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Conserved domains on  [gi|384468733|gb|EIE53154|]
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polyamine ABC transporter, ATP-binding component, putative [Citreicella sp. 357]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-354 0e+00

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 512.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVN 80
Cdd:COG3842    1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG3842   81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETN 240
Cdd:COG3842  161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 241 LIEVPVLNISNGLAEVslpGGRAIQCPT--RLVDATQGVLSVRPERIDLCAPS-EADLIATAGAQVYLGTDIQLKAHLAG 317
Cdd:COG3842  241 LLPGTVLGDEGGGVRT---GGRTLEVPAdaGLAAGGPVTVAIRPEDIRLSPEGpENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 384468733 318 GEQMTVRLQNAAATVLPQsGARLGLRLEAGAARLLAA 354
Cdd:COG3842  318 GQELVVRVPNRAALPLEP-GDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-354 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 512.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVN 80
Cdd:COG3842    1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG3842   81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETN 240
Cdd:COG3842  161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 241 LIEVPVLNISNGLAEVslpGGRAIQCPT--RLVDATQGVLSVRPERIDLCAPS-EADLIATAGAQVYLGTDIQLKAHLAG 317
Cdd:COG3842  241 LLPGTVLGDEGGGVRT---GGRTLEVPAdaGLAAGGPVTVAIRPEDIRLSPEGpENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 384468733 318 GEQMTVRLQNAAATVLPQsGARLGLRLEAGAARLLAA 354
Cdd:COG3842  318 GQELVVRVPNRAALPLEP-GDRVGLSWDPEDVVVLPA 353
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 6-237 1.80e-140

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: 397.76  E-value: 1.80e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIG 237
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
4-285 1.09e-135

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 391.23  E-value: 1.09e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVF 83
Cdd:PRK09452  13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:PRK09452  93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 164 SALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIE 243
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 384468733 244 VPVL-NISNGLAEVSLPGGRAIQCPTRLVDATQGV-LSVRPERI 285
Cdd:PRK09452 253 ATVIeRLDEQRVRANVEGRECNIYVNFAVEPGQKLhVLLRPEDL 296
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 6-343 5.40e-121

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: 352.80  E-value: 5.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:TIGR03265  85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIevP 245
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL--P 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  246 VLNISNGLAEVslpGGRAIQC-PTRLVDATQGVLSVRPE--RIDLCAPSEADLIATAGAQVYLGTDIQLKAHLAGGEQMT 322
Cdd:TIGR03265 243 GTRGGGSRARV---GGLTLACaPGLAQPGASVRLAVRPEdiRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQA 319

                         330       340
                  ....*....|....*....|.
gi 384468733  323 VRlqnaaATVLPQSGARLGLR 343
Cdd:TIGR03265 320 LV-----ADVSASEVERLGIR 335
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
6-287 3.05e-89

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 271.95  E-value: 3.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTaLHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:NF040840   2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEvP 245
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIE-G 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 384468733 246 VLNISNGLAEVSLpGGRAIQCPTRLVDATQgvLSVRPERIDL 287
Cdd:NF040840 240 VAEKGGEGTILDT-GNIKIELPEEKKGKVR--IGIRPEDITI 278
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-164 1.99e-45

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: 152.42  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI--APLPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 MFGLQRLGWGVVDAEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
6-213 8.99e-45

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 152.95  E-value: 8.99e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFT----ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPpY------ 75
Cdd:NF038007   2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-Ysqkiil 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 -RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:NF038007  81 rRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQrETGIAFVFVTHdQEEALTMSDRIAVMSDGR 213
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTH-SDEASTYGNRIINMKDGK 217
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-200 1.06e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 115.41  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGediaplppyRRPVNTVFQHYAL---FP 90
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 hMTVLENVMFGL-QRLG-WGVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:NF040873  72 -LTVRDLVAMGRwARRGlWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 384468733 167 DLKLRQAVRMELKQIqRETGIAFVFVTHDQEEAL 200
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVR 183
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-226 3.18e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 95.19  E-value: 3.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE-----DIAPlppyRRPVNTVFQHYA 87
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDIAT----RRRVGYMSQAFS 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFPHMTVLENVM-----FGLQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:NF033858 350 LYGELTVRQNLElharlFHLPA-----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAfVFV-THDQEEALTmSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
5-225 1.14e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.41  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlppyRRPVNTVFQ 84
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYA---------LFPHMTVLENV-----MFGLqrlgwgvvDAEGRARQALELVH---LSAFLKRRPGQLSGGQQQRVALA 147
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLdffgrLFGQ--------DAAERRRRIDELLRatgLAPFADRPAGKLSGGMKQKLGLC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 148 RALAPEPRVLLLDEPLSALD-LKLRQAvrMEL-KQIQRETGIAFVFV-THDQEEALTMsDRIAVMSDGRVQQVGTPREIY 224
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDpLSRRQF--WELiDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225


