  242 LPGTVLGDEGGgvRTGGRTlevPADAGLA-AGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 514971686 325 ILAQVSPAQTA-YQ--EQVYVRLDLQQCFFFAQ 354
Cdd:COG3842  321 LVVRVPNRAALpLEpgDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
12-354 1.02e-144

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 413.72  E-value: 1.02e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:COG3842    6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAQRVAQQLQ--TCFGAH---PISEALAhHQEPIRCCFRPHQVQVFSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3842  242 LPGTVLGDEGGgvRTGGRTlevPADAGLA-AGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 514971686 325 ILAQVSPAQTA-YQ--EQVYVRLDLQQCFFFAQ 354
Cdd:COG3842  321 LVVRVPNRAALpLEpgDRVGLSWDPEDVVVLPA 353
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
12-226 1.87e-100

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: 295.97  E-value: 1.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03259   77 VFQDYALFPHLTVAENIAFGLKlrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03259  157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
12-333 1.75e-97

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: 293.87  E-value: 1.75e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEqqqiPAEARNIGL 91
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL----PPQKRDYGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  250 IPAQRVA-QQLQTCFGAHPISEALAHHQEPIRCCFRPHQVQV-FSQPTTGAIPATVLSSSFMGHAEQLRLQLD--PETII 325
Cdd:TIGR03265 241 LPGTRGGgSRARVGGLTLACAPGLAQPGASVRLAVRPEDIRVsPAGNAANLLLARVEDMEFLGAFYRLRLRLEglPGQAL 320

                  ....*...
gi 514971686  326 LAQVSPAQ 333
Cdd:TIGR03265 321 VADVSASE 328
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-253 3.39e-88

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 270.67  E-value: 3.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQ 80
Cdd:PRK09452   4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----T 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 QIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK09452  80 HVPAENRHVNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEIL-KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQM-QNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
                        250
                 ....*....|....*.
gi 514971686 238 LFAARYFSALNEIPAQ 253
Cdd:PRK09452 239 LFVARFIGEINIFDAT 254
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
13-253 3.36e-74

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 234.12  E-value: 3.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSR----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIPAEAR 87
Cdd:NF040933   4 RVENVTKIFKKGkkevVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKlVASPGKIIVPPEDR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQ-RQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:NF040933  84 NIGMVFQNWALYPNMTVFDNIAFPLKikKVPKDEiEKKVKEVA-EILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYF 244
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242

                 ....*....
gi 514971686 245 SALNEIPAQ 253
Cdd:NF040933 243 GDINLLEGK 251
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
12-294 1.04e-71

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 227.27  E-value: 1.04e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:NF040840   2 IRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK----DITNLPPEKRGIAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:NF040840  77 VYQNYMLFPHKTVFENIAFGLKlrKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 514971686 250 IPAQRVAQQLQTCFGAHPISEALAHHQE-PIRCCFRPHQVQVFSQP 294
Cdd:NF040840 237 IEGVAEKGGEGTILDTGNIKIELPEEKKgKVRIGIRPEDITISTEK 282
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
12-224 1.25e-54

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


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 179.94  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqILWNEQQQIPAEAR 87
Cdd:NF040729   2 LKIQNISKTFINNKKENEVlkdiSFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEI-----LVNGNEVTKPGPDR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 niGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:NF040729  77 --GFVFQNYALFPWMTVKENIEYPMKqqKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDHRLRdQIRQNTIE-ILKQTGTTTVIVTHDPEEALQIADQIILM--HQGEIIQ 224
Cdd:NF040729 155 LMDEPLGAVDFQMR-QILQEELEsIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
27-172 1.43e-48

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 160.89  E-value: 1.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneQQQIPAEARNIGLVFQDYALFPHLSVLD 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT--DDERKSLRKEIGYVFQDPQLFPRLTVRE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  107 NVMFG--LKKLPKAQRQAVAEQALQHVSMQH----HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:pfam00005  79 NLRLGllLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
21-216 1.39e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 104.62  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  21 FGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNIGLVFQDYAL-- 98
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-------------AGGARVAYVPQRSEVpd 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  99 -FPhLSVLDNVMFG-------LKKLPKAQRqAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040873  69 sLP-LTVRDLVAMGrwarrglWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 171 FSNLDHRLRDQIrqntIEILKQ---TGTTTVIVTHDPEEALQIADQIIL 216
Cdd:NF040873 147 TTGLDAESRERI----IALLAEehaRGATVVVVTHDLELVRRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
15-241 2.24e-23

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 101.74  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  15 RQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqqiPAEARNI----- 89
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---------PVDAGDIatrrr 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 -GLVFQDYALFPHLSVLDNVM-----FGlkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:NF033858 341 vGYMSQAFSLYGELTVRQNLElharlFH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALY--RQPATLFAA 241
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVaaRGAATLEEA 496
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
36-216 1.64e-11

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: 61.62  E-value: 1.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqIPAEARNIGLVFQdyalfphlsvldnvmfglkkl 115
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDGEDILEEVLDQ--------------------- 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   116 pkaqrqavaeqalqhvSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQN-----TIEIL 190
Cdd:smart00382  49 ----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLK 112
                          170       180
                   ....*....|....*....|....*.
gi 514971686   191 KQTGTTTVIVTHDPEEALQIADQIIL 216
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
11-222 1.91e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.20  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPS---SGSIQLEQQILwnEQQQIPA-EA 86
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVC--RFKDIRDsEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPHLSVLDNVM-------FGLKKLPKAQRQAvaEQALQHVSmqhhLHSYPYTLSG----GEQQRVALA 155
Cdd:NF040905  78 LGIVIIHQELALIPYLSIAENIFlgnerakRGVIDWNETNRRA--RELLAKVG----LDESPDTLVTdigvGKQQLVEIA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDH----RLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQI-IL----------MHQG 220
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEedsaALLDLLLE-----LKAQGITSIIISHKLNEIRRVADSItVLrdgrtietldCRAD 226

                 ..
gi 514971686 221 EI 222
Cdd:NF040905 227 EV 228
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
10-226 1.81e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 58.59  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMlRLIAGLETPSSGSiQLEQQILWNEQQQipAEARNI 89
Cdd:NF000106  12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-RPWRF*TWCANRR--ALRRTI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GL-------VFQDYALFPHLSVLDNVMfglkKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:NF000106  88 G*hrpvr*gRRESFSGRENLYMIGR*L----DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEV-WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
11-247 6.38e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.83  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQIlwneqqqipAEARNI 89
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDM---------ADARHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYA---------LFPHLSVLDNV-----MFGLkklPKAQRQAVAEQALQHVSMqhhlhsYPYT------LSGGEQ 149
Cdd:NF033858  72 RAVCPRIAympqglgknLYPTLSVFENLdffgrLFGQ---DAAERRRRIDELLRATGL------APFAdrpagkLSGGMK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLD--HR-----LRDQIRQntieilkQTGTTTVIV-THDPEEALQIaDQIILMHQGE 221
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDplSRrqfweLIDRIRA-------ERPGMSVLVaTAYMEEAERF-DWLVAMDAGR 214
                        250       260
                 ....*....|....*....|....*...
gi 514971686 222 IIQIGTPKALYRQ--PATLFAAryFSAL 247
Cdd:NF033858 215 VLATGTPAELLARtgADTLEAA--FIAL 240
GguA NF040905
sugar ABC transporter ATP-binding protein;
144-170 2.57e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 2.57e-03
                         10        20
                 ....*....|....*....|....*..
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
12-354 1.02e-144

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 413.72  E-value: 1.02e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:COG3842    6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAQRVAQQLQ--TCFGAH---PISEALAhHQEPIRCCFRPHQVQVFSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3842  242 LPGTVLGDEGGgvRTGGRTlevPADAGLA-AGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 514971686 325 ILAQVSPAQTA-YQ--EQVYVRLDLQQCFFFAQ 354
Cdd:COG3842  321 LVVRVPNRAALpLEpgDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
12-356 1.40e-123

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 360.16  E-value: 1.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ--QQIPAEARNI 89
Cdd:COG3839    4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG------EILIGGRdvTDLPPKDRNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG3839   78 AMVFQSYALYPHMTVYENIAFPLKlrKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS-- 245
Cdd:COG3839  158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGsp 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 ALNEIPAQRVAQQLQTCFGAHPISEALA-HHQEPIRCCFRPHQVQVfSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3839  238 PMNLLPGTVEGGGVRLGGVRLPLPAALAaAAGGEVTLGIRPEHLRL-ADEGDGGLEATVEVVEPLGSETLVHVRLGGQEL 316
                        330       340       350
                 ....*....|....*....|....*....|....
gi 514971686 325 ILaqVSPAQTAYQ--EQVYVRLDLQQCFFFAQDS 356
Cdd:COG3839  317 VA--RVPGDTRLRpgDTVRLAFDPERLHLFDAET 348
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
12-345 1.50e-120

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 352.14  E-value: 1.50e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQ---QIPAEARN 88
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG------RIVLNGRDlftNLPPRERR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVMFGLKKLP--KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1118   77 VGFVFQHYALFPHMTVAENIAFGLRVRPpsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSA 246
Cdd:COG1118  157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 247 LNEIPAQRVAQQLQTcfGAHPISEALAHHQEPIRCCFRPHQVQVFSQPTT-GAIPATVLSSSFMGHAEQLRLQLDPET-- 323
Cdd:COG1118  237 VNVLRGRVIGGQLEA--DGLTLPVAEPLPDGPAVAGVRPHDIEVSREPEGeNTFPATVARVSELGPEVRVELKLEDGEgq 314
                        330       340
                 ....*....|....*....|....*..
gi 514971686 324 IILAQVSPAQTAYQ-----EQVYVRLD 345
Cdd:COG1118  315 PLEAEVTKEAWAELglapgDPVYLRPR 341
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
12-226 1.87e-100

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: 295.97  E-value: 1.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03259   77 VFQDYALFPHLTVAENIAFGLKlrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03259  157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
12-333 1.75e-97

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: 293.87  E-value: 1.75e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEqqqiPAEARNIGL 91
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL----PPQKRDYGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  250 IPAQRVA-QQLQTCFGAHPISEALAHHQEPIRCCFRPHQVQV-FSQPTTGAIPATVLSSSFMGHAEQLRLQLD--PETII 325
Cdd:TIGR03265 241 LPGTRGGgSRARVGGLTLACAPGLAQPGASVRLAVRPEDIRVsPAGNAANLLLARVEDMEFLGAFYRLRLRLEglPGQAL 320

                  ....*...
gi 514971686  326 LAQVSPAQ 333
Cdd:TIGR03265 321 VADVSASE 328
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
6-250 5.79e-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: 278.90  E-value: 5.79e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   6 AAQANVLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQ 81
Cdd:COG1116    2 SAAAPALELRGVSKRFPTGGGGVTAlddvSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-------P 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:COG1116   75 VTGPGPDRGVVFQEPALLPWLTVLDNVALGLElrGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQG-----EIIQIGTPKAlyRQ 234
Cdd:COG1116  155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPRP--RD 232
                        250
                 ....*....|....*.
gi 514971686 235 PATLFAARYFSALNEI 250
Cdd:COG1116  233 RELRTSPEFAALRAEI 248
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
12-243 7.51e-91

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: 272.19  E-value: 7.51e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03300   77 VFQNYALFPHLTVFENIAFGLrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:cd03300  157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-253 3.39e-88

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 270.67  E-value: 3.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQ 80
Cdd:PRK09452   4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----T 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 QIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK09452  80 HVPAENRHVNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEIL-KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQM-QNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
                        250
                 ....*....|....*.
gi 514971686 238 LFAARYFSALNEIPAQ 253
Cdd:PRK09452 239 LFVARFIGEINIFDAT 254
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
12-239 3.28e-84

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: 255.73  E-value: 3.28e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQERNVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03296   79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEirakvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLF 239
Cdd:cd03296  159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
12-225 1.35e-83

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: 253.55  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEAR 87
Cdd:cd03293    1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------PVTGPGP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03293   74 DRGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQ--GEIIQI 225
Cdd:cd03293  154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
11-237 1.49e-81

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 248.76  E-value: 1.49e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIG 90
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG1126   81 MVFQQFNLFPHLTVLENVTLAPikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1126  161 DEPTSALDPELVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
12-326 7.56e-81

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 251.16  E-value: 7.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHARDRKVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10851  79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 ALNEIPAQRVAQQLQTcfGAH--PISEALAhHQEPIRCCFRPHQVQVFSQPTTGA-IPATVLSSSFMGHAEQLRLQ---- 318
Cdd:PRK10851 239 EVNRLQGTIRGGQFHV--GAHrwPLGYTPA-YQGPVDLFLRPWEVDISRRTSLDSpLPVQVLEVSPKGHYWQLVVQplgw 315

                 ....*....
gi 514971686 319 -LDPETIIL 326
Cdd:PRK10851 316 yNEPLTVVM 324
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
8-356 1.87e-80

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 250.02  E-value: 1.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQipaea 86
Cdd:PRK11432   3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgEDVTHRSIQQ----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK11432  78 RDICMVFQSYALFPHMSLGENVGYGLKmlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYF 244
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 245 SALNEIPAQRVAQQLqTCFGAH---PISEALAHHQEPIRCCFRPHQVQvFSQPTTGAIPATVLSSSFMG---------HA 312
Cdd:PRK11432 238 GDANIFPATLSGDYV-DIYGYRlprPAAFAFNLPDGECTVGVRPEAIT-LSEQGEESQRCTIKHVAYMGpqyevtvdwHG 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 514971686 313 EQLRLQLDPEtiilaQVSPAQTayqEQVYVRLDLQQCFFFAQDS 356
Cdd:PRK11432 316 QELLLQVNAT-----QLQPDLG---EHYYLEIHPYGMFLLADAA 351
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
42-329 3.17e-80

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: 248.56  E-value: 3.17e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQ 119
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE----DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKmrKVPRAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  120 RQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVI 199
Cdd:TIGR01187  77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  200 VTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNEIPAQRVAQQ-LQTCFGAHPISEALAHH--- 275
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKsEQVVLAGVEGRRCDIYTdvp 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  276 ---QEPIRCCFRPHQVQVFSQP---TTGAIPATVLSSSFMGHAEQLRLQLDPETIILAQV 329
Cdd:TIGR01187 237 vekDQPLHVVLRPEKIVIEEEDeanSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSE 296
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
14-248 1.80e-78

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 240.86  E-value: 1.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVF 93
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ----DATRVHARDRKIGFVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   94 QDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR00968  79 QHYALFKHLTVRDNIAFGLEirKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686  172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
12-226 2.03e-77

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: 237.54  E-value: 2.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqqIPAEARNIGL 91
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03301   77 VFQNYALYPHMTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03301  157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
12-222 6.83e-77

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: 236.23  E-value: 6.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPAE 85
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKELAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARNIGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEAlQIADQIILMHQGEI 222
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
6-244 9.60e-77

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: 237.54  E-value: 9.60e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   6 AAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIP 83
Cdd:cd03294   19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaaMSRKELRE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 AEARNIGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:cd03294   99 LRRKKISMVFQSFALLPHRTVLENVAFGLevQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:cd03294  179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258

                 ...
gi 514971686 242 RYF 244
Cdd:cd03294  259 EFF 261
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
11-294 1.24e-75

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 238.58  E-value: 1.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIG 90
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11607  95 MMFQSYALFPHMTVEQNIAFGLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514971686 249 EIPAQRVAQQ-----LQTCFGAHPI---SEALAHHQEPIRCCFRPHQVQVFSQP 294
Cdd:PRK11607 255 VFEGVLKERQedglvIDSPGLVHPLkvdADASVVDNVPVHVALRPEKIMLCEEP 308
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
13-253 3.36e-74

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 234.12  E-value: 3.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSR----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIPAEAR 87
Cdd:NF040933   4 RVENVTKIFKKGkkevVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKlVASPGKIIVPPEDR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQ-RQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:NF040933  84 NIGMVFQNWALYPNMTVFDNIAFPLKikKVPKDEiEKKVKEVA-EILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYF 244
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242

                 ....*....
gi 514971686 245 SALNEIPAQ 253
Cdd:NF040933 243 GDINLLEGK 251
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
12-238 4.66e-74

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: 229.53  E-value: 4.66e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqIPAEARNIG 90
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQ--DYALFpHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1122   79 LVFQnpDDQLF-APTVEEDVAFGPEnlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 167 MDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:COG1122  158 LDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
9-223 7.57e-74

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 228.77  E-value: 7.57e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQi 82
Cdd:COG1136    2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSEREL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 pAEARN--IGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1136   81 -ARLRRrhIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPeEALQIADQIILMHQGEII 223
Cdd:COG1136  160 VNRPKLILADEPTGNLDSKTGEEV----LELLrelnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
12-234 1.93e-73

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 228.02  E-value: 1.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGL 91
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---RRRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG1131   78 VPQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 170 PFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG1131  158 PTSGLDpearRELWELLRE-----LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
13-274 5.08e-73

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 229.21  E-value: 5.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ--QQIPAEA--R 87
Cdd:COG1125    3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSG------RILIDGEdiRDLDPVElrR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:COG1125   77 RIGYVIQQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA-- 241
Cdd:COG1125  157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAdf 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 514971686 242 ----RYFSALNEIPAQRVAQ-QLQTCFGAHPISEALAH 274
Cdd:COG1125  237 vgadRGLRRLSLLRVEDLMLpEPPTVSPDASLREALSL 274
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
12-357 9.68e-73

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 230.50  E-value: 9.68e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEaRNIG 90
Cdd:PRK11650   4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PAD-RDIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11650  80 MVFQNYALYPHMSVRENMAYGLKirGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRqntIEILK---QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK11650 160 EPLSNLDAKLRVQMR---LEIQRlhrRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 --ALNEIPAQRVAQQLQTCFGAH---PISEALAHHQ-EPIRCCFRPHQVQVfsQPTTGAIPATVLSSSFMGhAEQL-RLQ 318
Cdd:PRK11650 237 spAMNLLDGRVSADGAAFELAGGialPLGGGYRQYAgRKLTLGIRPEHIAL--SSAEGGVPLTVDTVELLG-ADNLaHGR 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 514971686 319 LDPETIILAQVSPAQTAYQEQVYVRLDLQQCFFFAQDSQ 357
Cdd:PRK11650 314 WGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTG 352
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
16-331 1.41e-72

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: 229.99  E-value: 1.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  16 QLSKQFGSrFAVhQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVF 93
Cdd:COG4148    6 DFRLRRGG-FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflPPHRRRIGYVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:COG4148   84 QEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 174 LDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG4148  164 LDLARKAEI----LPYLerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAqRVAQQLQT------CFGAHPISEALAHHQ--EPIRCCFRPHQVQVFSQPTTG-----AIPATVLSSSFMGHAE-QL 315
Cdd:COG4148  240 LEA-TVAAHDPDygltrlALGGGRLWVPRLDLPpgTRVRVRIRARDVSLALEPPEGssilnILPGRVVEIEPADGGQvLV 318
                        330
                 ....*....|....*.
gi 514971686 316 RLQLDpETIILAQVSP 331
Cdd:COG4148  319 RLDLG-GQTLLARITR 333
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
7-231 1.67e-72

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: 225.63  E-value: 1.67e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   7 AQANVLTIRQLSKQFGSRfAVHQ-ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN----EQQQ 81
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDR-VVLDgVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPaeaRNIGLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1127   80 LR---RRIGMLFQGGALFDSLTVFENVAFPLRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 159 APKPQVLLMDEPFSNLD----HRLRDQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG1127  157 ALDPEILLYDEPTAGLDpitsAVIDELIR----ELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
12-250 9.77e-72

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: 223.72  E-value: 9.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAE-ARNI 89
Cdd:cd03295    1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE---DIREQDPVElRRKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03295   78 GYVIQQIGLFPHMTVEENIALvpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:cd03295  158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237

                 ....*
gi 514971686 246 ALNEI 250
Cdd:cd03295  238 ADRLL 242
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
12-294 1.04e-71

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 227.27  E-value: 1.04e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:NF040840   2 IRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK----DITNLPPEKRGIAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:NF040840  77 VYQNYMLFPHKTVFENIAFGLKlrKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 514971686 250 IPAQRVAQQLQTCFGAHPISEALAHHQE-PIRCCFRPHQVQVFSQP 294
Cdd:NF040840 237 IEGVAEKGGEGTILDTGNIKIELPEEKKgKVRIGIRPEDITISTEK 282
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
12-222 1.41e-71

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 222.40  E-value: 1.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGL 91
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03262  161 EPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
12-221 1.72e-70

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: 1.72e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGL 91
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGlkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03229   81 VFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03229  129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
19-261 8.43e-69

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


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 220.49  E-value: 8.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   19 KQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqQIPAEARN-----IGLVF 93
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMK---QSPVELREvrrkkIGMVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   94 QDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR01186  78 QQFALFPHMTILQNTSLGPEllGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNEI- 250
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSq 237
                         250
                  ....*....|...
gi 514971686  251 --PAQRVAQQLQT 261
Cdd:TIGR01186 238 vfDAERIAQRMNT 250
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
14-231 2.53e-67

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: 212.36  E-value: 2.53e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW--NEQQQIPAEaRNIGL 91
Cdd:cd03261    3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLR-RRMGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03261   82 LFQSGALFDSLTVFENVAFPLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQT-GTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03261  162 EPTAGLDPIASGVI-DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
12-248 2.84e-67

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: 212.20  E-value: 2.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqqIPAEARNIGL 91
Cdd:cd03299    1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03299   76 VPQNYALFPHMTVYKNIAYGLKKRkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:cd03299  156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
37-226 2.87e-67

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: 211.38  E-value: 2.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKK 114
Cdd:cd03297   23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTG 194
Cdd:cd03297  103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
                        170       180       190
                 ....*....|....*....|....*....|..
gi 514971686 195 TTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03297  183 IPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
5-246 2.52e-66

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: 218.23  E-value: 2.52e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQFGSRF-----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-E 78
Cdd:COG1123  254 AAAAEPLLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlS 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  79 QQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRV 152
Cdd:COG1123  334 RRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRlhgLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRV 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:COG1123  414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
                        250
                 ....*....|....
gi 514971686 233 RQPATLFAARYFSA 246
Cdd:COG1123  494 ANPQHPYTRALLAA 507
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
26-237 4.00e-66

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 214.20  E-value: 4.00e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPAEARNIGLVFQDYALFPHLS 103
Cdd:COG4175   42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDItkLSKKELRELRRKKMSMVFQHFALLPHRT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD----HR 177
Cdd:COG4175  122 VLENVAFGLEiqGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDplirRE 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 178 LRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG4175  202 MQDEL----LELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN 257
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
12-224 1.43e-64

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 206.25  E-value: 1.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqqQIPAEAR 87
Cdd:COG4525    4 LTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 niGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4525   79 --GVVFQKDALLPWLNVLDNVAFGLRlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILM--HQGEIIQ 224
Cdd:COG4525  157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
11-223 7.59e-64

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 202.98  E-value: 7.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ-------QQI 82
Cdd:COG2884    1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG------QVLVNGQdlsrlkrREI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 PAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:COG2884   75 PYLRRRIGVVFQDFRLLPDRTVYENVALPLRvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIrqntIEILK---QTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG2884  155 RPELLLADEPTGNLDPETSWEI----MELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
12-243 3.65e-63

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 201.52  E-value: 3.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSrFAVHqASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQ--QIPAEARNI 89
Cdd:COG3840    2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG------RILWNGQDltALPPAERPV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG3840   74 SMLFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQV-EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:COG3840  153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
11-231 6.99e-63

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: 201.43  E-value: 6.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAE--ARN 88
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA----SLSRRelARR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:COG1120   77 IAYVPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAV-EEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 162 PQVLLMDEPFSNLD--HRLR--DQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG1120  156 PPLLLLDEPTSHLDlaHQLEvlELLR----RLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-221 1.47e-62

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: 199.23  E-value: 1.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGS--RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGL 91
Cdd:cd03225    2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQ--DYALFpHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03225   80 VFQnpDDQFF-GPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03225  159 DEPTAGLDPAGRRELLE-LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
9-241 1.40e-61

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 201.80  E-value: 1.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVlTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEqqqIPAEARN 88
Cdd:PRK11000   2 ASV-TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-ND---VPPAERG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11000  77 VGMVFQSYALYPHLSVAENMSFGLKlaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 167 MDEPFSNLDHRLRDQIRqntIEIL---KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:PRK11000 157 LDEPLSNLDAALRVQMR---IEISrlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
12-230 2.18e-61

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 196.16  E-value: 2.18e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP---SSGSIQLEQQILwneqQQIPAEARN 88
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL----TALPAEQRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVMFGL-KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4136   78 IGILFQDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiadqiilmhQGEIIQIGTPKA 230
Cdd:COG4136  158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
11-234 2.31e-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: 194.69  E-value: 2.31e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEAR-NI 89
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE----DVRKEPREARrQI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNV-MFG-LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4555   77 GVLPDERGLYDRLTVRENIrYFAeLYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 168 DEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG4555  157 DEPTNGLDvmarRLLREILRA-----LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
11-231 2.86e-60

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 194.51  E-value: 2.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW-NEQQQIPAEARN 88
Cdd:COG3638    2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:COG3638   82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG3638  161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
5-230 9.22e-59

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: 190.34  E-value: 9.22e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQFGSRFAV----HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNE 78
Cdd:COG4181    2 SSSSAPIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  79 QQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG4181   82 DARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKA 230
Cdd:COG4181  162 ATEPAILFADEPTGNLDAATGEQI----IDLLfelnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
11-235 1.85e-56

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: 184.32  E-value: 1.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEA 86
Cdd:cd03258    1 MIELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL---TLLSGKEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RN----IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:cd03258   78 RKarrrIGMIFQHFNLLSSRTVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:cd03258  158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
12-222 3.17e-56

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: 181.44  E-value: 3.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPaeaRNIGL 91
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---RRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03230   78 LPEEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 172 SNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03230  124 SGLDPESRREFW-ELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
11-241 6.04e-56

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: 190.88  E-value: 6.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPS---SGSIQLEQQILWNEQQQIPAe 85
Cdd:COG1123    4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 aRNIGLVFQD--YALFPhLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:COG1123   83 -RRIGMVFQDpmTQLNP-VTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
39-331 7.58e-56

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: 186.47  E-value: 7.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLP 116
Cdd:TIGR02142  25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRAR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  117 KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTT 196
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIP 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  197 TVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY-FSALNEIpaqRVAQ--------QLQTCFGAHP 267
Cdd:TIGR02142 185 ILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREdQGSLIEG---VVAEhdqhygltALRLGGGHLW 261
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  268 ISEALAHHQEPIRCCFRPHQVQVFSQPTTG-----AIPATVLSSSfmgHAE--QLRLQLDPE-TIILAQVSP 331
Cdd:TIGR02142 262 VPENLGPTGARLRLRVPARDVSLALQKPEAtsirnILPARVVEIE---DSDigRVGVVLESGgKTLWARITR 330
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
33-250 1.15e-55

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: 182.28  E-value: 1.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   33 SAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneQQQIPAEARNIglVFQDYALFPHLSVLDNVMFG- 111
Cdd:TIGR01184   7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----QITEPGPDRMV--VFQNYSLLPWLTVRENIALAv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  112 ---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:TIGR01184  80 drvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686  189 ILKQTGTTTVIVTHDPEEALQIADQIILM------HQGEIIQIGTPKALYRQpATLFAARYFSALNEI 250
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPFPRPRDRL-EVVEDPSYYDLRNEA 226
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
11-226 2.85e-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: 181.16  E-value: 2.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:cd03257    1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RN-IGLVFQDY--ALFPHLSVLDNVMFGLKKL----PKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:cd03257   81 RKeIQMVFQDPmsSLNPRMTIGEQIAEPLRIHgklsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQI----LDLLKklqeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
12-231 3.78e-55

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: 180.84  E-value: 3.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:cd03260   81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlhgIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03260  160 PEVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
12-224 1.25e-54

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


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 179.94  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqILWNEQQQIPAEAR 87
Cdd:NF040729   2 LKIQNISKTFINNKKENEVlkdiSFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEI-----LVNGNEVTKPGPDR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 niGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:NF040729  77 --GFVFQNYALFPWMTVKENIEYPMKqqKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDHRLRdQIRQNTIE-ILKQTGTTTVIVTHDPEEALQIADQIILM--HQGEIIQ 224
Cdd:NF040729 155 LMDEPLGAVDFQMR-QILQEELEsIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
12-237 2.96e-54

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: 179.23  E-value: 2.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR 87
Cdd:COG1124    2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDY--ALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:COG1124   80 RVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1124  160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
15-260 2.47e-53

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 176.44  E-value: 2.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  15 RQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ 94
Cdd:PRK09493   5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  95 DYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:PRK09493  85 QFYLFPHLTALENVMFGplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPatlfaaryfsalneiP 251
Cdd:PRK09493 165 SALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP---------------P 228

                 ....*....
gi 514971686 252 AQRVAQQLQ 260
Cdd:PRK09493 229 SQRLQEFLQ 237
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
5-237 4.40e-53

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 176.53  E-value: 4.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQ---Q 80
Cdd:COG4598    2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgEEIRLKPDrdgE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 QIPAEAR-------NIGLVFQDYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQ 150
Cdd:COG4598   82 LVPADRRqlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:COG4598  162 RAAIARALAMEPEVMLFDEPTSALDPELVGEvlkvMRD-----LAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
                        250
                 ....*....|.
gi 514971686 227 TPKALYRQPAT 237
Cdd:COG4598  237 PPAEVFGNPKS 247
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
12-231 5.66e-53

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: 175.00  E-value: 5.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRF--AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPaeaRNI 89
Cdd:cd03263    1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---QSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03263   78 GYCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIrQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03263  158 DEPTSGLDPASRRAI-WDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
14-215 5.72e-53

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: 174.34  E-value: 5.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARN----- 88
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ---ETPPLNSKKASKfrrek 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   89 IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR03608  78 LGYLFQNFALIENETVEENLDLGLKykKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 514971686  167 MDEPFSNLDHRLRDQIrqntIEILKQ---TGTTTVIVTHDPEEAlQIADQII 215
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEV----LDLLLElndEGKTIIIVTHDPEVA-KQADRVI 204
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
26-238 5.75e-53

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: 176.49  E-value: 5.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR-NIGLVFQ--DYALFpHL 102
Cdd:TIGR04521  20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRkKVGLVFQfpEHQLF-EE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  103 SVLDNVMFGLK--KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:TIGR04521  99 TVYKDIAFGPKnlGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686  180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
12-228 7.09e-53

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: 174.93  E-value: 7.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILwneqqQIPAEARN-- 88
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDIT-----GLPPHEIArl 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 -IGLVFQDYALFPHLSVLDNVM----------FGLKKLPKAQRQAV--AEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:cd03219   76 gIGRTFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:cd03219  156 RALATDPKLLLLDEPAAGLNPEETEELA-ELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
12-235 1.46e-52

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 174.94  E-value: 1.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQI-----LWNEQQQIPAE 85
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIdtarsLSQQKGLIRQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARNIGLVFQDYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PRK11264  84 RQHVGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
12-222 2.29e-52

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 172.69  E-value: 2.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNI 89
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK----PLSAMPPPEwrRQV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-LSGGEQQRVALARALAPKPQVLLMD 168
Cdd:COG4619   77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:COG4619  156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
14-245 7.89e-52

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 172.50  E-value: 7.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQiLWNEQQQIPAEA-----RN 88
Cdd:COG4161    5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH-QFDFSQKPSEKAirllrQK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVM---FGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4161   84 VGMVFQQYNLWPHLTVMENLIeapCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTpKALYRQPATLFAARYFS 245
Cdd:COG4161  164 LFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
12-268 1.66e-51

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 174.88  E-value: 1.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEA 86
Cdd:COG1135    2 IELENLSKTFPTKGGPVTAlddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:COG1135   82 RKIGMIFQHFNLLSSRTVAENVALPLEiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDhrlrdqiRQNTIEIL-------KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1135  162 LLCDEATSALD-------PETTRSILdllkdinRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
                        250       260       270
                 ....*....|....*....|....*....|..
gi 514971686 238 LFAARYF-SALNEIPAQRVAQQLQTCFGAHPI 268
Cdd:COG1135  235 ELTRRFLpTVLNDELPEELLARLREAAGGGRL 266
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
12-220 1.99e-51

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 172.19  E-value: 1.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQIPAEARniGL 91
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAER--GV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK11248  75 VFQNEGLLPWRNVQDNVAFGLQlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQG 220
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
12-231 2.79e-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: 171.21  E-value: 2.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNI 89
Cdd:cd03256    1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgTDINKLKGKALRQLRRQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03256  160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
7-229 6.85e-51

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 170.27  E-value: 6.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEA 86
Cdd:COG1121    2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYAL---FPhLSVLDNVMFGL-------KKLPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:COG1121   75 RRIGYVPQRAEVdwdFP-ITVRDVVLMGRygrrglfRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVLLAR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGeIIQIGTPK 229
Cdd:COG1121  153 ALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE 223
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
11-236 1.07e-50

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: 170.22  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEARN- 88
Cdd:COG0411    4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDI-----TGLPPHRIAr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLV--FQDYALFPHLSVLDNVMFG------------LKKLPKAQRQ-----AVAEQALQHVSMQHHLHSYPYTLSGGEQ 149
Cdd:COG0411   79 LGIArtFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG0411  159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238

                 ....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG0411  239 EVRADPR 245
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-235 1.41e-50

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 169.83  E-value: 1.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLR-------LIAGLETpsSGSIQLEQQ 73
Cdd:COG1117    1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  74 ILWNEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSG 146
Cdd:COG1117   79 DIYDPDVDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRlhgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTgTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:COG1117  158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE-----LKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
                        250
                 ....*....|...
gi 514971686 223 IQIGTPKALYRQP 235
Cdd:COG1117  232 VEFGPTEQIFTNP 244
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
14-245 4.28e-50

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 168.27  E-value: 4.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQ----QIPAEARNI 89
Cdd:PRK11124   5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkAIRELRRNV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLKK---LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11124  85 GMVFQQYNLWPHLTVQQNLIEAPCRvlgLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 167 MDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTpKALYRQPATLFAARYFS 245
Cdd:PRK11124 165 FDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
11-221 4.45e-50

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: 167.04  E-value: 4.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARN 88
Cdd:TIGR02673   1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgEDVNRLRGRQLPLLRRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   89 IGLVFQDYALFPHLSVLDNVMFGL----KKLPKAQRQAvaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:TIGR02673  81 IGVVFQDFRLLPDRTVYENVALPLevrgKKEREIQRRV--GAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686  165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILD-LLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
13-226 1.59e-49

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: 164.53  E-value: 1.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAEARniglv 92
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----SLSPKEL----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 fqdyalfphlsvldnvmfglkklpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd03214   72 -------------------------ARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 173 NLDhrLRDQIRqnTIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03214  127 HLD--IAHQIE--LLELLRrlarERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
12-222 2.93e-49

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 166.39  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqqqipAEARN-IG 90
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL--------AEAREdTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLKklpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:PRK11247  85 LMFQDARLLPWKKVIDNVGLGLK----GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514971686 171 FSNLDHRLRDQIrQNTIEIL-KQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK11247 161 LGALDALTRIEM-QDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
12-248 2.93e-49

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 170.60  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE----QQILWNEQQQIpaEAR 87
Cdd:PRK10070  29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREV--RRK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266

                 ...
gi 514971686 246 ALN 248
Cdd:PRK10070 267 GVD 269
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
11-232 5.33e-49

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: 165.16  E-value: 5.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGS-RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR-N 88
Cdd:TIGR02315   1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRrR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   89 IGLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQaVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686  158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
11-245 1.24e-48

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: 164.39  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLE--TPS---SGSIQLEQQILWNEQQQIPAE 85
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGvriEGKVLFDGQDIYDKKIDVVEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   86 ARNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:TIGR00972  81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRlhgIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  159 APKPQVLLMDEPFSNLdhrlrDQIRQNTIEILKQ---TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:TIGR00972 160 AVEPEVLLLDEPTSAL-----DPIATGKIEELIQelkKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234
                         250
                  ....*....|
gi 514971686  236 ATLFAARYFS 245
Cdd:TIGR00972 235 KEKRTEDYIS 244
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
27-172 1.43e-48

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 160.89  E-value: 1.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneQQQIPAEARNIGLVFQDYALFPHLSVLD 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT--DDERKSLRKEIGYVFQDPQLFPRLTVRE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  107 NVMFG--LKKLPKAQRQAVAEQALQHVSMQH----HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:pfam00005  79 NLRLGllLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
14-260 4.28e-48

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: 163.76  E-value: 4.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   14 IRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqIPAEARNIGL 91
Cdd:TIGR04520   3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKVGM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   92 VFQDyalfPH-----LSVLDNVMFGL--KKLPKAQ-RQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:TIGR04520  82 VFQN----PDnqfvgATVEDDVAFGLenLGVPREEmRKRVDE-ALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  164 VLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQPATLFAAR 242
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLE-TIRKLNKEEGITVIsITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKEIG 234
                         250
                  ....*....|....*....
gi 514971686  243 YfsalnEIP-AQRVAQQLQ 260
Cdd:TIGR04520 235 L-----DVPfITELAKALK 248
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
13-221 7.10e-48

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: 159.33  E-value: 7.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneQQQIPAEARNIGLV 92
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 FQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd00267   79 PQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 173 NLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd00267  110 GLDPASRERLL-ELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
36-226 3.59e-47

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: 159.58  E-value: 3.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK-- 113
Cdd:cd03298   23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSpg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 -KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQ 192
Cdd:cd03298   99 lKLTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
                        170       180       190
                 ....*....|....*....|....*....|....
gi 514971686 193 TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03298  178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
11-219 2.75e-46

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: 156.87  E-value: 2.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARNIG 90
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE---PIRDAREDYRRRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:COG4133   79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 171 FSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALqiADQIILMHQ 219
Cdd:COG4133  159 FTALDAAGVALLAE-LIAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
15-205 7.47e-46

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: 156.03  E-value: 7.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  15 RQLSKQFGSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEARNIGLV 92
Cdd:cd03292    4 INVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 FQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03292   84 FQDFRLLPDRNVYENVAFALEvtgVPPREIRKRVPA-ALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPE 205
Cdd:cd03292  163 PTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKE 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
12-234 8.28e-46

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 166.55  E-value: 8.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--R 87
Cdd:COG2274  474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPASlrR 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFpHLSVLDNVMFGLKKLPKAQRQAVAEQA--LQHVS-----MQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:COG2274  550 QIGVVLQDVFLF-SGTIRENITLGDPDATDEEIIEAARLAglHDFIEalpmgYDTVVGEGGSNLSGGQRQRLAIARALLR 628
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG2274  629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLAR 699
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
8-234 8.64e-46

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 158.25  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQ--QIp 83
Cdd:PRK13635   2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETvwDV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 aeARNIGLVFQDY-ALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:PRK13635  80 --RRQVGMVFQNPdNQFVGATVQDDVAFGLENigVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLE-TVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
12-228 1.01e-45

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 157.20  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNI 89
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaaWSPWEL----ARRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYAL-FPhLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLH-SYPyTLSGGEQQRVALARALA------ 159
Cdd:COG4559   78 AVLPQHSSLaFP-FTVEEVVALGRapHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepv 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 160 -PKPQVLLMDEPFSNLDhrLRDQirQNTIEILKQ---TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG4559  156 dGGPRWLFLDEPTSALD--LAHQ--HAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
39-226 1.24e-45