                 .
gi 384468733 225 E 225
Cdd:NF033858 226 A 226
GguA NF040905
sugar ABC transporter ATP-binding protein;
13-213 2.81e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 79.83  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPvSG---GQIRLNGE-----DIAPlpPYRRPVNTVFQ 84
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEvcrfkDIRD--SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVD---AEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:NF040905  86 ELALIPYLSIAENIFLGNERAKRGVIDwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 162 PLSALD-------LKLrqavRMELKqiqrETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:NF040905 166 PTAALNeedsaalLDL----LLELK----AQGITSIIISHKLNEIRRVADSITVLRDGR 216
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
13-219 4.80e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 69.38  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCG--KTTLLRCI----AGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHy 86
Cdd:NF000106  21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*gpdAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRE- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 alfpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:NF000106 100 ----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 167 DLKLRQAVRMELKQIQREtGIAFVFVTHDQEEA------LTMSDRIAVMSDGRVQQVGT 219
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKT 233
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 31-208 2.04e-12

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: 64.32  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    31 NEFFTLLGPSGCGKTTLLRCIAGF-EPVSGGQIRLNGEDIaplppyrrpvntvfqhyalfphmtvlenvmfglqrlgwgv 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDI---------------------------------------- 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   110 vdaegraRQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME-----LKQIQRE 184
Cdd:smart00382  42 -------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 384468733   185 TGIAFVFVTHDQEEALTMSDRIAV 208
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
134-214 1.18e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 56.34  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 134 GQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLklrqAVRMELKQIQRE---TGIAFVFVTHDQEEALTMSDRIAVMS 210
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV----GAKYEIYTIINElaaEGKGVIVISSELPELLGMCDRIYVMN 478


                 ....
gi 384468733 211 DGRV 214
Cdd:NF040905 479 EGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-354 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 512.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVN 80
Cdd:COG3842    1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG3842   81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETN 240
Cdd:COG3842  161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 241 LIEVPVLNISNGLAEVslpGGRAIQCPT--RLVDATQGVLSVRPERIDLCAPS-EADLIATAGAQVYLGTDIQLKAHLAG 317
Cdd:COG3842  241 LLPGTVLGDEGGGVRT---GGRTLEVPAdaGLAAGGPVTVAIRPEDIRLSPEGpENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 384468733 318 GEQMTVRLQNAAATVLPQsGARLGLRLEAGAARLLAA 354
Cdd:COG3842  318 GQELVVRVPNRAALPLEP-GDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 6-351 2.16e-146

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 417.17  E-value: 2.16e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:COG3839    4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:COG3839   84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGE--TNLIE 243
Cdd:COG3839  164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 244 VPVLNisnglAEVSLpGGRAIQCPTRLVDATQG--VLSVRPERIDLCAPSEADLIATAGAQVYLGTDIQLKAHLaGGEQM 321
Cdd:COG3839  244 GTVEG-----GGVRL-GGVRLPLPAALAAAAGGevTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL-GGQEL 316

                        330       340       350
                 ....*....|....*....|....*....|
gi 384468733 322 TVRLqnaAATVLPQSGARLGLRLEAGAARL 351
Cdd:COG3839  317 VARV---PGDTRLRPGDTVRLAFDPERLHL 343
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 6-237 1.80e-140

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: 397.76  E-value: 1.80e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIG 237
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
4-285 1.09e-135

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 391.23  E-value: 1.09e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVF 83
Cdd:PRK09452  13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:PRK09452  93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 164 SALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIE 243
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 384468733 244 VPVL-NISNGLAEVSLPGGRAIQCPTRLVDATQGV-LSVRPERI 285
Cdd:PRK09452 253 ATVIeRLDEQRVRANVEGRECNIYVNFAVEPGQKLhVLLRPEDL 296
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 6-347 9.21e-128