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 159.65  E-value: 1.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLP 116
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVaeqaLQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD-----------HRLRDQIRqn 185
Cdd:PRK11144 106 VAQFDKI----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellpylERLAREIN-- 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 186 tIEILkqtgtttvIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11144 180 -IPIL--------YVSHSLDEILRLADRVVVLEQGKVKAFG 211
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
12-236 3.61e-45

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: 155.01  E-value: 3.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR-NIG 90
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKRARlGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03218   79 YLPQEASIFRKLTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:cd03218  159 EPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
11-222 4.04e-45

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: 154.41  E-value: 4.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQIPAE 85
Cdd:TIGR02982   1 VISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvLGQELHGASKKQLVQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPK---AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:TIGR02982  81 RRRIGYIFQAHNLLGFLTARQNVQMALELQPNlsyQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686  163 QVLLMDEPFSNLDhrlrDQIRQNTIEILKQ----TGTTTVIVTHDPeEALQIADQIILMHQGEI 222
Cdd:TIGR02982 161 KLVLADEPTAALD----SKSGRDVVELMQKlakeQGCTILMVTHDN-RILDVADRILQMEDGKL 219
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
11-229 9.29e-45

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 153.97  E-value: 9.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqQQIPAEAR-NI 89
Cdd:TIGR04406   1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH--LPMHERARlGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   90 GLVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR04406  79 GYLPQEASIFRKLTVEENIMAVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686  167 MDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDI-KKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
11-236 1.97e-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: 155.60  E-value: 1.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSR----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP---SSGSIQLEQQILWN--EQQQ 81
Cdd:COG0444    1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPAEARNIGLVFQD-Y-ALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM---QHHLHSYPYTLSGGEQQRVA 153
Cdd:COG0444   81 RKIRGREIQMIFQDpMtSLNPVMTVGDQIAEPLRihgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG0444  161 IARALALEPKLLIADEPTTALDVTIQAQI----LNLLKdlqrELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236

                 ....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG0444  237 ELFENPR 243
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
12-231 2.58e-44

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: 152.20  E-value: 2.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEARN-- 88
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDI-----TGLPPHERAra 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 -IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQH----VSMQHHLhsyPYTLSGGEQQRVALARALAPKPQ 163
Cdd:cd03224   76 gIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELfprlKERRKQL---AGTLSGGEQQMLAIARALMSRPK 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 164 VLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03224  153 LLLLDEPSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
11-235 3.01e-44

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 152.88  E-value: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQIlwnEQQQIPAEARN- 88
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDI---THLPMHKRARLg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNVM--FGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1137   80 IGYLPQEASIFRKLTVEDNILavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 167 MDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:COG1137  160 LDEPFAGVDpiavADIQKIIRH-----LKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
21-217 1.29e-42

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: 147.68  E-value: 1.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  21 FGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqipaeaRNIGLVFQDYAL-- 98
Cdd:cd03235    9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-------KRIGYVPQRRSIdr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  99 -FPhLSVLDNVMFGL-------KKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:cd03235   82 dFP-ISVRDVVLMGLyghkglfRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 514971686 171 FSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILM 217
Cdd:cd03235  160 FAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
5-234 1.61e-41

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 152.99  E-value: 1.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIP 83
Cdd:COG4988  330 PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV----DLSDLD 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 AEA--RNIGLVFQDYALFpHLSVLDNVMFGlkkLPKAQRQAVaEQALQHVSMQHHLHSYP-----------YTLSGGEQQ 150
Cdd:COG4988  406 PASwrRQIAWVPQNPYLF-AGTIRENLRLG---RPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQ 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKA 230
Cdd:COG4988  481 RLALARALLRDAPLLLLDEPTAHLDAETEAEI-LQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEE 557

                 ....
gi 514971686 231 LYRQ 234
Cdd:COG4988  558 LLAK 561
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
9-236 1.96e-41

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: 145.12  E-value: 1.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEAR 87
Cdd:COG0410    1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDI-----TGLPPHRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 N---IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRqavAEQALQHV--------SMQHHLHSypyTLSGGEQQRVALAR 156
Cdd:COG0410   76 ArlgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAE---VRADLERVyelfprlkERRRQRAG---TLSGGEQQMLAIGR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:COG0410  150 ALMSRPKLLLLDEPSLGLAPLIVEEIFE-IIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
12-235 5.81e-41

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 144.98  E-value: 5.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSR---------FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqQQI 82
Cdd:COG4167    5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--GDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 PAEARNIGLVFQD--YALFPHLSV---LDnvmFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVA 153
Cdd:COG4167   83 KYRCKHIRMIFQDpnTSLNPRLNIgqiLE---EPLRlntDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYR 233
Cdd:COG4167  160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239

                 ..
gi 514971686 234 QP 235
Cdd:COG4167  240 NP 241
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
28-222 1.23e-40

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: 142.88  E-value: 1.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   28 HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNI--GLVFQDYALFPHLSVL 105
Cdd:TIGR02211  22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKklGFIYQFHHLLPDFTAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  106 DNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIR 183
Cdd:TIGR02211 102 ENVAMPLliGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 514971686  184 QNTIEILKQTGTTTVIVTHDPEEALQIaDQIILMHQGEI 222
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
31-226 2.23e-40

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: 141.92  E-value: 2.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMF 110
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  111 GLK---KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:TIGR01277  94 GLHpglKLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 514971686  188 EILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
8-237 4.54e-40

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 142.42  E-value: 4.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-----------EQQILW 76
Cdd:PRK10619   2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  77 NEQQQIPAEARNIGLVFQDYALFPHLSVLDNVM---FGLKKLPKAQRQAVAEQALQHVSMQHHLH-SYPYTLSGGEQQRV 152
Cdd:PRK10619  82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240

                 ....*
gi 514971686 233 RQPAT 237
Cdd:PRK10619 241 GNPQS 245
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
12-221 9.39e-40

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: 138.67  E-value: 9.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSR--FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQ--QQIPAEA- 86
Cdd:cd03228    1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI------LIDGVdlRDLDLESl 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 -RNIGLVFQDYALFpHLSVLDNVmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03228   75 rKNIAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGE 221
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-231 1.09e-39

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 140.49  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  24 RFAVHqaswsAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLS 103
Cdd:PRK10771  17 RFDLT-----VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTPPSRRPVSMLFQENNLFSHLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLK---KLPKAQRQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK10771  88 VAQNIGLGLNpglKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
9-223 2.02e-39

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 146.32  E-value: 2.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEA 86
Cdd:COG1129    2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GEPVRFrsPRDA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RN--IGLVFQDYALFPHLSVLDNVMFG--LKKLP----KAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1129   77 QAagIAIIHQELNLVPNLSVAENIFLGrePRRGGlidwRAMRRR-ARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDH----RLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG1129  156 SRDARVLILDEPTASLTEreveRLFRIIRR-----LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
13-265 2.49e-39

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 142.63  E-value: 2.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSRF----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEAR 87
Cdd:PRK11153   3 ELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgQDLTALSEKELRKARR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK11153  83 QIGMIFQHFNLLSSRTVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
                        250       260
                 ....*....|....*....|....*
gi 514971686 246 AL--NEIPAQ---RVAQQLQTCFGA 265
Cdd:PRK11153 243 STlhLDLPEDylaRLQAEPTTGSGP 267
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
12-238 4.49e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 140.93  E-value: 4.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSK--QFGSRF---AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNE--QQQIPA 84
Cdd:PRK13634   3 ITFQKVEHryQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkkNKKLKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 EARNIGLVFQ--DYALFPHlSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHH-LHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK13634  83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
31-223 6.44e-39

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: 137.77  E-value: 6.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQQQIPAE-ARNIGLVFQD--YALFPHlSVLDN 107
Cdd:cd03226   20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI------LLNGKPIKAKErRKSIGYVMQDvdYQLFTD-SVREE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLKKLPKAQRQAvaEQALQ--HVSMQHHLHsyPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQN 185
Cdd:cd03226   93 LLLGLKELDAGNEQA--ETVLKdlDLYALKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV-GE 167
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514971686 186 TIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03226  168 LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
10-207 1.08e-38

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 137.99  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSrfAVHQAS------WSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQ 81
Cdd:PRK10584   5 NIVEVHHLKKSVGQ--GEHELSiltgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPAEARNIGLVFQDYALFPHLSVLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK10584  83 AKLRAKHVGFVFQSFMLIPTLNALENVELPalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEA 207
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
5-236 1.49e-38

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: 144.91  E-value: 1.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQI 82
Cdd:COG4987  327 PAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL----RDL 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 PAEA--RNIGLVFQDYALFpHLSVLDNVMFGLkklPKAQRQAVaEQALQHVSMQHHLHSYPY-----------TLSGGEQ 149
Cdd:COG4987  403 DEDDlrRRIAVVPQRPHLF-DTTLRENLRLAR---PDATDEEL-WAALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG4987  478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHE 554

                 ....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG4987  555 ELLAQNG 561
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
6-236 1.66e-38

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 140.25  E-value: 1.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   6 AAQANVLTIRQLSKQF---GSRF--------AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQ 73
Cdd:COG4608    2 AMAEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  74 ILWNEQQQIPAEARNIGLVFQD-YA-LFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGG 147
Cdd:COG4608   82 ITGLSGRELRPLRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRihgLASKAERRERVAELLELVGLrPEHADRYPHEFSGG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 148 EQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQT-GTTTVIVTHDpeeaL----QIADQIILMHQGEI 222
Cdd:COG4608  162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQV-LNLLEDLQDElGLTYLFISHD----LsvvrHISDRVAVMYLGKI 236
                        250
                 ....*....|....
gi 514971686 223 IQIGTPKALYRQPA 236
Cdd:COG4608  237 VEIAPRDELYARPL 250
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
22-234 1.88e-38

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 144.92  E-value: 1.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQ--QQIPAEA--RNIGLVFQDYA 97
Cdd:COG1132  351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI------LIDGVdiRDLTLESlrRQIGVVPQDTF 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  98 LFpHLSVLDNVMFGLkklPKAQRQAVaEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1132  425 LF-SGTIRENIRYGR---PDATDEEV-EEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG1132  500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
11-228 2.20e-38

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 137.98  E-value: 2.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARN 88
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadWSPAEL----ARR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYAL-FPhLSVLDNVMFGLKKLP--KAQRQAVAEQALQHVSMQHHLH-SYPyTLSGGEQQRVALARALA----- 159
Cdd:PRK13548  78 RAVLPQHSSLsFP-FTVEEVVAMGRAPHGlsRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLAqlwep 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 160 -PKPQVLLMDEPFSNLDhrLRDQirQNTIEILKQ----TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK13548 156 dGPPRWLLLDEPTSALD--LAHQ--HHVLRLARQlaheRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
12-226 3.72e-38

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: 135.78  E-value: 3.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGqIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQI--PAEARN- 88
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG------TIRIDGQDVLkqPQKLRRr 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQDYALFPHLSVLDNV--MFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:cd03264   74 IGYLPQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 167 MDEPFSNLDHRLRDQIRqntiEILKQTGTTTVIV--THDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03264  154 VDEPTAGLDPEERIRFR----NLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
12-226 4.21e-38

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: 135.96  E-value: 4.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA- 86
Cdd:cd03266    2 ITADALTKRFRDVKKTVQAvdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF----DVVKEPAEAr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:cd03266   78 RRLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 165 LLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03266  158 LLLDEPTTGLDvmatRALREFIRQ-----LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
17-231 4.31e-38

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: 135.96  E-value: 4.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSiqleqqiLWNEQQQIPAEA----RNIGLV 92
Cdd:cd03265    6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-------ATVAGHDVVREPrevrRRIGIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 FQDYALFPHLSVLDNV-MFG-LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:cd03265   79 FQDLSVDDELTGWENLyIHArLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 171 FSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03265  159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
23-229 5.18e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 137.43  E-value: 5.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQ--DYAlFP 100
Cdd:PRK13632  21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI--SKENLKEIRKKIGIIFQnpDNQ-FI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK13632  98 GATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514971686 179 RDQIRQNTIEiLKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPK 229
Cdd:PRK13632 178 KREIKKIMVD-LRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
11-258 5.53e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 137.93  E-value: 5.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQIPAEARNIG 90
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG------EVLWDGEPLDPEDRRRIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 lvfqdY-----ALFPHLSVLDNVMF--GLKKLPKAQrqavAEQALQHVSMQHHLHSYPY----TLSGGEQQRVALARALA 159
Cdd:COG4152   75 -----YlpeerGLYPKMKVGEQLVYlaRLKGLSKAE----AKRRADEWLERLGLGDRANkkveELSKGNQQKVQLIAALL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ- 234
Cdd:COG4152  146 HDPELLILDEPFSGLDpvnvELLKDVIRE-----LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQf 220
                        250       260
                 ....*....|....*....|....*..
gi 514971686 235 PATLFAARY---FSALNEIPAQRVAQQ 258
Cdd:COG4152  221 GRNTLRLEAdgdAGWLRALPGVTVVEE 247
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
10-245 1.40e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 135.74  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQiPA 84
Cdd:PRK14267   3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVD-PI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 EAR-NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQ--AVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK14267  82 EVRrEVGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
                        250
                 ....*....|
gi 514971686 236 ATLFAARYFS 245
Cdd:PRK14267 240 EHELTEKYVT 249
cbiO PRK13640
energy-coupling factor transporter ATPase;
10-238 1.43e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 136.47  E-value: 1.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGS--------IQLEQQILWNEQ 79
Cdd:PRK13640   4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  80 QQIpaearniGLVFQDY-ALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK13640  84 EKV-------GIVFQNPdNQFVGATVGDDVAFGLenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235

                 ..
gi 514971686 237 TL 238
Cdd:PRK13640 236 ML 237
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
12-223 1.03e-36

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: 131.96  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRRIGA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNvmFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03268   77 LIEAPGFYPNLTAREN--LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 172 SNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03268  155 NGLDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
11-230 4.48e-36

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: 131.75  E-value: 4.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-SIQL--EQQILWNeqqqIPAEAR 87
Cdd:COG1119    3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgERRGGED----VWELRK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLV---FQDYaLFPHLSVLDNVMFGL-------KKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:COG1119   79 RIGLVspaLQLR-FPRDETVLDVVLSGFfdsiglyREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEIIQIGtPKA 230
Cdd:COG1119  157 LVKDPELLILDEPTAGLDLGARELLLA-LLDKLAAEGAPTLVlVTHHVEEIPPGITHVLLLKDGRVVAAG-PKE 228
cbiO PRK13650
energy-coupling factor transporter ATPase;
9-249 5.68e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 132.16  E-value: 5.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVLTIRQLSKQFGS---RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL-----WNEQQ 80
Cdd:PRK13650   2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvWDIRH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 QIpaearniGLVFQDY-ALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:PRK13650  82 KI-------GMVFQNPdNQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGND 233
                        250       260
                 ....*....|....*....|
gi 514971686 238 L--------FAARYFSALNE 249
Cdd:PRK13650 234 LlqlgldipFTTSLVQSLRQ 253
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
11-214 8.95e-36

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 130.32  E-value: 8.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFG----SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:PRK11629   5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RN--IGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PRK11629  85 RNqkLGFIYQFHHLLPDFTALENVAMPLliGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpeeaLQIADQI 214
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
12-226 1.76e-35

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: 128.94  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQIPAEARNIGL 91
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG------EVLFDGKPLDIAARNRIGY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03269   75 LPEERGLYPKMKVIDQLVYlaQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03269  155 PFSGLDpvnvELLKDVIRE-----LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
8-235 1.78e-35

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 130.66  E-value: 1.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilWNEQQQIPAEAR 87
Cdd:PRK11831   4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-------LFDGENIPAMSR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 N--------IGLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK11831  77 SrlytvrkrMSMLFQSGALFTDMNVFDNVAYPLRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNldhrlRDQIRQNTI-----EILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK11831 157 AIALEPDLIMFDEPFVG-----QDPITMGVLvklisELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231

                 ....
gi 514971686 232 YRQP 235
Cdd:PRK11831 232 QANP 235
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
12-223 9.01e-35

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: 125.62  E-value: 9.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEARN- 88
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEVSFasPRDARRa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 -IGLVFQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03216   76 gIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03216  107 DEPTAALTpaevERLFKVIRR-----LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
26-223 1.38e-34

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: 126.94  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQI-PAEAR-NIGLVFQDYALFpHLS 103
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLdPADLRrNIGYVPQDVTLF-YGT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLkklPKAQRQAV---AEQALQHVSMQHHLHSYPY-------TLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:cd03245   94 LRDNITLGA---PLADDERIlraAELAGVTDFVNKHPNGLDLqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514971686 174 LDHRLRDQIRQNtieiLKQT--GTTTVIVTHDPeEALQIADQIILMHQGEII 223
Cdd:cd03245  171 MDMNSEERLKER----LRQLlgDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
26-241 1.81e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 128.27  E-value: 1.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALF-Phl 102
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQnpDDQLFaP-- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK13639  95 TVEEDVAFGPLnlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
9-223 1.90e-34

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 132.46  E-value: 1.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWN-EQQQI--PAE 85
Cdd:COG3845    3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG------EILIDgKPVRIrsPRD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARN--IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQ-RQAVAEQALQHVSMQHHL----HSYPYTLSGGEQQRVALARAL 158
Cdd:COG3845   77 AIAlgIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRlDRKAARARIRELSERYGLdvdpDAKVEDLSVGEQQRVEILKAL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNL-----DHrLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG3845  157 YRGARILILDEPTAVLtpqeaDE-LFEILRR-----LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
10-232 2.29e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 127.56  E-value: 2.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGS--RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR 87
Cdd:PRK13648   6 SIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLRK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQD-YALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK13648  84 HIGIVFQNpDNQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 165 LLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13648 164 IILDEATSMLDPDARQNL-LDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
cbiO PRK13637
energy-coupling factor transporter ATPase;
26-238 2.54e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 127.86  E-value: 2.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALFPHlS 103
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-T 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLKKL----PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:PRK13637 101 IEKDIAFGPINLglseEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
11-234 4.00e-34

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: 131.85  E-value: 4.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQF-----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE 85
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   86 ARN-----IGLVFQDYALFPHLSVLDNVM--FGLKkLPK--AQRQAVaeQALQHVSMQHH-----LHSYPYTLSGGEQQR 151
Cdd:TIGR03269 359 GRGrakryIGILHQEYDLYPHRTVLDNLTeaIGLE-LPDelARMKAV--ITLKMVGFDEEkaeeiLDKYPDELSEGERHR 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  152 VALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515

                  ...
gi 514971686  232 YRQ 234
Cdd:TIGR03269 516 VEE 518
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
10-243 4.05e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 126.57  E-value: 4.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWneQQQIPA 84
Cdd:PRK14247   2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 EARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQR--QAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK14247  80 LRRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237

                 ....*..
gi 514971686 237 TLFAARY 243
Cdd:PRK14247 238 HELTEKY 244
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
10-224 4.31e-34

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 126.73  E-value: 4.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQF---------GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQ 79
Cdd:PRK10419   2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  80 QQIPAEARNIGLVFQDY--ALFPHLSV---LDNVMFGLKKLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVA 153
Cdd:PRK10419  82 AQRKAFRRDIQMVFQDSisAVNPRKTVreiIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVC 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
16-203 4.51e-34

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 125.76  E-value: 4.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  16 QLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVF 93
Cdd:PRK10908   6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSgHDITRLKNREVPFLRRQIGMIF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHLSVLDNVMFGL----KKLPKAQRQAVAeqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK10908  86 QDHHLLMDRTVYDNVAIPLiiagASGDDIRRRVSA--ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 514971686 170 PFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHD 203
Cdd:PRK10908 164 PTGNLDDALSEGILR-LFEEFNRVGVTVLMATHD 196
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
27-224 4.65e-34

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: 126.84  E-value: 4.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEARNIGLVFQDY--ALFPHLS 103
Cdd:TIGR02769  27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQDSpsAVNPRMT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  104 V---LDNVMFGLKKLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:TIGR02769 107 VrqiIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 514971686  180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
26-241 8.84e-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: 130.96  E-value: 8.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTT----MLRLIagletPSSGSIQLEQQIL--WNEQQQIPAEaRNIGLVFQD-YA- 97
Cdd:COG4172  301 AVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLdgLSRRALRPLR-RRMQVVFQDpFGs 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  98 LFPHLSVLDNVMFGLK----KLPKAQRQAVAEQALQHVSMQH-HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:COG4172  375 LSPRMTVGQIIAEGLRvhgpGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 173 NLDHRLRDQIrqntIEILKQ----TGTTTVIVTHDpeeaLQ----IADQIILMHQGEIIQIGTPKALYRQPAT-----LF 239
Cdd:COG4172  455 ALDVSVQAQI----LDLLRDlqreHGLAYLFISHD----LAvvraLAHRVMVMKDGKVVEQGPTEQVFDAPQHpytraLL 526

                 ..
gi 514971686 240 AA 241
Cdd:COG4172  527 AA 528
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
11-231 1.84e-33

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 125.13  E-value: 1.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgSIQLEQQILWNEQQQIPAEARNI- 89
Cdd:PRK09984   4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-SAGSHIELLGRTVQREGRLARDIr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 ------GLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRV 152
Cdd:PRK09984  83 ksrantGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVT-HDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
31-222 2.08e-33

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: 122.32  E-value: 2.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEAR-NIGLVFQDYALFPHlSVLDNVm 109
Cdd:cd03246   22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDPNELGdHVGYLPQDDELFSG-SIAENI- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 110 fglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEI 189
Cdd:cd03246   97 ----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAIAA 141
                        170       180       190
                 ....*....|....*....|....*....|...
gi 514971686 190 LKQTGTTTVIVTHDPeEALQIADQIILMHQGEI 222
Cdd:cd03246  142 LKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
11-236 2.16e-33

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 124.50  E-value: 2.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAE 85
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK14239  85 RKEIGMVFQQPNPFP-MSIYENVVYGLRlkgIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKI-EETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
23-234 2.70e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 125.20  E-value: 2.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE------QQILWNEQQqipaearNIGLVFQ-- 94
Cdd:PRK13633  22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsdEENLWDIRN-------KAGMVFQnp 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  95 DYALFPHLsVLDNVMFGLKKL---PKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:PRK13633  95 DNQIVATI-VEEDVAFGPENLgipPEEIRERV-DESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 172 SNLDHRLRDQIrQNTI-EILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13633 173 AMLDPSGRREV-VNTIkELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
11-231 3.88e-33

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 123.47  E-value: 3.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEAR--- 87
Cdd:PRK10895   3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE----DISLLPLHARarr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK10895  79 GIGYLPQEASIFRRLSVYDNLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
14-223 1.09e-32

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 127.87  E-value: 1.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilwneqqQIPAEARnIGLVF 93
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------SIPKGLR-IGYLP 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHLSVLDNVMFGLKKLPKAQRQ-AVAEQA-------------LQHVSMQHHLHSYPY----------------- 142
Cdd:COG0488   68 QEPPLDDDLTVLDTVLDGDAELRALEAElEELEAKlaepdedlerlaeLQEEFEALGGWEAEAraeeilsglgfpeedld 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 ----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHrlrdqirqNTIE----ILKQTGTTTVIVTHDpeEAL--QIAD 212
Cdd:COG0488  148 rpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleeFLKNYPGTVLVVSHD--RYFldRVAT 217
                        250
                 ....*....|.
gi 514971686 213 QIILMHQGEII 223
Cdd:COG0488  218 RILELDRGKLT 228
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
39-243 2.18e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 122.08  E-value: 2.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA----RNIGLVFQDYALFPHLSVLDNVMFGLKK 114
Cdd:PRK14246  38 IFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 ---LPKAQRQAVAEQALQHVSMQHHLH----SYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:PRK14246 118 hgiKEKREIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 188 EILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:PRK14246 198 ELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
cbiO PRK13643
energy-coupling factor transporter ATPase;
16-271 3.60e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 122.53  E-value: 3.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  16 QLSKQFGSRfAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN--EQQQIPAEARNIGLVF 93
Cdd:PRK13643  12 QPNSPFASR-ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 Q--DYALFPHlSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK13643  91 QfpESQLFEE-TVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARyfsaLN 248
Cdd:PRK13643 170 EPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHE----LG 244
                        250       260
                 ....*....|....*....|....*..
gi 514971686 249 EIPAQRVAQQLQT----CFGAHPISEA 271
Cdd:PRK13643 245 VPKATHFADQLQKtgavTFEKLPITRA 271
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
31-260 5.25e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 121.38  E-value: 5.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipaEARN-IGLVFQDY--ALFPhLSVLDN 107
Cdd:PRK13647  25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSkVGLVFQDPddQVFS-STVWDD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQn 185
Cdd:PRK13647 101 VAFGPVnmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 186 TIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYR----QPATL---FAARYFSALNEIPAQRVAQQ 258
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDedivEQAGLrlpLVAQIFEDLPELGQSKLPLT 259

                 ..
gi 514971686 259 LQ 260
Cdd:PRK13647 260 VK 261
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
11-217 6.11e-32

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: 119.85  E-value: 6.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQF------GSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW------N 77
Cdd:COG4778    4 LLEVENLSKTFtlhlqgGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqaS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  78 EQQQIPAEARNIGLVFQdyalF----PHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQ 150
Cdd:COG4778   84 PREILALRRRTIGYVSQ----FlrviPRVSALDVVAEPLLERgvDREEARARARELLARLNLPERLwDLPPATFSGGEQQ 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILM 217
Cdd:COG4778  160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
37-226 1.32e-31

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: 118.91  E-value: 1.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLEtpSSGSIqLEQQILWNEQQQIPAEAR-NIGLVFQDYALFPHLSVLDNVMFGL--- 112
Cdd:cd03234   33 GQVMAILGSSGSGKTTLLDAISGRV--EGGGT-TSGQILFNGQPRKPDQFQkCVAYVRQDDILLPGLTVRETLTYTAilr 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 --KKLPKAQRQAVAEQ-ALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEI 189
Cdd:cd03234  110 lpRKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL----VST 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 190 LKQTGTT--TVIVT-HDP-EEALQIADQIILMHQGEIIQIG 226
Cdd:cd03234  186 LSQLARRnrIVILTiHQPrSDLFRLFDRILLLSSGEIVYSG 226
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
12-235 1.45e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 120.14  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPhLSVLDNVMFGLKKL---PKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK14258  88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQ-----GEIIQIGTPKALYRQ 234
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246

                 .
gi 514971686 235 P 235
Cdd:PRK14258 247 P 247
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
22-227 4.95e-31

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: 123.70  E-value: 4.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALF 99
Cdd:COG4618  343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqWDREEL----GRHIGYLPQDVELF 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 PHlSVLDNVmfglKKLPKAQRQAVAEqALQHVSMqHHL-HSYP--Y---------TLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4618  419 DG-TIAENI----ARFGDADPEKVVA-AAKLAGV-HEMiLRLPdgYdtrigeggaRLSGGQRQRIGLARALYGDPRLVVL 491
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHR----LRDQIRQntieiLKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGT 227
Cdd:COG4618  492 DEPNSNLDDEgeaaLAAAIRA-----LKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
26-231 9.01e-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: 116.94  E-value: 9.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIP-AEARN-IGLVFQDYALFPHlS 103
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISrKSLRSmIGVVLQDTFLFSG-T 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLkklPKAQRQAVAEqALQHVSMQHHLHSYP--Y---------TLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd03254   93 IMENIRLGR---PNATDEEVIE-AAKEAGAHDFIMKLPngYdtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATS 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 173 NLDHRLrDQIRQNTIEILKQtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03254  169 NIDTET-EKLIQEALEKLMK-GRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDEL 224
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
12-223 9.98e-31

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 117.88  E-value: 9.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGS-----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipa 84
Cdd:COG1101    2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKR--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 eARNIGLVFQDYAL--FPHLSVLDNVM--------FGLKK-LPKAQRQAVAEQ-ALQHVSMQHHLHSYPYTLSGGEQQRV 152
Cdd:COG1101   79 -AKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRgLTKKRRELFRELlATLGLGLENRLDTKVGLLSGGQRQAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG1101  158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
26-236 1.09e-30

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: 116.70  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP----SSGSIQLEQQILwneqQQIPAEARNIGLVFQD--YALF 99
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL----LPLSIRGRHIATIMQNprTAFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  100 PHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHH---LHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNL 174
Cdd:TIGR02770  77 PLFTMGNHAIETLRSLgkLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  175 DHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPK 218
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
23-231 1.30e-30

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: 116.56  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHL 102
Cdd:cd03253   13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLF-ND 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQhhlhSYP--YT---------LSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03253   90 TIGYNIRYGRPDATDEEVIEAAKAAQIHDKIM----RFPdgYDtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03253  166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
11-222 1.80e-30

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 114.84  E-value: 1.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSkqfgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNeqqqIPAEARNI 89
Cdd:cd03215    4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRR----SPRDAIRA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVF-----QDYALFPHLSVLDNVMFglkklpkaqrqavaeqalqhvsmqhhlhsyPYTLSGGEQQRVALARALAPKPQV 164
Cdd:cd03215   76 GIAYvpedrKREGLVLDLSVAENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03215  126 LILDEPTRGVDVGAKAEIYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
26-235 3.89e-30

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 117.76  E-value: 3.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVFQD-YA-LFPHL 102
Cdd:PRK11308  30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKADPEAQKLLRQKIQIVFQNpYGsLNPRK 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK11308 110 KVGQILEEPLLintSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 179 RDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
12-228 4.96e-30

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: 120.68  E-value: 4.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLET--PSSGSI--------------------- 68
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   69 ---------QLEQQILWNEQQQIPAE-ARNIGLVFQ-DYALFPHLSVLDNVMFGLKKLPKAQRQAV--AEQALQHVSMQH 135
Cdd:TIGR03269  81 pcpvcggtlEPEEVDFWNLSDKLRRRiRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVgrAVDLIEMVQLSH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  136 HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQII 215
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
                         250
                  ....*....|...
gi 514971686  216 LMHQGEIIQIGTP 228
Cdd:TIGR03269 241 WLENGEIKEEGTP 253
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
11-231 9.84e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 116.06  E-value: 9.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwnEQQQIPAEARN-- 88
Cdd:PRK13537   7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL-------CGEPVPSRARHar 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 --IGLVFQDYALFPHLSVLDNVM-----FGlkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:PRK13537  80 qrVGVVPQFDNLDPDFTVRENLLvfgryFG---LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
11-223 1.28e-29

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 119.40  E-value: 1.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNIG 90
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV-------------KIG 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALF-PHLSVLDNVMFGLKKLPKAQ-RQAVA------EQALQHVSmqhhlhsypyTLSGGEQQRVALARALAPKP 162
Cdd:COG0488  382 YFDQHQEELdPDKTVLDELRDGAPGGTEQEvRGYLGrflfsgDDAFKPVG----------VLSGGEKARLALAKLLLSPP 451
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 163 QVLLMDEPFSNLDhrlrdqIrqNTIEILKQ-----TGtTTVIVTHDpEEALQ-IADQIILMHQGEII 223
Cdd:COG0488  452 NVLLLDEPTNHLD------I--ETLEALEEalddfPG-TVLLVSHD-RYFLDrVATRILEFEDGGVR 508
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
11-238 1.31e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 116.10  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSR-----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-----QQILWNEQQ 80
Cdd:PRK13631  21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigDKKNNHELI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 QIPAEA---------RNIGLVFQ--DYALFPHlSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQH-HLHSYPYTLSG 146
Cdd:PRK13631 101 TNPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALgvKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
                        250
                 ....*....|..
gi 514971686 227 TPKALYRQPATL 238
Cdd:PRK13631 259 TPYEIFTDQHII 270
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
33-232 1.56e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 114.94  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  33 SAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALFPhLSVLDNVMF 110
Cdd:PRK13636  28 NIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQdpDNQLFS-ASVYQDVSF 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK13636 107 GAVnlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 514971686 189 ILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13636 187 MQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-230 1.97e-29

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 118.61  E-value: 1.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQq 80
Cdd:PRK15439   1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  81 qiPAEARNIG--LVFQDYALFPHLSVLDNVMFGLKKLPKAQRQavAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK15439  80 --PAKAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQG-------------- 220
Cdd:PRK15439 156 MRDSRILILDEPTASLTpaetERLFSRIRE-----LLAQGVGIVFISHKLPEIRQLADRISVMRDGtialsgktadlstd 230
                        250
                 ....*....|
gi 514971686 221 EIIQIGTPKA 230
Cdd:PRK15439 231 DIIQAITPAA 240
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
37-223 2.07e-29

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 119.44  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR--NIGLVFQDYALFPHLSVLDNVMFG--L 112
Cdd:PRK10535  34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRreHFGFIFQRYHLLSHLTAAQNVEVPavY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQ 192
Cdd:PRK10535 114 AGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV-MAILHQLRD 192
                        170       180       190
                 ....*....|....*....|....*....|.
gi 514971686 193 TGTTTVIVTHDPEEALQiADQIILMHQGEII 223
Cdd:PRK10535 193 RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
cbiO PRK13641
energy-coupling factor transporter ATPase;
29-260 2.59e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 114.54  E-value: 2.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  29 QASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL--EQQILWNEQQQIPAEARNIGLVFQ--DYALFPHlSV 104
Cdd:PRK13641  25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNVMFGLKKLPKAQRQAvAEQALQ---HVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEA-KEKALKwlkKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 181 QIRQNTIEILKqTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLfaARYFsaLNEIPAQRVAQQLQ 260
Cdd:PRK13641 183 EMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL--KKHY--LDEPATSRFASKLE 257
cbiO PRK13649
energy-coupling factor transporter ATPase;
37-234 6.68e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 113.30  E-value: 6.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN--EQQQIPAEARNIGLVFQ--DYALFPHlSVLDNVMFGL 112
Cdd:PRK13649  33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 KKLPKAQRQA--VAEQALQHVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEI 189
Cdd:PRK13649 112 QNFGVSQEEAeaLAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKK 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 514971686 190 LKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13649 191 LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
11-223 1.20e-28

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 116.27  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSkqfgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEARN 88
Cdd:COG1129  256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD-----GKPVRIrsPRDAIR 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVF-----QDYALFPHLSVLDNVMFG-LKKL-------PKAQRQAVAE--QAL--------QHVSmqhhlhsypyTLS 145
Cdd:COG1129  327 AGIAYvpedrKGEGLVLDLSIRENITLAsLDRLsrgglldRRRERALAEEyiKRLriktpspeQPVG----------NLS 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 146 GGEQQRVALARALAPKPQVLLMDEPFSNLD-------HRLrdqIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMH 218
Cdd:COG1129  397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRL---IRE-----LAAEGKAVIVISSELPELLGLSDRILVMR 468

                 ....*
gi 514971686 219 QGEII 223
Cdd:COG1129  469 EGRIV 473
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
7-242 2.01e-28

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: 115.94  E-value: 2.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   7 AQANVLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKT----TMLRLIAGLETPSSGSIQLE-QQILwn 77
Cdd:COG4172    2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDLL-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  78 eqqQIPAEA------RNIGLVFQD--YALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT 143
Cdd:COG4172   80 ---GLSERElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLrlhRGLSGAAARARALELLERVGIpdpERRLDAYPHQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDpeeaL----QIADQII 215
Cdd:COG4172  157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQI----LDLLKdlqrELGMALLLITHD----LgvvrRFADRVA 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 514971686 216 LMHQGEIIQIGTPKALYRQPA-----TLFAAR 242
Cdd:COG4172  229 VMRQGEIVEQGPTAELFAAPQhpytrKLLAAE 260
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
31-234 2.37e-28

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: 110.71  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPhLSVLDNVMF 110
Cdd:cd03249   23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFD-GTIAENIRY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLKKLPKAQRQAVAEQALQH---VSMQHHLHS----YPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIr 183
Cdd:cd03249  100 GKPDATDEEVEEAAKKANIHdfiMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV- 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 184 QNTIEILKQtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03249  179 QEALDRAMK-GRTTIVIAHR-LSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
7-248 2.47e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 111.73  E-value: 2.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-----SIQLEQQILWNEQQQ 81
Cdd:PRK14271  17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPAEaRNIGLVFQDYALFPhLSVLDNVMFGL---KKLPKAQRQAVAEQALQHV----SMQHHLHSYPYTLSGGEQQRVAL 154
Cdd:PRK14271  97 LEFR-RRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 155 ARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
                        250
                 ....*....|....
gi 514971686 235 PATLFAARYFSALN 248
Cdd:PRK14271 253 PKHAETARYVAGLS 266
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
7-240 3.96e-28

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 110.46  E-value: 3.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQILWNEQQQIpae 85
Cdd:PRK11300   1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEGLPGHQI--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARnIGLV--FQDYALFPHLSVLDNVMF------------GLKKLP---KAQRQAV--AEQALQHVSMQHHLHSYPYTLSG 146
Cdd:PRK11300  78 AR-MGVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPafrRAESEALdrAATWLERVGLLEHANRQAGNLAY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
                        250
                 ....*....|....
gi 514971686 227 TPKALYRQPATLFA 240
Cdd:PRK11300 237 TPEEIRNNPDVIKA 250
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
12-228 4.32e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 110.49  E-value: 4.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAE--ARNI 89
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----MLSSRqlARRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQ--------------DYALFPHLSvldnvMFGlkKLPKAQRQAVaEQALQ--HVSmqhHLHSYPYT-LSGGEQQRV 152
Cdd:PRK11231  79 ALLPQhhltpegitvrelvAYGRSPWLS-----LWG--RLSAEDNARV-NQAMEqtRIN---HLADRRLTdLSGGQRQRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLD--HR--LRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDinHQveLMRLMRE-----LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
12-241 6.00e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 113.01  E-value: 6.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGL 91
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRRVAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYAL--------------FPHLSVLDnvmfglkKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:PRK09536  82 VPQDTSLsfefdvrqvvemgrTPHRSRFD-------TWTETDRAAV-ERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 158 LAPKPQVLLMDEPFSNLDhrLRDQIRqnTIEI---LKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYrQ 234
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD--INHQVR--TLELvrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL-T 228

                 ....*..
gi 514971686 235 PATLFAA 241
Cdd:PRK09536 229 ADTLRAA 235
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
13-228 1.06e-27

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 109.40  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAE--ARNIG 90
Cdd:COG4604    3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV----ATTPSRelAKRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFG-----LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4604   79 ILRQENHINSRLTVRELVAFGrfpysKGRLTAEDREII-DEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 166 LMDEPFSNLD--H--RLRDQIRQNTIEIlkqtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG4604  158 LLDEPLNNLDmkHsvQMMKLLRRLADEL----GKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
10-242 1.06e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 109.89  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqIPAEARN 88
Cdd:PRK13652   2 HLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQ--DYALFPHlSVLDNVMFGLKKLpKAQRQAVA---EQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:PRK13652  80 VGLVFQnpDDQIFSP-TVEQDIAFGPINL-GLDEETVAhrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAAR 242
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
5-212 1.17e-27

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 109.49  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQAN-VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLR-------LIAGLETpsSGSIQLEQQILW 76
Cdd:PRK14243   3 TLNGTEtVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  77 NEQQQiPAEARN-IGLVFQDYALFPHlSVLDNVMFGLKKLP-KAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQ 150
Cdd:PRK14243  81 APDVD-PVEVRRrIGMVFQKPNPFPK-SIYDNIAYGARINGyKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQ 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLD--HRLRDQirqntiEILKQTGT--TTVIVTHDPEEALQIAD 212
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSD 218
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
24-234 1.67e-27