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 369.86  E-value: 9.21e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI-APLPPYRRPVNTVFQ 84
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:COG1118   83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEV 244
Cdd:COG1118  163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 245 pvlNISNGLAEVslpGGRAIQCPTRLVDAtQGVLSVRPERIDLCAPSEADliATAGAQVY----LGTDIQLKAHLAGGEQ 320
Cdd:COG1118  243 ---RVIGGQLEA---DGLTLPVAEPLPDG-PAVAGVRPHDIEVSREPEGE--NTFPATVArvseLGPEVRVELKLEDGEG 313

                        330       340       350
                 ....*....|....*....|....*....|
gi 384468733 321 MTVRLQ---NAAATVLPQSGARLGLRLEAG 347
Cdd:COG1118  314 QPLEAEvtkEAWAELGLAPGDPVYLRPRPA 343
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 6-343 5.40e-121

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: 352.80  E-value: 5.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:TIGR03265  85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIevP 245
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL--P 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  246 VLNISNGLAEVslpGGRAIQC-PTRLVDATQGVLSVRPE--RIDLCAPSEADLIATAGAQVYLGTDIQLKAHLAGGEQMT 322
Cdd:TIGR03265 243 GTRGGGSRARV---GGLTLACaPGLAQPGASVRLAVRPEdiRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQA 319

                         330       340
                  ....*....|....*....|.
gi 384468733  323 VRlqnaaATVLPQSGARLGLR 343
Cdd:TIGR03265 320 LV-----ADVSASEVERLGIR 335
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 36-352 1.30e-113

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: 333.31  E-value: 1.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   36 LLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGR 115
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  116 ARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHD 195
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  196 QEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEvpVLNISNGLAEVSLPGGRAIQCPTR----LV 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFE--ATVIERKSEQVVLAGVEGRRCDIYtdvpVE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  272 DATQGVLSVRPERIDLCAPSEAD----LIATAGAQVYLGTDIQLKAHLAGG--EQMTVRLQNAAATVLPQSGARLGLRLE 345
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVIEEEDEANssnaIIGHVIDITYLGMTLEVHVRLETGqkVLVSEFFNEDDPHMSPSIGDRVGLTWH 318


                  ....*..
gi 384468733  346 AGAARLL 352
Cdd:TIGR01187 319 PGSEVVL 325
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 6-218 1.53e-111

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: 323.70  E-value: 1.53e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 6-238 1.00e-103

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: 304.65  E-value: 1.00e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGL--QRLGWGVVDAE--GRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:cd03296   83 YALFRHMTVFDNVAFGLrvKPRSERPPEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGE 238
Cdd:cd03296  163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 6-218 9.28e-101

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: 296.09  E-value: 9.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03301   81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03301  161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
6-348 2.04e-99

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 297.91  E-value: 2.04e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQ 84
Cdd:PRK11650   4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:PRK11650  84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGE--TNLI 242
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 243 EVpvlNISNGLAEVSLPGGRAIQCPT--RLVDATQGVLSVRPERIDLC-----APSEADLIATAGAQVYLGTDIqlkahl 315
Cdd:PRK11650 244 DG---RVSADGAAFELAGGIALPLGGgyRQYAGRKLTLGIRPEHIALSsaeggVPLTVDTVELLGADNLAHGRW------ 314

                        330       340       350
                 ....*....|....*....|....*....|...
gi 384468733 316 aGGEQMTVRLqnaAATVLPQSGARLGLRLEAGA 348
Cdd:PRK11650 315 -GGQPLVVRL---PHQERPAAGSTLWLHLPANQ 343
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-328 5.03e-99

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 297.90  E-value: 5.03e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQ 84
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:PRK11607  99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEv 244
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE- 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 245 pvlnisnGLAEVSLPGGRAIQCP-----------TRLVDATQGVLSVRPERIDLCAPSEADLIATAGAQV----YLGTDI 309
Cdd:PRK11607 258 -------GVLKERQEDGLVIDSPglvhplkvdadASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVihiaYLGDLS 330

                        330
                 ....*....|....*....
gi 384468733 310 QLKAHLAGGEQMTVRLQNA 328
Cdd:PRK11607 331 IYHVRLKSGQMISAQLQNA 349
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 3-228 1.45e-96

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 287.37  E-value: 1.45e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRp 78
Cdd:COG1116    5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 vnTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG1116   84 --VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSD--GRVQQ---VGTPR----EIYESPA 228
Cdd:COG1116  162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEeidVDLPRprdrELRTSPE 240
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 6-238 1.52e-93

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 281.21  E-value: 1.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTV 82
Cdd:COG1125    2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelRRRIGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHL--SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG1125   82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGE 238
Cdd:COG1125  162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 6-242 3.99e-93