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: 108.47  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  24 RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHLS 103
Cdd:cd03251   15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLF-NDT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLKKLPKAQRQAVAEQALQH---VSMQHHLHSY----PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:cd03251   92 VAENIAYGRPGATREEVEEAARAANAHefiMELPEGYDTVigerGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 177 RLRDQIrQNTIEILKQtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03251  172 ESERLV-QAALERLMK-NRTTFVIAHR-LSTIENADRIVVLEDGKIVERGTHEELLAQ 226
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
5-217 1.69e-27

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: 113.15  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    5 TAAQANVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIP 83
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----DAD 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   84 AEA--RNIGLVFQDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQA-----LQHVSMQHH--LHSYPYTLSGGEQQRVAL 154
Cdd:TIGR02857 391 ADSwrDQIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAgldefVAALPQGLDtpIGEGGAGLSGGQAQRLAL 469
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686  155 ARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIEILKQ--TGTTTVIVTHDPEEALQiADQIILM 217
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRAlaQGRTVLLVTHRLALAAL-ADRIVVL 529
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
18-223 2.04e-27

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: 106.87  E-value: 2.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  18 SKQFGSRFAV-HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSsgsiQLEQQILWNEQQQIPAEARN-IGLVFQD 95
Cdd:cd03213   15 SSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL----GVSGEVLINGRPLDKRSFRKiIGYVPQD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  96 YALFPHLSVLDNVMFGLKklpkaqrqavaeqalqhvsmqhhLHSypytLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:cd03213   91 DILHPTLTVRETLMFAAK-----------------------LRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 176 HRLRDQIRQnTIEILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEII 223
Cdd:cd03213  144 SSSALQVMS-LLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
cbiO PRK13642
energy-coupling factor transporter ATPase;
11-232 3.69e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 108.64  E-value: 3.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQ---ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL-----WNEQqqi 82
Cdd:PRK13642   4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvWNLR--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 paeaRNIGLVFQDY-ALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK13642  81 ----RKIGMVFQNPdNQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
cbiO PRK13645
energy-coupling factor transporter ATPase;
26-228 4.40e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 108.56  E-value: 4.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-SIQLEQQILWNEQQ--QIPAEARNIGLVFQ--DYALFP 100
Cdd:PRK13645  26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKikEVKRLRKEIGLVFQfpEYQLFQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HlSVLDNVMFGLKKLPKAQRQAVAE--QALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHR 177
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 178 LRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
21-216 1.39e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 104.62  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  21 FGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNIGLVFQDYAL-- 98
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-------------AGGARVAYVPQRSEVpd 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  99 -FPhLSVLDNVMFG-------LKKLPKAQRqAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040873  69 sLP-LTVRDLVAMGrwarrglWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 171 FSNLDHRLRDQIrqntIEILKQ---TGTTTVIVTHDPEEALQIADQIIL 216
Cdd:NF040873 147 TTGLDAESRERI----IALLAEehaRGATVVVVTHDLELVRRADPCVLL 191
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
14-236 2.05e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 110.18  E-value: 2.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQ--LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTT----MLRLIAgletpSSGSIQLEQQIL--WNEQQQIPAE 85
Cdd:PRK15134 287 IRKgiLKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhnLNRRQLLPVR 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARnIGLVFQD--YALFPHLSVLDNVMFGL----KKLPKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQRVALARAL 158
Cdd:PRK15134 362 HR-IQVVFQDpnSSLNPRLNVLQIIEEGLrvhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARAL 440
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
cbiO PRK13646
energy-coupling factor transporter ATPase;
26-234 2.18e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 106.79  E-value: 2.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNE--QQQIPAEARNIGLVFQdyalFPHLS 103
Cdd:PRK13646  22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPVRKRIGMVFQ----FPESQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VL-DNV----MFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK13646  98 LFeDTVereiIFGPKnfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 176 HRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
11-227 2.67e-26

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 106.03  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRF---------AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQ 81
Cdd:PRK15112   4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  82 IPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK15112  82 YSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRlntDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGT 227
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
14-234 5.00e-26

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 104.39  E-value: 5.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqiPAEarnIGLVF 93
Cdd:COG1134   29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA------LLE---LGAGF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QdyalfPHLSVLDNVMF-----GLKKL-PKAQRQAVAEQAlqhvSMQHHLHSyPY-TLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1134  100 H-----PELTGRENIYLngrllGLSRKeIDEKFDEIVEFA----ELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILL 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 167 MDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK---ALYRQ 234
Cdd:COG1134  170 VDEVLAVGDaafqKKCLARIRE-----LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEeviAAYEA 239
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
24-226 6.07e-26

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: 103.77  E-value: 6.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  24 RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqiPAEarnIGLVFQdyalfPHLS 103
Cdd:cd03220   35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS------LLG---LGGGFN-----PELT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHsYPY-TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03220  101 GRENIYLNgrLLGLSRKEIDEKIDEIIEFSELGDFID-LPVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 514971686 181 QIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03220  180 KC-QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
17-231 6.99e-26

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 106.45  E-value: 6.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEAR----NIGLV 92
Cdd:PRK13536  47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-------PVPARARlaraRIGVV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 FQDYALFPHLSVLDNVM-----FGLKKlpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLvfgryFGMST---REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
cbiO PRK13644
energy-coupling factor transporter ATPase;
35-236 3.40e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 103.14  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqLEQQILWNEQQQIPAEARNIGLVFQD-YALFPHLSVLDNVMFGLK 113
Cdd:PRK13644  26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 KL--PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNtIEILK 191
Cdd:PRK13644 105 NLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER-IKKLH 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 514971686 192 QTGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK13644 184 EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
12-226 3.61e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 102.70  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIP-AEARNI 89
Cdd:PRK11701   7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdGQLRDLYALSeAERRRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 -----GLVFQDYA--LFPHLSVLDNVmfGLKKLPKAQR-----QAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK11701  87 lrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARhygdiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIAR 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 157 ALAPKPQVLLMDEPFSNLD----HRLRDQIRQNTIEIlkqtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVREL----GLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
22-227 7.33e-25

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: 105.89  E-value: 7.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALF 99
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqWDRETF----GKHIGYLPQDVELF 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  100 PHlSVLDNVM-FGlkklPKAQRQAVAEQAlqHVSMQHHL-HSYP--Y---------TLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR01842 405 PG-TVAENIArFG----ENADPEKIIEAA--KLAGVHELiLRLPdgYdtvigpggaTLSGGQRQRIALARALYGDPKLVV 477
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686  167 MDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGT 227
Cdd:TIGR01842 478 LDEPNSNLDEE-GEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGRIARFGE 536
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
37-235 9.79e-25

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 102.86  E-value: 9.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK 113
Cdd:PRK15079  47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 KL-PKAQRQAVAEQA---LQHVSMQHHL-HSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK15079 127 TYhPKLSRQEVKDRVkamMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 514971686 189 ILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK15079 207 LQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
26-223 1.71e-24

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: 100.10  E-value: 1.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGLVF-QDYALFPHLSV 104
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFgQKTQLWWDLPV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LD--NVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:cd03267  113 IDsfYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 183 RQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03267  193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
11-231 2.67e-24

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 99.57  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQ-QQIPAEArnI 89
Cdd:PRK11614   5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA--V 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQ-HVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 169 EPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK11614 163 EPSLGLAPIIIQQIF-DTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
23-234 3.20e-24

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: 99.48  E-value: 3.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL------WNEQQqipaearnIGLVFQDY 96
Cdd:cd03252   14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpaWLRRQ--------VGVVLQEN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  97 ALFpHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-------LSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03252   86 VLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIvgeqgagLSGGQRQRIAIARALIHNPRILIFDE 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03252  165 ATSALDYESEHAIMRNMHDICA--GRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
12-228 5.09e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 100.55  E-value: 5.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRF-----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqILWNEQ------- 79
Cdd:PRK13651   3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKnkkktke 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  80 ------------------QQIPAEARNIGLVFQ--DYALFPHlSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSM-QHH 136
Cdd:PRK13651  80 kekvleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLdESY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 137 LHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrdqiRQNTIEILK------QTGTTTVIVTHDPEEALQI 210
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD-------PQGVKEILEifdnlnKQGKTIILVTHDLDNVLEW 231
                        250
                 ....*....|....*...
gi 514971686 211 ADQIILMHQGEIIQIGTP 228
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDT 249
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
11-226 1.90e-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: 97.59  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIP-AEARN 88
Cdd:TIGR02323   3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsGAELELYQLSeAERRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   89 I-----GLVFQDYALFPHLSVLDNVMFGLKKLPKAQR-----QAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR02323  83 LmrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686  158 LAPKPQVLLMDEPFSNLD----HRLRDQIRQntieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
15-241 2.24e-23

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 101.74  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  15 RQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqqiPAEARNI----- 89
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---------PVDAGDIatrrr 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 -GLVFQDYALFPHLSVLDNVM-----FGlkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:NF033858 341 vGYMSQAFSLYGELTVRQNLElharlFH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALY--RQPATLFAA 241
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVaaRGAATLEEA 496
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
37-235 4.73e-23

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 100.95  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMFGLKKLP 116
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTP 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  117 KAQRQAVAEQALQHVSMQHHLHSYpYT--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIE 188
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFIMEFPNGY-DTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQE 658
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 514971686  189 ILKQTGTTTVIVTHDPEEAlQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:TIGR00958 659 SRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
26-235 6.05e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 100.31  E-value: 6.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVFQD-YA-LFPHL 102
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgQRIDTLSPGKLQALRRDIQFIFQDpYAsLDPRQ 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLKKLPKAQRQAVAEQA---LQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVawlLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 179 RDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
12-221 6.49e-23

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: 93.28  E-value: 6.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNIGL 91
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------KIGY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03221   68 FEQ-------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03221   99 NHLDLESIEAL----EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
12-204 7.66e-23

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 94.73  E-value: 7.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQQIPaeARNIGL 91
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEP--HENILY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQavAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR01189  78 LGHLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 514971686  172 SNLD----HRLRDQIRQNTieilkQTGTTTVIVTHDP 204
Cdd:TIGR01189 156 TALDkagvALLAGLLRAHL-----ARGGIVLLTTHQD 187
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
11-235 2.20e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 96.35  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRF----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETP---SSGSIQLEQQILwneqQQI 82
Cdd:PRK11022   3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDL----QRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 PAEAR------NIGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM------QHHLHSYPYTLSGGE 148
Cdd:PRK11022  79 SEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238

                 ....*..
gi 514971686 229 KALYRQP 235
Cdd:PRK11022 239 HDIFRAP 245
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
10-254 3.62e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 98.00  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKT-TMLRLIAGLETpSSGSIQLEQQILWNEQQQI-- 82
Cdd:PRK10261  11 DVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRSRQVie 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  83 -----PAEAR-----NIGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQ---AVAEQALQHVSM---QHHLHSYPYTL 144
Cdd:PRK10261  90 lseqsAAQMRhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREeamVEAKRMLDQVRIpeaQTILSRYPHQL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 145 SGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAV 248
                        250       260       270
                 ....*....|....*....|....*....|.
gi 514971686 224 QIGTPKALYRQPATLFAARYFSALNEIPAQR 254
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAMK 279
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
37-204 4.30e-22

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: 97.43  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIGLVFQDYALFpHLSVLDNVMFGLkklP 116
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD--EVRRRVSVCAQDAHLF-DTTVRENLRLAR---P 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  117 KAQRQAVAEqALQHVSMQHHLHSYPY-----------TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqn 185
Cdd:TIGR02868 435 DATDEELWA-ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL--- 510
                         170       180
                  ....*....|....*....|.
gi 514971686  186 tIEILKQ--TGTTTVIVTHDP 204
Cdd:TIGR02868 511 -LEDLLAalSGRTVVLITHHL 530
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
14-254 4.97e-22

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: 98.16  E-value: 4.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    14 IRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGL 91
Cdd:TIGR01257  931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGM 1007
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   170 PFSNLDHRLRDQIRQNTIEIlkQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKN 1165

                   ....*
gi 514971686   250 IPAQR 254
Cdd:TIGR01257 1166 IQSQR 1170
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
18-221 5.94e-22

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: 92.15  E-value: 5.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  18 SKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipaeARNIGLVFQdYA 97
Cdd:cd03250   12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------------PGSIAYVSQ-EP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  98 LFPHLSVLDNVMFG--------------------LKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARA 157
Cdd:cd03250   76 WIQNGTIRENILFGkpfdeeryekvikacalepdLEILPDGDLTEIGEKGI--------------NLSGGQKQRISLARA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpEEALQIADQIILMHQGE 221
Cdd:cd03250  142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQ-LQLLPHADQIVVLDNGR 204
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
10-235 1.07e-21

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 92.87  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNI 89
Cdd:PRK09544   3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------------RI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLKklPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK09544  70 GYVPQKLYLDTTLPLTVNRFLRLR--PGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 170 PFSNLD-------HRLRDQIRQntieilkQTGTTTVIVTHDPEEALQIADQIILMHQgEIIQIGTPKALYRQP 235
Cdd:PRK09544 147 PTQGVDvngqvalYDLIDQLRR-------ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
8-215 1.43e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 91.70  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA- 86
Cdd:PRK10247   4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE----DISTLKPEIy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 -RNIGLVFQDYALFPHlSVLDNVMFglkklP-KAQRQAVAEQALQHVSMQ-----HHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK10247  80 rQQVSYCAQTPTLFGD-TVYDNLIF-----PwQIRNQQPDPAIFLDDLERfalpdTILTKNIAELSGGEKQRISLIRNLQ 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDhrlrDQIRQNTIEIL----KQTGTTTVIVTHDPEEaLQIADQII 215
Cdd:PRK10247 154 FMPKVLLLDEITSALD----ESNKHNVNEIIhryvREQNIAVLWVTHDKDE-INHADKVI 208
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
12-226 1.63e-21

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: 90.45  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNI 89
Cdd:cd03247    1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDyalfPHL---SVLDNVmfGLKklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLL 166
Cdd:cd03247   78 SVLNQR----PYLfdtTLRNNL--GRR------------------------------FSGGERQRLALARILLQDAPIVL 121
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03247  122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHH-LTGIEHMDKILFLENGKIIMQG 178
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
12-231 1.65e-21

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: 96.35  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   12 LTIRQLSKQFG-SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIG 90
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQFIN 551
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   91 LVFQDYALFPHlSVLDNVMFGLK------KLPKAQRQAVAEQALQHVSMQHH--LHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLGAKenvsqdEIWAACEIAEIKDDIENMPLGYQteLSEEGSSISGGQKQRIALARALLTDS 630
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686  163 QVLLMDEPFSNLDHRLRDQIRQNtieILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNN---LLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
16-231 3.14e-21

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 91.97  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  16 QLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneQQQIPAE-ARNIGLVF 93
Cdd:PRK10253  12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgEHI----QHYASKEvARRIGLLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVAeQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK10253  88 QNATTPGDITVQELVARGryphqplFTRWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
31-263 4.04e-21

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 91.06  E-value: 4.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQIL-------------WNEQQQIPAEARnigLVFQDYA 97
Cdd:COG4138   16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLsdwsaaelarhraYLSQQQSPPFAM---PVFQYLA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  98 LFphlsvldnvmfglkkLPKAQRQAVAEQALQHVS--------MQHHLHsypyTLSGGEQQRVALARALA-------PKP 162
Cdd:COG4138   92 LH---------------QPAGASSEAVEQLLAQLAealgledkLSRPLT----QLSGGEWQRVRLAAVLLqvwptinPEG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 163 QVLLMDEPFSNLDhrlrdqIRQNT-----IEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYrQPAT 237
Cdd:COG4138  153 QLLLLDEPMNSLD------VAQQAaldrlLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
                        250       260
                 ....*....|....*....|....*.
gi 514971686 238 LfaaryfSALNEIPAQRVAQQLQTCF 263
Cdd:COG4138  226 L------SEVFGVKFRRLEVEGHRWL 245
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
42-232 4.53e-21

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 91.61  E-value: 4.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQD--YALFpHLSVLDNVMFGLKKL--PK 117
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDpeQQIF-YTDIDSDIAFSLRNLgvPE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 118 AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK---QTG 194
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM----IAIIRrivAQG 186
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514971686 195 TTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13638 187 NHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1-235 4.95e-21

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 91.39  E-value: 4.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNE 78
Cdd:PRK10575   1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLesWSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  79 QqqipAEARNIGLVFQDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQR 151
Cdd:PRK10575  81 K----AFARKVAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 152 VALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235

                 ....
gi 514971686 232 YRQP 235
Cdd:PRK10575 236 MRGE 239
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
37-242 9.63e-21

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 93.76  E-value: 9.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALFpHLSVLDNVMFGLKK 114
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGI----ELRELDPESwrKHLSWVGQNPQLP-HGTLRDNVLLGNPD 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQA--LQHVSMQHHLHSYPY-----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntI 187
Cdd:PRK11174 450 ASDEQLQQALENAwvSEFLPLLPQGLDTPIgdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV----M 525
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 188 EILKQ--TGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQP---ATLFAAR 242
Cdd:PRK11174 526 QALNAasRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAGglfATLLAHR 584
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
10-204 1.87e-20

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 88.39  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQIPAEARNI 89
Cdd:PRK13539   1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-----GGDIDDPDVAEAC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVMFGLKKLpkAQRQAVAEQALQHVSMQHHLHsYPY-TLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK13539  76 HYLGHRNAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPLAH-LPFgYLSAGQKRRVALARLLVSNRPIWILD 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 514971686 169 EPFSNLDhRLRDQIRQNTIEILKQTGTTTVIVTHDP 204
Cdd:PRK13539 153 EPTAALD-AAAVALFAELIRAHLAQGGIVIAATHIP 187
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
26-223 3.10e-20

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 90.15  E-value: 3.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGLVF-QDYALFPHLSV 104
Cdd:COG4586   37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF---ARRIGVVFgQRSQLWWDLPA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNvmFGLKK----LPKAQ-RQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD---- 175
Cdd:COG4586  114 IDS--FRLLKaiyrIPDAEyKKRLDELV-ELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvsk 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 514971686 176 HRLRDQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG4586  191 EAIREFLK----EYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
11-230 4.29e-20

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: 91.42  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgsiqLEQQILWNEQQQIPA-----E 85
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT----WDGEIYWSGSPLKASnirdtE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAV------AEQALQHVSMQHHLHSYPYT-LSGGEQQRVALARAL 158
Cdd:TIGR02633  77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamylrAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  159 APKPQVLLMDEPFSNLDhRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEiiQIGTPKA 230
Cdd:TIGR02633 157 NKQARLLILDEPSSSLT-EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKDM 225
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
17-220 6.67e-20

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 91.00  E-value: 6.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqQILWNEQQQIPAEARNIGLVFQDY 96
Cdd:PRK09700  11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAQLGIGIIYQEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  97 ALFPHLSVLDNVMFGlkKLPK-----------AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK09700  90 SVIDELTVLENLYIG--RHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 166 LMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQG 220
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYlfliMNQ-----LRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
28-228 7.92e-20

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 90.88  E-value: 7.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   28 HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLetpSSGSIQLEQQILWNEQqqiPAEARNI----GLVFQDYALFPHLS 103
Cdd:TIGR00955  42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGM---PIDAKEMraisAYVQQDDLFIPTLT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  104 VLDNVMFGL-----KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT---LSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:TIGR00955 116 VREHLMFQAhlrmpRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686  173 NLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPE-EALQIADQIILMHQGEIIQIGTP 228
Cdd:TIGR00955 196 GLDSFMAYSVVQ-VLKGLAQKGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSP 251
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
26-226 9.90e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 88.02  E-value: 9.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipaeaRNIGLVFQ----DYAlFPH 101
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK-----NLVAYVPQseevDWS-FPV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 LsVLDNVMFG------LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK15056  96 L-VEDVVMMGryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514971686 176 HRLRDQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIIlMHQGEIIQIG 226
Cdd:PRK15056 175 VKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASG 223
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1-236 1.07e-19

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 88.63  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   1 MNAYTAAQANVLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPS---SGSIQLE-Q 72
Cdd:PRK09473   2 VPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNgR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  73 QIL-WNEQQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT 143
Cdd:PRK09473  82 EILnLPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLmlhKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
                        250
                 ....*....|...
gi 514971686 224 QIGTPKALYRQPA 236
Cdd:PRK09473 242 EYGNARDVFYQPS 254
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
11-236 1.37e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 87.06  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQfGSRFAVHQASWSAQRGQIICLLGHSGCGKTtmLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE--ARN 88
Cdd:PRK10418   4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCAlrGRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 IGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM---QHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:PRK10418  81 IATIMQNprSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
37-234 1.39e-19

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: 90.26  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEA--RNIGLVFQDYALFpHLSVLDNVMFGLkk 114
Cdd:COG5265  384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI----RDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYGR-- 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 lPKAQRQAVaEQALQHVsmqhHLH----SYP--Y-T--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:COG5265  457 -PDASEEEV-EAAARAA----QIHdfieSLPdgYdTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 180 DQIrQNTIEILKQtGTTTVIVTH------DpeealqiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG5265  531 RAI-QAALREVAR-GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAELLAQ 582
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
12-225 1.40e-19

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 90.03  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSR-FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIG 90
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE--DYRKLFS 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLsvldnvmfgLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-----LSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10522 401 AVFTDFHLFDQL---------LGPEGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDIL 471
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpEEALQIADQIILMHQGEIIQI 225
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
22-227 1.67e-19

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 90.02  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALF 99
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRASlrRNIAVVFQDAGLF 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 pHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPY-------TLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:PRK13657 422 -NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEATS 500
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 173 NLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGT 227
Cdd:PRK13657 501 ALDVETEAKVKAALDELMK--GRTTFIIAHR-LSTVRNADRILVFDNGRVVESGS 552
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
11-230 2.39e-19

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 89.22  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPsSGSiqLEQQILWNEQQQIPA-----E 85
Cdd:PRK13549   5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGT--YEGEIIFEGEELQASnirdtE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPK-----AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:PRK13549  81 RAGIAIIHQELALVKELSVLENIFLGNEITPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 161 KPQVLLMDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEiiQIGTPKA 230
Cdd:PRK13549 161 QARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGTRPA 227
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
12-204 2.66e-19

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 84.85  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGL 91
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARGLLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VFQDYALFPHLSVLDNVMFglkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03231   78 LGHAPGIKTTLSVLENLRF----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 514971686 172 SNLD----HRLRDQIRQNTieilkQTGTTTVIVTHDP 204
Cdd:cd03231  154 TALDkagvARFAEAMAGHC-----ARGGMVVLTTHQD 185
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
31-229 2.81e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 86.14  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQIL-------------WNEQQQIPAEARNiglVFQDYA 97
Cdd:PRK03695  16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsaaelarhraYLSQQQTPPFAMP---VFQYLT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  98 LfpHLSVldnvmfglkKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA-------RALAPKPQVLLMDEP 170
Cdd:PRK03695  92 L--HQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 171 FSNLD---HRLRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:PRK03695 161 MNSLDvaqQAALDRL----LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
5-205 3.16e-19

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 89.10  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSKQFGS-RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqiP 83
Cdd:COG4178  356 ETSEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------------P 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 AEARniglvfqdyALF----PHLSV--LDNVMFglkkLPKAQRQ---AVAEQALQHVSMQHHLHSY------PYTLSGGE 148
Cdd:COG4178  424 AGAR---------VLFlpqrPYLPLgtLREALL----YPATAEAfsdAELREALEAVGLGHLAERLdeeadwDQVLSLGE 490
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQntieILKQT--GTTTVIVTHDPE 205
Cdd:COG4178  491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ----LLREElpGTTVISVGHRST 545
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
11-231 4.16e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 88.55  E-value: 4.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLS-KQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNI 89
Cdd:COG3845  257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRL 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVF-----QDYALFPHLSVLDNVMFGLKKLPKAQR------QAVAEQALQHVSmqhhlhSY------PYT----LSGGE 148
Cdd:COG3845  334 GVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIE------EFdvrtpgPDTparsLSGGN 407
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG3845  408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486

                 ...
gi 514971686 229 KAL 231
Cdd:COG3845  487 AEA 489
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
26-245 5.25e-19

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 88.34  E-value: 5.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALFPHlS 103
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSEAAL----RQAISVVSQRVHLFSA-T 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGlkkLPKAQRQAVAEqALQHVSMQHHLHSYP----------YTLSGGEQQRVALARAL---APkpqVLLMDEP 170
Cdd:PRK11160 430 LRDNLLLA---APNASDEALIE-VLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALlhdAP---LLLLDEP 502
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 171 FSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQpatlfAARYFS 245
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ--NKTVLMITHR-LTGLEQFDRICVMDNGQIIEQGTHQELLAQ-----QGRYYQ 569
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
8-224 1.98e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 86.50  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwNEQQQIPAEAR 87
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI------DGQEMRFASTT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 N-----IGLVFQDYALFPHLSVLDNVMFGlkKLP-------KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK11288  75 AalaagVAIIYQELHLVPEMTVAENLYLG--QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQlfrvIRE-----LRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
5-222 2.71e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 86.26  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   5 TAAQANVLTIRQLSkqfGSRFAvhQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPA 84
Cdd:PRK15439 262 QAAGAPVLTVEDLT---GEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TA 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 EARNIGLVF-----QDYALFPHLSVLDNV---MFGLKKL---PKAQRqAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRV 152
Cdd:PRK15439 334 QRLARGLVYlpedrQSSGLYLDAPLAWNVcalTHNRRGFwikPAREN-AVLERYRRALNIKfNHAEQAARTLSGGNQQKV 412
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
12-222 2.89e-18

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.83  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSkqfGSRfaVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNIGL 91
Cdd:PRK10762 258 LKVDNLS---GPG--VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS---PQDGLANGI 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  92 VF--QDY---ALFPHLSVLDNV-----------MFGLKKlpKAQRQAVA-------------EQALQhvsmqhhlhsypy 142
Cdd:PRK10762 330 VYisEDRkrdGLVLGMSVKENMsltalryfsraGGSLKH--ADEQQAVSdfirlfniktpsmEQAIG------------- 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PLN03211 PLN03211
ABC transporter G-25; Provisional
13-226 3.27e-18

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 86.09  E-value: 3.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgsiqLEQQILWNEQQQIPAEARNIGLV 92
Cdd:PLN03211  70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 FQDYALFPHLSVLDNVMF-GLKKLPKAQRQAVAEQALQHVSMQHHL---------HSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLtkcentiigNSFIRGISGGERKRVSIAHEMLINP 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEAL-QIADQIILMHQGEIIQIG 226
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVL-TLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFG 289
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
31-222 2.17e-17

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: 80.21  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMF 110
Cdd:cd03248   34 SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLKKLPKAQRQAVAEQALQHVSMQHHLHSYpYT--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:cd03248  111 GLQSCSFECVKEAAQKAHAHSFISELASGY-DTevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 514971686 183 RQNTIEILKQtgtTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03248  190 QQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
11-223 2.42e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 83.13  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQipAEARNI 89
Cdd:PRK10762   4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKS--SQEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLSVLDNVM--------FGLKKLPKAQRQAvaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:PRK10762  82 GIIHQELNLIPQLTIAENIFlgrefvnrFGRIDWKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLF-RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
12-236 6.83e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 82.06  E-value: 6.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKT----TMLRLIagletPSSGSIQLEQQILWNEQQQIP 83
Cdd:PRK15134   6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPSGDIRFHGESLLH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 AEAR--------NIGLVFQD--YALFPhLSVLDNVMFGLKKLPKAQRQAVAE----QALQHVSMQH---HLHSYPYTLSG 146
Cdd:PRK15134  81 ASEQtlrgvrgnKIAMIFQEpmVSLNP-LHTLEKQLYEVLSLHRGMRREAARgeilNCLDRVGIRQaakRLTDYPHQLSG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
                        250
                 ....*....|
gi 514971686 227 TPKALYRQPA 236
Cdd:PRK15134 240 RAATLFSAPT 249
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
11-203 7.64e-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: 81.91  E-value: 7.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqqilwneqQQIPAEARNI 89
Cdd:TIGR03719   4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQPGIKV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   90 GLVFQDYALFPHLSVLDNVMFGLKKLPKAQR-----------------QAVAEQA-LQHVSMQHHLHSY----------- 140
Cdd:TIGR03719  71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaepdadfdKLAAEQAeLQEIIDAADAWDLdsqleiamdal 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686  141 ---PY-----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNtieiLKQTGTTTVIVTHD 203
Cdd:TIGR03719 151 rcpPWdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH----LQEYPGTVVAVTHD 217
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
21-254 1.70e-16

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: 78.74  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  21 FGSRFAVHQA------SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQ--IPAEAR-NI-- 89
Cdd:cd03291   41 FFSNLCLVGApvlkniNLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSwiMPGTIKeNIif 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYAlfpHLSVLDNVMF--GLKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03291  121 GVSYDEYR---YKSVVKACQLeeDITKFPEKDNTVLGEGGI--------------TLSGGQRARISLARAVYKDADLYLL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRQNTieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATlFAARY--FS 245
Cdd:cd03291  184 DSPFGYLDVFTEKEIFESC--VCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLmgYD 260

                 ....*....
gi 514971686 246 ALNEIPAQR 254
Cdd:cd03291  261 TFDQFSAER 269
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
37-225 1.93e-16

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 77.31  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLEQQILWNEqqqipaearniglvfqdyalfphLSVLDNVmfGLKK 114
Cdd:COG2401   56 GEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE-----------------------ASLIDAI--GRKG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQALqhVSMQHHLHSYPyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTG 194
Cdd:COG2401  111 DFKDAVELLNAVGL--SDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAG 187
                        170       180       190
                 ....*....|....*....|....*....|...
gi 514971686 195 TTTVIVTHDPE--EALQiADQIILMHQGEIIQI 225
Cdd:COG2401  188 ITLVVATHHYDviDDLQ-PDLLIFVGYGGVPEE 219
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
14-235 2.13e-16

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 80.53  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVF 93
Cdd:PRK10789 318 IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVS 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYP-------YTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK10789 396 QTPFLFSD-TVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDtevgergVMLSGGQKQRISIARALLLNAEILI 474
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNtieiLKQTGTT-TVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHN----LRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
36-220 2.32e-16

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: 77.37  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQiLWNEQQQIPAEARNIGLVfqDYAL----FPHLSVLDNVMFG 111
Cdd:cd03290   26 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSV--AYAAqkpwLLNATVEENITFG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 lKKLPKAQRQAVAEQAlqhvSMQHHLHSYPY-----------TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03290  103 -SPFNKQRYKAVTDAC----SLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTI-EILKQTGTTTVIVTHDpEEALQIADQIILMHQG 220
Cdd:cd03290  178 HLMQEGIlKFLQDDKRTLVLVTHK-LQYLPHADWIIAMKDG 217
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
30-222 2.44e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 79.96  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  30 ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGLVF------QDyALFPHLS 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIRAGIMLcpedrkAE-GIIPVHS 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNV---------MFGLKkLPKAQRQAVAEQALQHVSMQH-HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:PRK11288 348 VADNInisarrhhlRAGCL-INNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 174 LDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK11288 427 IDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
27-215 3.53e-16

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: 75.27  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilwneqqqIPAEArniglvfqdyalfphlsvld 106
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------------MPEGE-------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 107 NVMFglkkLPkaQR----QAVAEQALqhvsmqhhlhSYPY--TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03223   65 DLLF----LP--QRpylpLGTLREQL----------IYPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 514971686 181 QIRQntieILKQTGTTTVIVTHdPEEALQIADQII 215
Cdd:cd03223  129 RLYQ----LLKELGITVISVGH-RPSLWKFHDRVL 158
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
11-175 3.89e-16

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 76.00  E-value: 3.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ---QQIPAEAR 87
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG------EVLWQGEpirRQRDEYHQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NigLVFQDYA--LFPHLSVLDNVMFgLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK13538  75 D--LLYLGHQpgIKTELTALENLRF-YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
                        170
                 ....*....|
gi 514971686 166 LMDEPFSNLD 175
Cdd:PRK13538 152 ILDEPFTAID 161
hmuV PRK13547
heme ABC transporter ATP-binding protein;
11-233 4.82e-16

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 77.17  E-value: 4.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAG--LETPSSGSIQLEQQILWNEQ--QQIPAE- 85
Cdd:PRK13547   1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEplAAIDAPr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 --ARNIGLVFQDYALFPhLSVLDNVMFGlkKLPKAQRQA--------VAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK13547  81 laRLRAVLPQAAQPAFA-FSAREIVLLG--RYPHARRAGalthrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALA---------PKPQVLLMDEPFSNLD----HRLRDQIRQNTIEIlkQTGTTTVIvtHDPEEALQIADQIILMHQGEI 222
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDlahqHRLLDTVRRLARDW--NLGVLAIV--HDPNLAARHADRIAMLADGAI 233
                        250
                 ....*....|.
gi 514971686 223 IQIGTPKALYR 233
Cdd:PRK13547 234 VAHGAPADVLT 244
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
27-222 4.70e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 76.12  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETPSSGSIQLEQQ--ILWNEQQQIpaeARNIGLVFQD---YALFP 100
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvKIRNPQQAI---AQGIAMVPEDrkrDGIVP 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HLSVLDNVMF-------GLKKLPKAQRQAVAEQALQHVSMQHhlhSYPY----TLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13549 355 VMGVGKNITLaaldrftGGSRIDDAAELKTILESIQRLKVKT---ASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDE 431
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK13549 432 PTRGIDVGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
22-228 4.73e-15

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: 73.30  E-value: 4.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTM----LRLIagleTPSSGSIQLEQQILwneqQQIPAEA--RNIGLVFQD 95
Cdd:cd03244   15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDI----SKIGLHDlrSRISIIPQD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  96 YALFPhlsvlDNVMFGLKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTL-----------SGGEQQRVALARALAPKPQV 164
Cdd:cd03244   87 PVLFS-----GTIRSNLDPFGEYSDEEL-WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 165 LLMDEPFSNLDHRLrDQIRQNTIEiLKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTP 228
Cdd:cd03244  161 LVLDEATASVDPET-DALIQKTIR-EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
11-202 6.03e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 72.68  E-value: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARNIG 90
Cdd:PRK13540   1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTYQKQLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  91 LVFQDYALFPHLSVLDNVMFGLkklpKAQRQAVAEQALQHVSMQHHLHSYPY-TLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13540  78 FVGHRSGINPYLTLRENCLYDI----HFSPGAVGITELCRLFSLEHLIDYPCgLLSSGQKRQVALLRLWMSKAKLWLLDE 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTH 202
Cdd:PRK13540 154 PLVALDELSLLTI-ITKIQEHRAKGGAVLLTSH 185
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
27-222 6.18e-15

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: 76.02  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETPSSGSIQLEQQIL--WNEQQQIPAearNIGLVFQD---YALFP 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdiRNPAQAIRA---GIAMVPEDrkrHGIVP 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  101 HLSVLDNVMFG-LKKLPKAQR-QAVAEQALQHVSMQHhLH---SYPY----TLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR02633 353 ILGVGKNITLSvLKSFCFKMRiDAAAELQIIGSAIQR-LKvktASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 514971686  172 SNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:TIGR02633 432 RGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
40-262 6.29e-15

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 75.91  E-value: 6.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  40 ICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIGLVFQDYALFPHlSVLDNVMFGlkklpKAQ 119
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS--VLRQGVAMVQQDPVVLAD-TFLANVTLG-----RDI 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 120 RQAVAEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 189 ILKQtgTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQpatlfAARYFSALNeipAQRVAQQLQTC 262
Cdd:PRK10790 522 VREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA-----QGRYWQMYQ---LQLAGEELAAS 584
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
8-231 1.99e-14

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: 75.05  E-value: 1.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686     8 QANVLTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILwneqqqipa 84
Cdd:TIGR01257 1934 KTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSIL--------- 2004
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    85 eaRNIGLVFQDYALFPHLSVLDNVMFG---------LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:TIGR01257 2005 --TNISDVHQNMGYCPQFDAIDDLLTGrehlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686   156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
35-231 3.38e-14

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: 73.68  E-value: 3.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEqQQIPAEAR-----NIGLVFQDYALFPHLsvldnvm 109
Cdd:COG4615  356 RRGELVFIVGGNGSGKSTLAKLLTGLYRPESG------EILLDG-QPVTADNReayrqLFSAVFSDFHLFDRL------- 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 110 FGLKKLPKAQRqavAEQALQHVSMQHHLH------SypyT--LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDq 181
Cdd:COG4615  422 LGLDGEADPAR---ARELLERLELDHKVSvedgrfS---TtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR- 494
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 182 irqntI---EIL---KQTGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG4615  495 -----VfytELLpelKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAAL 544
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
11-235 5.49e-14

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 72.14  E-value: 5.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQqILWNE---QQQIP 83
Cdd:PRK15093   3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADR-MRFDDidlLRLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  84 AEAR-----NIGLVFQD--YALFPHLSVLDNVMfglKKLP----KAQ-------RQAVAEQALQHVSMQHH---LHSYPY 142
Cdd:PRK15093  81 RERRklvghNVSMIFQEpqSCLDPSERVGRQLM---QNIPgwtyKGRwwqrfgwRKRRAIELLHRVGIKDHkdaMRSFPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
                        250
                 ....*....|...
gi 514971686 223 IQIGTPKALYRQP 235
Cdd:PRK15093 238 VETAPSKELVTTP 250
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
26-228 5.60e-14

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: 70.13  E-value: 5.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALFP--- 100
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPLEDlrSSLTIIPQDPTLFSgti 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 --HLSVLDnvMFGLKKLPKAQRqaVAEQALQhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFSNL---- 174
Cdd:cd03369   99 rsNLDPFD--EYSDEEIYGALR--VSEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEATASIdyat 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 175 DHRLRDQIRQNTieilkqTGTTTVIVTHdpeeALQ-IA--DQIILMHQGEIIQIGTP 228
Cdd:cd03369  161 DALIQKTIREEF------TNSTILTIAH----RLRtIIdyDKILVMDAGEVKEYDHP 207
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
37-220 6.28e-14

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: 69.58  E-value: 6.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETpsSGSIqlEQQILWNEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFglkklp 116
Cdd:cd03232   33 GTLTALMGESGAGKTTLLDVLAGRKT--AGVI--TGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRF------ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 kaqrqavaeqalqhvsmqhhlHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIEILKQ---T 193
Cdd:cd03232  103 ---------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD----SQAAYNIVRFLKKladS 157
                        170       180
                 ....*....|....*....|....*...
gi 514971686 194 GTTTVIVTHDPEEAL-QIADQIILMHQG 220
Cdd:cd03232  158 GQAILCTIHQPSASIfEKFDRLLLLKRG 185
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
21-227 7.10e-14

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 73.41  E-value: 7.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    21 FGSRFAVH------QASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQ--IPAEARNIGLV 92
Cdd:TIGR01271  430 FFSNFSLYvtpvlkNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSwiMPGTIKDNIIF 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    93 FQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:TIGR01271  510 GLSYDEYRYTSVIKACQLeeDIALFPEKDKTVLGEGGI--------------TLSGGQRARISLARAVYKDADLYLLDSP 575
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686   171 FSNLDHRLRDQIRQNTieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGT 227
Cdd:TIGR01271  576 FTHLDVVTEKEIFESC--LCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGT 630
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
12-281 8.26e-14