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 277.84  E-value: 3.99e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733  166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLI 242
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 6-217 1.34e-92

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: 275.50  E-value: 1.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGT----FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlPPYRRPVnt 81
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRGY-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMS--DGRVQQV 217
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
6-240 3.54e-92

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 279.66  E-value: 3.54e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGL------QRLGWGVVDAegRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK10851  83 YALFRHMTVFDNIAFGLtvlprrERPNAAAIKA--KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGET 239
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240


                 .
gi 384468733 240 N 240
Cdd:PRK10851 241 N 241
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 6-241 1.86e-91

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: 273.44  E-value: 1.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTaLHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03299    1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03299   80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNL 241
Cdd:cd03299  160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
11-346 1.27e-90

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 276.14  E-value: 1.27e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFP 90
Cdd:PRK11000   9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 HMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:PRK11000  89 HLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 171 RQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIG--ETNLIEVPVLN 248
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLPVKVTA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 249 ISNGLAEVSLPGGRAIQCPtrlVDATqGV-------LSVRPERidLCAPSEADLIATAGAQVY--LGTDIQLKAHLAGGE 319
Cdd:PRK11000 249 TAIEQVQVELPNRQQVWLP---VEGR-GVqvganmsLGIRPEH--LLPSDIADVTLEGEVQVVeqLGNETQIHIQIPAIR 322

                        330       340
                 ....*....|....*....|....*..
gi 384468733 320 QMTVRLQNaaATVLPQSGARLGLRLEA 346
Cdd:PRK11000 323 QNLVYRQN--DVVLVEEGATFAIGLPP 347
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
6-287 3.05e-89

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 271.95  E-value: 3.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTaLHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:NF040840   2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEvP 245
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIE-G 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 384468733 246 VLNISNGLAEVSLpGGRAIQCPTRLVDATQgvLSVRPERIDL 287
Cdd:NF040840 240 VAEKGGEGTILDT-GNIKIELPEEKKGKVR--IGIRPEDITI 278
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
11-306 1.18e-87

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 267.74  E-value: 1.18e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFP 90
Cdd:PRK11432  12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 HMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:PRK11432  92 HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 171 RQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEVpvlNIS 250
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA---TLS 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 251 NGLAEVslpGGRAIQCP---TRLVDATQGVLSVRPERIDLCAPSEADLIATAGAQVYLG 306
Cdd:PRK11432 249 GDYVDI---YGYRLPRPaafAFNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMG 304
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 6-242 8.53e-86

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: 259.16  E-value: 8.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGgQIRLNGEDIAPLPP--YRRPVNT 81
Cdd:cd03295    1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRlIEPTSG-EIFIDGEDIREQDPveLRRKIGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHL--SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:cd03295   80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGET 239
Cdd:cd03295  160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239


                 ...
gi 384468733 240 NLI 242
Cdd:cd03295  240 RLL 242
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 6-353 1.21e-84

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.


Pssm-ID: 132302 [Multi-domain]  Cd Length: 362  Bit Score: 260.70  E-value: 1.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG--GQIRLNGEDIAPLPPYRRPVNTVF 83
Cdd:TIGR03258   6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   84 QHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  164 SALDLKLRQAVRMELKQIQRE-TGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLI 242
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  243 EVPVLNISN--GLAEVSLPGG--RAIQCPTRlvDATQGVLSVRPERIDLCAPS--EADLIATAGAQVYLGTDIQLKAHLA 316
Cdd:TIGR03258 246 PAIALGITEapGLVDVSCGGAviFAFGDGRH--DGRDKLACIRPEHLALTPRPagEGRFHATIASVEWHGAALHLLCDLD 323

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 384468733  317 GG--EQMTVRLQNAAATvLPQSGARLGLRLEAGAARLLA 353
Cdd:TIGR03258 324 AAcdEPMLVTMLRGRGP-APERGAKLALDCEADDAVLIE 361
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 5-237 1.42e-84

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 256.07  E-value: 1.42e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP----LPPYRRPVN 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdINKLRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQR-LGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:COG1126   81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIG 237
Cdd:COG1126  161 DEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 9-244 1.28e-82

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 256.18  E-value: 1.28e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   9 DRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTV 82
Cdd:COG4175   31 DEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrelRRKKMSMV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG4175  111 FQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 163 LSALD-LKLRQavrM--ELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGET 239
Cdd:COG4175  191 FSALDpLIRRE---MqdELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267


                 ....*
gi 384468733 240 NLIEV 244
Cdd:COG4175  268 DRSKV 272
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 9-236 1.91e-82