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 71.48  E-value: 8.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQqILWNEQQ--QIPAE 85
Cdd:COG4170    4 LDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADR-FRWNGIDllKLSPR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  86 AR------NIGLVFQD--YALFPHLSVLDNVMFGLKKLP--------KAQRQAVAEQALQHVSMQHH---LHSYPYTLSG 146
Cdd:COG4170   82 ERrkiigrEIAMIFQEpsSCLDPSAKIGDQLIEAIPSWTfkgkwwqrFKWRKKRAIELLHRVGIKDHkdiMNSYPHELTE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLD-------HRLRDQIRQNtieilkqTGTTTVIVTHDPEEALQIADQIILMHQ 219
Cdd:COG4170  162 GECQKVMIAMAIANQPRLLIADEPTNAMEsttqaqiFRLLARLNQL-------QGTSILLISHDLESISQWADTITVLYC 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 220 GEIIQIGTPKALYRQP------ATLFAARYFSalNEIPAQrvaQQLQTCFGAHPISEALahhqePIRC 281
Cdd:COG4170  235 GQTVESGPTEQILKSPhhpytkALLRSMPDFR--QPLPHK---SRLNTLPGSIPPLQHL-----PIGC 292
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
40-203 1.28e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 72.07  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  40 ICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqqilwneqQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLKKL---- 115
Cdd:PRK11819  36 IGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVkaal 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 ------------PKAQRQAVA-EQA-LQHVsMQHH---------------LHSYPY-----TLSGGEQQRVALARALAPK 161
Cdd:PRK11819 103 drfneiyaayaePDADFDALAaEQGeLQEI-IDAAdawdldsqleiamdaLRCPPWdakvtKLSGGERRRVALCRLLLEK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 514971686 162 PQVLLMDEPFSNLDhrlrdqirQNTIEILKQ-----TGtTTVIVTHD 203
Cdd:PRK11819 182 PDMLLLDEPTNHLD--------AESVAWLEQflhdyPG-TVVAVTHD 219
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
27-231 2.31e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 71.90  E-value: 2.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaearniglvfqdyALFPHLSVLD 106
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ----------------AWIQNDSLRE 717
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   107 NVMFGLKKLPKAQRQAVAEQAL-QHVSM-----QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:TIGR00957  718 NILFGKALNEKYYQQVLEACALlPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 514971686   181 QIRQNTI---EILKqtGTTTVIVTHDPEEALQIaDQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR00957  798 HIFEHVIgpeGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
10-203 2.63e-13

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: 71.12  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNI 89
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------------GETVKL 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   90 GLVFQDY-ALFPHLSV-------LDNVMFGLKKLPkaQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARALAPK 161
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVweeisggLDIIKLGKREIP--SRAYVGRFNFKGSDQQKKVGQ----LSGGERNRVHLAKTLKSG 461
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 514971686  162 PQVLLMDEPFSNLD-HRLRdqirqnTIE--ILKQTGtTTVIVTHD 203
Cdd:TIGR03719 462 GNVLLLDEPTNDLDvETLR------ALEeaLLNFAG-CAVVISHD 499
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
12-234 2.83e-13

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 67.94  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLE-QQILwneqqQIPAEAR- 87
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKgEDIT-----DLPPEERa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 --NIGLVFQDYALFPhlsvldnvmfGlkklpkaqrqavaeqalqhVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03217   76 rlGIFLAFQYPPEIP----------G-------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLA 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDhrlRDQIRQ--NTIEILKQTGTTTVIVTHDPEEALQI-ADQIILMHQGEIIQIGtPKALYRQ 234
Cdd:cd03217  127 ILDEPDSGLD---IDALRLvaEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
26-234 3.41e-13

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 70.82  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHLSVL 105
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVALVSQNVHLF-NDTIA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 106 DNVMFGLK-KLPKAQRQAVAEQ--ALQHVS-MQHHLHSY----PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHR 177
Cdd:PRK11176 435 NNIAYARTeQYSREQIEEAARMayAMDFINkMDNGLDTVigenGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 178 LRDQIrQNTIEILKQTGTTTVIvTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK11176 515 SERAI-QAALDELQKNRTSLVI-AHR-LSTIEKADEILVVEDGEIVERGTHAELLAQ 568
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
27-225 1.35e-12

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 68.66  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGLVF-----QDYALFPH 101
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGMAYitesrRDNGFFPN 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 LSVLDNV-------------MFGLKKLPKAQRQAVAEQALQHVSMqHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK09700 356 FSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 169 EPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQI 225
Cdd:PRK09700 435 EPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
35-203 1.48e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 68.82  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAeaRNI-GLVFqDY------ALFPHL----S 103
Cdd:PRK11147  27 EDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPP--RNVeGTVY-DFvaegieEQAEYLkryhD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMF-----GLKKLpkAQRQAVAEQA--------LQHVSMQHHLHsyPYT----LSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11147 104 ISHLVETdpsekNLNEL--AKLQEQLDHHnlwqlenrINEVLAQLGLD--PDAalssLSGGWLRKAALGRALVSNPDVLL 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 167 MDEPFSNLDhrlrdqirQNTIE----ILKQTGTTTVIVTHD 203
Cdd:PRK11147 180 LDEPTNHLD--------IETIEwlegFLKTFQGSIIFISHD 212
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
36-215 1.92e-12

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: 66.28  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaEARNIGLVfqDYALFphlSVLDNvmfglkKL 115
Cdd:cd03237   24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI--KADYEGTV--RDLLS---SITKD------FY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 PKAQRQAVAEQALQhvsMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGT 195
Cdd:cd03237   91 THPYFKTEIAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEK 167
                        170       180
                 ....*....|....*....|
gi 514971686 196 TTVIVTHDPEEALQIADQII 215
Cdd:cd03237  168 TAFVVEHDIIMIDYLADRLI 187
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
37-175 2.27e-12

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 65.64  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaeARNIGLVFQDYALFPHLSVLDNVMFgLKKLP 116
Cdd:PRK13543  37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR-----SRFMAYLGHLPGLKADLSTLENLHF-LCGLH 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA-LAPKPqVLLMDEPFSNLD 175
Cdd:PRK13543 111 GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLD 169
PLN03130 PLN03130
ABC transporter C family member; Provisional
37-227 2.86e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 68.23  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   37 GQIICLLGHSGCGKTTMLRLIAG-LETPSSGSIQLEQQILWNEQqqipaearnIGLVFqdyalfpHLSVLDNVMFGLKKL 115
Cdd:PLN03130  643 GSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQ---------VSWIF-------NATVRDNILFGSPFD 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  116 PkaqrqAVAEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQ 184
Cdd:PLN03130  707 P-----ERYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 514971686  185 NTI-EILKqtGTTTVIVTHDPEEALQIaDQIILMHQGEIIQIGT 227
Cdd:PLN03130  782 KCIkDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGT 822
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
42-203 3.77e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 67.22  E-value: 3.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwneqqqiPAEarNIGLVFQDYALFPHLSVLDNVMFGLKKL--PKAQ 119
Cdd:PRK15064  32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNE--RLGKLRQDQFAFEEFTVLDTVIMGHTELweVKQE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 120 RQA--------------VAE------------------QALQHVSMQHHLHSYPYT-LSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK15064  99 RDRiyalpemseedgmkVADlevkfaemdgytaearagELLLGVGIPEEQHYGLMSeVAPGWKLRVLLAQALFSNPDILL 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 514971686 167 MDEPFSNLDhrlrdqIrqNTI----EILKQTGTTTVIVTHD 203
Cdd:PRK15064 179 LDEPTNNLD------I--NTIrwleDVLNERNSTMIIISHD 211
PLN03232 PLN03232
ABC transporter C family member; Provisional
35-239 3.90e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 68.08  E-value: 3.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   35 QRGQIICLLGHSGCGKTTMLRLIAG----LETPS---SGSIQLEQQILWneqqqipaearniglVFqdyalfpHLSVLDN 107
Cdd:PLN03232  641 PVGSLVAIVGGTGEGKTSLISAMLGelshAETSSvviRGSVAYVPQVSW---------------IF-------NATVREN 698
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  108 VMFGLKKLPKAQRQAVAEQALQHvsmqhHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:PLN03232  699 ILFGSDFESERYWRAIDVTALQH-----DLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686  177 RLRDQIRQNTI-EILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQpATLF 239
Cdd:PLN03232  774 HVAHQVFDSCMkDELK--GKTRVLVTNQ-LHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
10-223 4.39e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 67.22  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilWneqqqipAEARNI 89
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------W-------SENANI 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYAL-FPH-LSVLDnVMFGLKKlPKAQRQAV----------AEQALQHVSMqhhlhsypytLSGGEQQRVALARA 157
Cdd:PRK15064 385 GYYAQDHAYdFENdLTLFD-WMSQWRQ-EGDDEQAVrgtlgrllfsQDDIKKSVKV----------LSGGEKGRMLFGKL 452
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 158 LAPKPQVLLMDEPFSNLDhrlrdqirQNTIEIL-----KQTGtTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD--------MESIESLnmaleKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
44-204 4.97e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 64.12  E-value: 4.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  44 GHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE-ARNIGLVFQdyalfphLSVLDNVMFGLKKLPKAqrqA 122
Cdd:PRK13541  33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYiGHNLGLKLE-------MTVFENLKFWSEIYNSA---E 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 123 VAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTH 202
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL-NNLIVMKANSGGIVLLSSH 181

                 ..
gi 514971686 203 DP 204
Cdd:PRK13541 182 LE 183
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
87-202 7.12e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 66.98  E-value: 7.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   87 RNI-GLVFQDYALFpHLSVLDNVMFG-----LKKLPKAQRQAVAEQALQHVSMQHHLHSYPY--TLSGGEQQRVALARAL 158
Cdd:PTZ00265 1295 RNLfSIVSQEPMLF-NMSIYENIKFGkedatREDVKRACKFAAIDEFIESLPNKYDTNVGPYgkSLSGGQKQRIAIARAL 1373
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 514971686  159 APKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTH 202
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
143-226 1.34e-11

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: 62.73  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALA--PKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDpEEALQIADQIILM--- 217
Cdd:cd03238   87 TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQL-LEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpg 164
                         90
                 ....*....|..
gi 514971686 218 ---HQGEIIQIG 226
Cdd:cd03238  165 sgkSGGKVVFSG 176
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
17-203 1.35e-11

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: 65.58  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWnEQQQIPAEARniGLVfQDY 96
Cdd:COG1245  347 LTKSYGG-FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISY-KPQYISPDYD--GTV-EEF 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  97 ALFPHLSVLDNVMF--------GLKKLpkaqrqavaeqalqhvsmqhhLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:COG1245  422 LRSANTDDFGSSYYkteiikplGLEKL---------------------LDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 514971686 169 EPFSNLD--HRLR--DQIRQntieILKQTGTTTVIVTHD 203
Cdd:COG1245  481 EPSAHLDveQRLAvaKAIRR----FAENRGKTAMVVDHD 515
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
37-228 1.40e-11

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 63.93  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLE-QQILwneqqQIPAEAR---NIGLVFQDYALFPHLSVLDnvmF 110
Cdd:COG0396   26 GEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDgEDIL-----ELSPDERaraGIFLAFQYPVEIPGVSVSN---F 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 --------GLKKLPKAQRQAVAEQALQHVSM-QHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlRD 180
Cdd:COG0396   98 lrtalnarRGEELSAREFLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD---ID 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514971686 181 QIRQ--NTIEILKQTGTTTVIVTHDpEEALQI--ADQIILMHQGEIIQIGTP 228
Cdd:COG0396  175 ALRIvaEGVNKLRSPDRGILIITHY-QRILDYikPDFVHVLVDGRIVKSGGK 225
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
36-216 1.64e-11

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: 61.62  E-value: 1.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqIPAEARNIGLVFQdyalfphlsvldnvmfglkkl 115
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDGEDILEEVLDQ--------------------- 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   116 pkaqrqavaeqalqhvSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQN-----TIEIL 190
Cdd:smart00382  49 ----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLK 112
                          170       180
                   ....*....|....*....|....*.
gi 514971686   191 KQTGTTTVIVTHDPEEALQIADQIIL 216
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
11-222 1.91e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.20  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPS---SGSIQLEQQILwnEQQQIPA-EA 86
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVC--RFKDIRDsEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 RNIGLVFQDYALFPHLSVLDNVM-------FGLKKLPKAQRQAvaEQALQHVSmqhhLHSYPYTLSG----GEQQRVALA 155
Cdd:NF040905  78 LGIVIIHQELALIPYLSIAENIFlgnerakRGVIDWNETNRRA--RELLAKVG----LDESPDTLVTdigvGKQQLVEIA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDH----RLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQI-IL----------MHQG 220
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEedsaALLDLLLE-----LKAQGITSIIISHKLNEIRRVADSItVLrdgrtietldCRAD 226

                 ..
gi 514971686 221 EI 222
Cdd:NF040905 227 EV 228
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
143-254 3.82e-11

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: 64.65  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  143 TLSGGEQQRVALARALAPK-PQVL-LMDEPFSNLdHRlRDQIRQ-NTIEILKQTGTTTVIVTHDpEEALQIADQIILM-- 217
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGL-HQ-RDNRRLiNTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIgp 564
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 514971686  218 ----HQGEIIQIGTPKALYRQPATLfAARYFSALNEI--PAQR 254
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILANPDSL-TGQYLSGRKKIevPAER 606
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
17-203 4.73e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.06  E-value: 4.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQ-----QQIPAEA--RNI 89
Cdd:PRK13409 346 LTKKLGD-FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdYDGTVEDllRSI 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYALFPHLsvldNVMFGLKKLpkaqrqavaeqalqhvsmqhhLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13409 425 TDDLGSSYYKSEI----IKPLQLERL---------------------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514971686 170 PFSNLD--HRLR--DQIRQntieILKQTGTTTVIVTHD 203
Cdd:PRK13409 480 PSAHLDveQRLAvaKAIRR----IAEEREATALVVDHD 513
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
34-223 1.32e-10

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: 60.35  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  34 AQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIqlEQQILWN------EQQQIPAEarnIGLVFQDYALFPHLSVLDN 107
Cdd:cd03233   30 VKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSV--EGDIHYNgipykeFAEKYPGE---IIYVSEEDVHFPTLTVRET 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLKKlpkaqrqavaeQALQHVSmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:cd03233  104 LDFALRC-----------KGNEFVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 514971686 188 EILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEII 223
Cdd:cd03233  163 TMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
37-203 1.44e-10

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: 60.84  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilWNEqqqIPAEARniGLVFQDYalFPHLsvLDNVMFGLKK-- 114
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD--WDE---ILDEFR--GSELQNY--FTKL--LEGDVKVIVKpq 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 ----LPKAQRQAVAE------------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:cd03236   95 yvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
                        170       180
                 ....*....|....*....|....*
gi 514971686 179 RDQIRQnTIEILKQTGTTTVIVTHD 203
Cdd:cd03236  175 RLNAAR-LIRELAEDDNYVLVVEHD 198
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
143-226 1.59e-10

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: 60.35  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLL--MDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDpEEALQIADQIILM--- 217
Cdd:cd03270  137 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLI-ETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIgpg 214
                         90
                 ....*....|..
gi 514971686 218 ---HQGEIIQIG 226
Cdd:cd03270  215 agvHGGEIVAQG 226
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
14-223 1.70e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 62.05  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQQIPAEARNIGLVF 93
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  94 QDYALFPHLSVLDNVMFGL----------KKLPKAQRQAVAEQAL-----QHVSmqhhlhsypyTLSGGEQQRVALARAL 158
Cdd:PRK10982  80 QELNLVLQRSVMDNMWLGRyptkgmfvdqDKMYRDTKAIFDELDIdidprAKVA----------TLSVSQMQMIEIAKAF 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFT-IIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
10-175 1.98e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.06  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNI 89
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-------------GETVKL 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDY-ALFPHLSV-------LDNVMFGLKKLPkaQRQAVA-------EQAlQHVSMqhhlhsypytLSGGEQQRVAL 154
Cdd:PRK11819 390 AYVDQSRdALDPNKTVweeisggLDIIKVGNREIP--SRAYVGrfnfkggDQQ-KKVGV----------LSGGERNRLHL 456
                        170       180
                 ....*....|....*....|.
gi 514971686 155 ARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLD 477
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
31-202 7.67e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 60.81  E-value: 7.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQ-------QILWNEQQqipaearnIGLVFQDYALFPHlS 103
Cdd:PTZ00265  405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdiNLKWWRSK--------IGVVSQDPLLFSN-S 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  104 VLDNVMFGLKKLP-------------------------------------------------KAQRQAVAEQALQHVSMQ 134
Cdd:PTZ00265  476 IKNNIKYSLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemRKNYQTIKDSEVVDVSKK 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  135 HHLHSY---------------PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEILK-QTGTTTV 198
Cdd:PTZ00265  556 VLIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKgNENRITI 634

                  ....
gi 514971686  199 IVTH 202
Cdd:PTZ00265  635 IIAH 638
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
11-203 1.04e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.96  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSI----QLEqqILWNEQQQIpaea 86
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLE--VAYFDQHRA---- 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  87 rniglvfqdyALFPHLSVLDNVMFGLKKL-------------------PKAQRQAVAeqalqhvsmqhhlhsypyTLSGG 147
Cdd:PRK11147 393 ----------ELDPEKTVMDNLAEGKQEVmvngrprhvlgylqdflfhPKRAMTPVK------------------ALSGG 444
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 148 EQQRVALARALApKPQVLL-MDEPFSNLDhrlrdqirQNTIEILKQTGT----TTVIVTHD 203
Cdd:PRK11147 445 ERNRLLLARLFL-KPSNLLiLDEPTNDLD--------VETLELLEELLDsyqgTVLLVSHD 496
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
31-243 1.57e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.36  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNIG--LVFQD---YALFPHLSVL 105
Cdd:PRK10982 268 SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN---ANEAINHGfaLVTEErrsTGIYAYLDIG 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 106 DNVM----------FGL---KKLPKAQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:PRK10982 345 FNSLisnirnyknkVGLldnSRMKSDTQWVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 173 NLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRLASLH 490
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
10-226 1.81e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 58.59  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMlRLIAGLETPSSGSiQLEQQILWNEQQQipAEARNI 89
Cdd:NF000106  12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-RPWRF*TWCANRR--ALRRTI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GL-------VFQDYALFPHLSVLDNVMfglkKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:NF000106  88 G*hrpvr*gRRESFSGRENLYMIGR*L----DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEV-WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
PTZ00243 PTZ00243
ABC transporter; Provisional
27-235 2.50e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 59.02  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaearniglvfqdyALFPHLSVLD 106
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ----------------AWIMNATVRG 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  107 NVMF----GLKKLPKAQRQAVAEQALQHVS--MQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PTZ00243  740 NILFfdeeDAARLADAVRVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514971686  181 QIRQNTIeILKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PTZ00243  820 RVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTS 872
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
20-222 4.24e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 57.72  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  20 QFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGlETPSSGSIQLeqqILWNEQ----QQIPAEARNIGLV--- 92
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSNDL---TLFGRRrgsgETIWDIKKHIGYVsss 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  93 -FQDYALfpHLSVLDNVMFGL-------KKLPKAQRQaVAEQALQHVSMQHHLHSYPY-TLSGGeQQRVAL-ARALAPKP 162
Cdd:PRK10938 345 lHLDYRV--STSVRNVILSGFfdsigiyQAVSDRQQK-LAQQWLDILGIDKRTADAPFhSLSWG-QQRLALiVRALVKHP 420
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQ-IADQIILMHQGEI 222
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRR-FVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDGDI 481
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
35-221 5.33e-09

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: 57.87  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiQLEQQILWNEqqqipaearniglVFQDYA---LFPHLSVLDNvmfG 111
Cdd:COG1245   97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPSWDE-------------VLKRFRgteLQDYFKKLAN---G 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 LKK----------------------LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG1245  159 EIKvahkpqyvdlipkvfkgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLDhrlrdqIRQ-----NTIEILKQTGTTTVIVTHDpeeaLQI----ADQIILMHqGE 221
Cdd:COG1245  239 PSSYLD------IYQrlnvaRLIRELAEEGKYVLVVEHD----LAIldylADYVHILY-GE 288
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
17-221 5.73e-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: 54.89  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  17 LSKQFGSRFAVHQASwSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaearniglvfqdy 96
Cdd:cd03222    6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI-------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  97 alfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:cd03222   71 ----------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 514971686 177 RLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMhQGE 221
Cdd:cd03222  105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGE 148
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
11-247 6.38e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.83  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQIlwneqqqipAEARNI 89
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDM---------ADARHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  90 GLVFQDYA---------LFPHLSVLDNV-----MFGLkklPKAQRQAVAEQALQHVSMqhhlhsYPYT------LSGGEQ 149
Cdd:NF033858  72 RAVCPRIAympqglgknLYPTLSVFENLdffgrLFGQ---DAAERRRRIDELLRATGL------APFAdrpagkLSGGMK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLD--HR-----LRDQIRQntieilkQTGTTTVIV-THDPEEALQIaDQIILMHQGE 221
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDplSRrqfweLIDRIRA-------ERPGMSVLVaTAYMEEAERF-DWLVAMDAGR 214
                        250       260
                 ....*....|....*....|....*...
gi 514971686 222 IIQIGTPKALYRQ--PATLFAAryFSAL 247
Cdd:NF033858 215 VLATGTPAELLARtgADTLEAA--FIAL 240
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
143-254 6.54e-09

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 57.73  E-value: 6.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKpqvlLM------DEPFSNLdHRlRDQIR-QNTIEILKQTGTTTVIVTHDpEEALQIADQII 215
Cdd:COG0178  485 TLSGGEAQRIRLATQIGSG----LVgvlyvlDEPSIGL-HQ-RDNDRlIETLKRLRDLGNTVIVVEHD-EDTIRAADYII 557
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 514971686 216 LM------HQGEIIQIGTPKALYRQPATLfAARYFSALNEI--PAQR 254
Cdd:COG0178  558 DIgpgageHGGEVVAQGTPEEILKNPDSL-TGQYLSGRKRIpvPKKR 603
PLN03073 PLN03073
ABC transporter F family; Provisional
40-175 2.09e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.02  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  40 ICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqipaearnigLVFQDYalfpHLSVLD----NVMFGLKKL 115
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRM--------------AVFSQH----HVDGLDlssnPLLYMMRCF 599
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 PkaqrqAVAEQALQHvsmqhHLHSYP----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PLN03073 600 P-----GVPEQKLRA-----HLGSFGvtgnlalqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
ycf16 CHL00131
sulfate ABC transporter protein; Validated
10-227 4.24e-08

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 53.49  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGleTPSSgSIqLEQQILWNEQQ--QIPAEAR 87
Cdd:CHL00131   6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAY-KI-LEGDILFKGESilDLEPEER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 N---IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE---------QALQHVSM-QHHLHSYPYT-LSGGEQQRVA 153
Cdd:CHL00131  82 AhlgIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDplefleiinEKLKLVGMdPSFLSRNVNEgFSGGEKKRNE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDhrlRDQIRQ--NTIEILKQTGTTTVIVTHDPeEALQ--IADQIILMHQGEIIQIGT 227
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD---IDALKIiaEGINKLMTSENSIILITHYQ-RLLDyiKPDYVHVMQNGKIIKTGD 235
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
12-234 4.69e-08

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: 54.92  E-value: 4.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    12 LTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETpSSGSIQLEQqILWNE---QQQIPAea 86
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-VSWNSvtlQTWRKA-- 1293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    87 rnIGLVFQDYALF---------PHLSVLDNVMFglKKLPKAQRQAVAEQALQHVSMQhhLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR01271 1294 --FGVIPQKVFIFsgtfrknldPYEQWSDEEIW--KVAEEVGLKSVIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARS 1367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNtieiLKQT-GTTTVIVTHDPEEALQIADQIIL-----MHQGEIIQ-IGTPKA 230
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKT----LKQSfSNCTVILSEHRVEALLECQQFLViegssVKQYDSIQkLLNETS 1443

                   ....
gi 514971686   231 LYRQ 234
Cdd:TIGR01271 1444 LFKQ 1447
PLN03140 PLN03140
ABC transporter G family member; Provisional
37-251 4.73e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 55.24  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   37 GQIICLLGHSGCGKTTMLRLIAGLETpsSGSIQLEQQILWNEQQQiPAEARNIGLVFQDYALFPHLSVLDNVMFGL---- 112
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRESLIYSAflrl 982
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  113 -KKLPKAQRQAVAEQALQHV---SMQHHLHSYP--YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRdQIRQNT 186
Cdd:PLN03140  983 pKEVSKEEKMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA-AIVMRT 1061
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686  187 IEILKQTGTTTVIVTHDPE-EALQIADQIILMHQ-GEIIQIGTpkaLYRQPATLFaaRYFSALNEIP 251
Cdd:PLN03140 1062 VRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSGP---LGRNSHKII--EYFEAIPGVP 1123
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
11-222 4.98e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.79  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPaearn 88
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKlgYFAQHQLE----- 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  89 igLVFQDYALFPHLSVLdnvmfglkklpkaqrqavAEQALQHvSMQHHLHSYPYT----------LSGGEQQRVALARAL 158
Cdd:PRK10636 387 --FLRADESPLQHLARL------------------APQELEQ-KLRDYLGGFGFQgdkvteetrrFSGGEKARLVLALIV 445
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 159 APKPQVLLMDEPFSNLDHrlrdQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
143-215 6.05e-08

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: 52.61  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQ------RVALARALAPKPQVLLMDEPFSNLDhrlRDQIRQNTIEILK----QTGTTTVIVTHDpEEALQIAD 212
Cdd:cd03240  115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEerksQKNFQLIVITHD-EELVDAAD 190

                 ...
gi 514971686 213 QII 215
Cdd:cd03240  191 HIY 193
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
25-226 7.93e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 54.13  E-value: 7.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  25 FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilwneqqQIPAEARNIGLvfqDYALFPHLSV 104
Cdd:PRK13545  38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV------------DIKGSAALIAI---SSGLNGQLTG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNV-----MFGLKklpKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:PRK13545 103 IENIelkglMMGLT---KEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 514971686 180 DQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13545 180 KKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
37-204 2.38e-07

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: 52.44  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   37 GQIICLLGHSGCGKTTMLRLIAGLETPSSG--SIQLEQQILWNEQQqiPAEARNiglVFQDYALFPHlSVLDNVMFGLkk 114
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILGELWPVYGGrlTKPAKGKLFYVPQR--PYMTLG---TLRDQIIYPD-SSEDMKRRGL-- 549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  115 lpkaqRQAVAEQALQHVSMQHHLH---------SYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQN 185
Cdd:TIGR00954 550 -----SDKDLEQILDNVQLTHILEreggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
                         170
                  ....*....|....*....
gi 514971686  186 tieiLKQTGTTTVIVTHDP 204
Cdd:TIGR00954 625 ----CREFGITLFSVSHRK 639
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
142-231 4.42e-07

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: 51.94  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  142 YTLSGGEQQRVALARALAPK---PQVLLMDEPFSNLdHrlRDQIRQ--NTIEILKQTGTTTVIVTHDpEEALQIADQIIL 216
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL-H--FDDIKKllEVLQRLVDKGNTVVVIEHN-LDVIKTADYIID 903
                          90       100
                  ....*....|....*....|.
gi 514971686  217 M------HQGEIIQIGTPKAL 231
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTPEEV 924
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
136-234 5.51e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.17  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 136 HLHSYPYT-LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQI 214
Cdd:PRK10938 127 ALLDRRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE-LLASLHQSGITLVLVLNRFDEIPDFVQFA 205
                         90       100
                 ....*....|....*....|
gi 514971686 215 ILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK10938 206 GVLADCTLAETGEREEILQQ 225
uvrA PRK00349
excinuclease ABC subunit UvrA;
143-254 1.25e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALAralapkPQ-------VL-LMDEPFSNLdHRlRDQIRQ-NTIEILKQTGTTTVIVTHDpEEALQIADQ 213
Cdd:PRK00349 489 TLSGGEAQRIRLA------TQigsgltgVLyVLDEPSIGL-HQ-RDNDRLiETLKHLRDLGNTLIVVEHD-EDTIRAADY 559
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 514971686 214 IILM------HQGEIIQIGTPKALYRQPATLFAArYFSALNEI--PAQR 254
Cdd:PRK00349 560 IVDIgpgagvHGGEVVASGTPEEIMKNPNSLTGQ-YLSGKKKIevPKER 607
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
35-203 1.27e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.19  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiQLEQQILWNEqqqIPAEARniGLVFQDYalFPHLSvlDNvmfGLK- 113
Cdd:PRK13409  97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWDE---VLKRFR--GTELQNY--FKKLY--NG---EIKv 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 --------KLPKAQRQAVAE------------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:PRK13409 163 vhkpqyvdLIPKVFKGKVREllkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
                        170       180       190
                 ....*....|....*....|....*....|....
gi 514971686 174 LD--HRLR--DQIRqntiEILKqtGTTTVIVTHD 203
Cdd:PRK13409 243 LDirQRLNvaRLIR----ELAE--GKYVLVVEHD 270
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
143-254 1.64e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 50.21  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  143 TLSGGEQQRVALARALAPKPQ--VLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDpEEALQIADQIIL---- 216
Cdd:PRK00635  476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLIN-VIKKLRDQGNTVLLVEHD-EQMISLADRIIDigpg 553
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 514971686  217 --MHQGEIIQIGTPKALYRQPATLFAARYFSALN-EIPAQR 254
Cdd:PRK00635  554 agIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTiPIPEKR 594
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
37-226 2.37e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 49.72  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    37 GQIICLLGHSGCGKTTMLRLIAGlETPSSgSIQLEQQILWNEQQQIPAEARNIGLVF---QDYALFPHLSVLDNVMFGLK 113
Cdd:TIGR00956   87 GELTVVLGRPGSGCSTLLKTIAS-NTDGF-HIGVEGVITYDGITPEEIKKHYRGDVVynaETDVHFPHLTVGETLDFAAR 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   114 -KLPKAQRQAVAEQA----LQHVSMQHHLHSYPYT----------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:TIGR00956  165 cKTPQNRPDGVSREEyakhIADVYMATYGLSHTRNtkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 514971686   179 RDQIRQNTIEILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR00956  245 ALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIYFG 293
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
37-220 3.42e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 49.34  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686    37 GQIICLLGHSGCGKTTMLRLIAGLETpssGSIQLEQQILWNEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGL---- 112
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAylrq 865
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   113 -KKLPKAQRQAVAEQALQHVSMQhhlhSYPYTLSG--GE------QQRVALARALAPKPQVLL-MDEPFSNLDHRLRDQI 182
Cdd:TIGR00956  866 pKSVSKSEKMEYVEEVIKLLEME----SYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 514971686   183 RQnTIEILKQTGTTTVIVTHDPEEAL-QIADQIILMHQG 220
Cdd:TIGR00956  942 CK-LMRKLADHGQAILCTIHQPSAILfEEFDRLLLLQKG 979
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
12-231 3.50e-06

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: 47.93  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETpSSGSIQLEQqILWNeqqQIPAEA--R 87
Cdd:cd03289    3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-VSWN---SVPLQKwrK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  88 NIGLVFQDYALF---------PH--------LSVLDNVmfGLKklpkaqrqAVAEQALQHVSMQhhLHSYPYTLSGGEQQ 150
Cdd:cd03289   78 AFGVIPQKVFIFsgtfrknldPYgkwsdeeiWKVAEEV--GLK--------SVIEQFPGQLDFV--LVDGGCVLSHGHKQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQntieILKQT-GTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:cd03289  146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK----TLKQAfADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQ 221

                 ..
gi 514971686 230 AL 231
Cdd:cd03289  222 KL 223
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
36-203 5.42e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 46.54  E-value: 5.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  36 RGQIICLLGHSGCGKTTMLRLIA-GLETPSSGSIQLEQQILWneqqqIPAEARNIGLVFQ-------------DYALFPH 101
Cdd:COG0419   22 DDGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLIN-----VGSEEASVELEFEhggkryrierrqgEFAEFLE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 ---------------LSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSY-----PYTLSGGEQQRVALARALApk 161
Cdd:COG0419   97 akpserkealkrllgLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLS-- 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 514971686 162 pqvLLMDepFSNLDHRLRDQIrqntIEILKQTGtttvIVTHD 203
Cdd:COG0419  175 ---LILD--FGSLDEERLERL----LDALEELA----IITHV 203
PTZ00243 PTZ00243
ABC transporter; Provisional
145-239 5.69e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 48.62  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  145 SGGEQQRVALARALAPKPQ-VLLMDEPFSNLDHRLRDQIrQNTIeiLKQTGTTTVI-VTHDPEEALQIaDQIILMHQGEI 222
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQI-QATV--MSAFSAYTVItIAHRLHTVAQY-DKIIVMDHGAV 1522
                          90
                  ....*....|....*..
gi 514971686  223 IQIGTPKALYRQPATLF 239
Cdd:PTZ00243 1523 AEMGSPRELVMNRQSIF 1539
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
121-251 6.48e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 48.29  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  121 QAVAEQALQHVSMQHHLhsypYTLSGGEQQRVALARAL---APKPQVLLMDEPFSNL-DHRLRDQIrqNTIEILKQTGTT 196
Cdd:PRK00635  791 HALCSLGLDYLPLGRPL----SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhTHDIKALI--YVLQSLTHQGHT 864
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  197 TVIVTHDpEEALQIADQII-LMHQG--------------EIIQIGTPKALYRQPatlfaarYFSALNEIP 251
Cdd:PRK00635  865 VVIIEHN-MHVVKVADYVLeLGPEGgnlggyllascspeELIHLHTPTAKALRP-------YLSSPQELP 926
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
126-228 6.76e-06

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 46.84  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 126 QALQHVSMQH-HLHSYPYTLSGGEQQRVALARAL---APKPQVLLMDEPFSNLD-----------HRLRDQirqntieil 190
Cdd:cd03271  151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHfhdvkkllevlQRLVDK--------- 221
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 514971686 191 kqtGTTTVIVTHDpEEALQIADQIILM------HQGEIIQIGTP 228
Cdd:cd03271  222 ---GNTVVVIEHN-LDVIKCADWIIDLgpeggdGGGQVVASGTP 261
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
25-226 1.16e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 46.35  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  25 FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilwnEQQQIPAEARNIGLVFQdyalfphLSV 104
Cdd:PRK13546  38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD--------RNGEVSVIAISAGLSGQ-------LTG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNVMFGLKKLPKAQRQ--AVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEikAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 514971686 183 RQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13546 183 LDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
143-217 2.95e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 44.57  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQV----------LLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIAD 212
Cdd:cd03279  123 TLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAV-ATALELIRTENRMVGVISHVEELKERIPQ 201

                 ....*
gi 514971686 213 QIILM 217
Cdd:cd03279  202 RLEVI 206
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
12-256 4.16e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 45.55  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  12 LTIRQlskqfGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQ--QILWNEQQ----QIPA- 84
Cdd:PRK10636   7 LQIRR-----GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQEtpalPQPAl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  85 --------EARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK10636  82 eyvidgdrEYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDhrLRDQIRQNtiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ-IGTPKALYRQ 234
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD--LDAVIWLE--KWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEyTGNYSSFEVQ 237
                        250       260
                 ....*....|....*....|..
gi 514971686 235 PATLFAARyfSALNEIPAQRVA 256
Cdd:PRK10636 238 RATRLAQQ--QAMYESQQERVA 257
PLN03232 PLN03232
ABC transporter C family member; Provisional
143-239 7.18e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 44.97  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLrDQIRQNTI-EILKQtgTTTVIVTHDPEEALQiADQIILMHQGE 221
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIrEEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQ 1446
                          90
                  ....*....|....*...
gi 514971686  222 IIQIGTPKALYRQPATLF 239
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAF 1464
PLN03073 PLN03073
ABC transporter F family; Provisional
143-175 8.38e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 44.47  E-value: 8.38e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
144-234 1.40e-04

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: 44.17  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686   144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEilKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
                           90
                   ....*....|.
gi 514971686   224 QIGTPKALYRQ 234
Cdd:TIGR00957 1499 EFGAPSNLLQQ 1509
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
144-217 2.09e-04

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: 41.58  E-value: 2.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 144 LSGGEQQRVALARALA-----PKPQVLLmDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPEEALqIADQIILM 217
Cdd:cd03227   78 LSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHLPELAE-LADKLIHI 153
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
144-241 2.29e-04

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 42.20  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLdhrlrDQIRQNTIEILKQTG---TTTVIVTHDPEEALQiADQIILMHQG 220
Cdd:cd03288  157 FSVGQRQLFCLARAFVRKSSILIMDEATASI-----DMATENILQKVVMTAfadRTVVTIAHRVSTILD-ADLVLVLSRG 230
                         90       100
                 ....*....|....*....|.
gi 514971686 221 EIIQIGTPKALYRQPATLFAA 241
Cdd:cd03288  231 ILVECDTPENLLAQEDGVFAS 251
uvrA PRK00349
excinuclease ABC subunit UvrA;
143-228 2.38e-04

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQ---VLLMDEPFSNL---D--------HRLRDQirqntieilkqtGTTTVIVTHDpeeaL 208
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDirkllevlHRLVDK------------GNTVVVIEHN----L 893
                         90       100
                 ....*....|....*....|....*....
gi 514971686 209 QI---ADQIILM------HQGEIIQIGTP 228
Cdd:PRK00349 894 DViktADWIIDLgpeggdGGGEIVATGTP 922
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
143-228 2.68e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 43.09  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQ---VLLMDEPFSNL---D--------HRLRDQirqntieilkqtGTTTVIVTHDPeEAL 208
Cdd:COG0178  826 TLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDirkllevlHRLVDK------------GNTVVVIEHNL-DVI 892
                         90       100
                 ....*....|....*....|....*.
gi 514971686 209 QIADQIILM------HQGEIIQIGTP 228
Cdd:COG0178  893 KTADWIIDLgpeggdGGGEIVAEGTP 918
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
143-192 3.03e-04

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 39.14  E-value: 3.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686  143 TLSGGEQQR---VALARALA----------PKPQVLLMDEPFSNLDHRLRDQIrqntIEILKQ 192
Cdd:pfam13558  32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTA----LELLRA 90
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
112-232 4.51e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.51  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  112 LKKLpKAQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARAL--APK-PQVLLMDEPFSNLDHRLRDQIrQNTIE 188
Cdd:PRK00635 1673 LKKI-QKPLQALIDNGLGYLPLGQNLSS----LSLSEKIAIKIAKFLylPPKhPTLFLLDEIATSLDNQQKSAL-LVQLR 1746
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 514971686  189 ILKQTGTTTVIVTHDPeEALQIADQIILM------HQGEIIQIGTPKALY 232
Cdd:PRK00635 1747 TLVSLGHSVIYIDHDP-ALLKQADYLIEMgpgsgkTGGKILFSGPPKDIS 1795
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
284-352 1.05e-03

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 37.21  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686  284 RPHQVQVFSQPTtgAIPATVLSSSFMGHAEQLRLQLDPETIILAQVSPAQT---AYQEQVYVRLDLQQCFFF 352
Cdd:pfam08402   4 RPEKIRLAAAAN--GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHArppAPGDRVGLGWDPEDAHVL 73
GguA NF040905
sugar ABC transporter ATP-binding protein;
144-170 2.57e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 2.57e-03
                         10        20
                 ....*....|....*....|....*..
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
PLN03130 PLN03130
ABC transporter C family member; Provisional
145-240 3.66e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 39.34  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  145 SGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTI-EILKqtGTTTVIVTHDPEEALQiADQIILMHQGEII 223
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIrEEFK--SCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
                          90
                  ....*....|....*..
gi 514971686  224 QIGTPKALYRQPATLFA 240
Cdd:PLN03130 1452 EFDTPENLLSNEGSAFS 1468
PLN03140 PLN03140
ABC transporter G family member; Provisional
144-226 4.36e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 39.44  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686  144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPE-EALQIADQIILMHQGEI 222
Cdd:PLN03140  337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPApETFDLFDDIILLSEGQI 416

                  ....
gi 514971686  223 IQIG 226
Cdd:PLN03140  417 VYQG 420
 
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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