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: 251.79  E-value: 1.91e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   9 DRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTV 82
Cdd:cd03294   28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:cd03294  108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFI 236
Cdd:cd03294  188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 6-213 1.27e-77

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: 235.93  E-value: 1.27e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL----PPYRRPVNT 81
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGlqrlgwgvvdaegrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:cd03229   81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:cd03229  127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
4-214 4.35e-77

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 236.48  E-value: 4.35e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGT----FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP----- 74
Cdd:COG1136    3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelar 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 YRRpvNT---VFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALA 151
Cdd:COG1136   83 LRR--RHigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 152 PEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDqEEALTMSDRIAVMSDGRV 214
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 6-214 1.90e-75

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: 232.00  E-value: 1.90e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFG----TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------Y 75
Cdd:cd03255    1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALtMSDRIAVMSDGRV 214
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-227 3.95e-75

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: 240.58  E-value: 3.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRF-----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP----- 73
Cdd:COG1123  259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrslr 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  74 PYRRPVNTVFQH--YALFPHMTVLENVMFGLQRLGWG-VVDAEGRARQALELVHLSA-FLKRRPGQLSGGQQQRVALARA 149
Cdd:COG1123  339 ELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARA 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:COG1123  419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 10-262 1.07e-74

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: 234.61  E-value: 1.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  10 RVEKRFGTFTaLHgVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE---DIAP---LPPYRRPVNTVF 83
Cdd:COG4148    6 DFRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRRRIGYVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFGLQRLGwgvvDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:COG4148   84 QEARLFPHLSVRGNLLYGRKRAP----RAERRISfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNL 241
Cdd:COG4148  160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSV 239

                        250       260
                 ....*....|....*....|...
gi 384468733 242 IEVPVL--NISNGLAEVSLPGGR 262
Cdd:COG4148  240 LEATVAahDPDYGLTRLALGGGR 262
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 13-244 5.51e-74

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: 233.21  E-value: 5.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTVFQHY 86
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   87 ALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733  167 DLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEV 244
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQV 238
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-236 1.65e-73

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 227.55  E-value: 1.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-----PY 75
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHYALFPHMTVLENVMFGLQRLGwGVVDAE--GRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPE 153
Cdd:COG1127   81 RRRIGMLFQGGALFDSLTVFENVAFPLREHT-DLSEAEirELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 154 PRVLLLDEPLSALD-LKLRQAVRMeLKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPaNRFV 232
Cdd:COG1127  160 PEILLYDEPTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWV 237


                 ....
gi 384468733 233 ADFI 236
Cdd:COG1127  238 RQFL 241
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 10-218 5.87e-73

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: 225.25  E-value: 5.87e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  10 RVEKRFGTFTAlhGVSVDIaDNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNG------EDIAPLPPYRRPVNTVF 83
Cdd:cd03297    5 DIEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFGLQRLGWGVVdaEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:cd03297   82 QQYALFPHLNVRENLAFGLKRKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 164 SALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03297  160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 6-214 1.10e-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: 222.02  E-value: 1.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPYRRPVNT 81
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGL-QRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03262  161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
6-238 4.60e-71

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 221.17  E-value: 4.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTaLHgVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:COG3840    2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQ---RLgwgvvDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG3840   80 NNLFPHLTVAQNIGLGLRpglKL-----TAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGE 238
Cdd:COG3840  155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 6-229 8.35e-71

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: 221.22  E-value: 8.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGT----FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPV 79
Cdd:COG1124    2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHY--ALFPHMTVLENVMFGLQRLGwgVVDAEGRARQALELVHL-SAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:COG1124   82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 157 LLLDEPLSALDLklrqAVRME----LKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPAN 229
Cdd:COG1124  160 LLLDEPTSALDV----SVQAEilnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
6-226 6.30e-70

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 218.39  E-value: 6.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVFQ 84
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFgLQRL-GWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:COG1131   81 EPALYPDLTVRENLRF-FARLyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 164 SALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:COG1131  160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
6-245 1.13e-68

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 218.79  E-value: 1.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-----YR 76
Cdd:COG1135    2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 RPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:COG1135   82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 157 LLLDEPLSALD-------LKLrqavrmeLKQIQRETGIAFVFVTHDqeealtMS------DRIAVMSDGRVQQVGTPREI 223
Cdd:COG1135  162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228

                        250       260
                 ....*....|....*....|..
gi 384468733 224 YESPANRFVADFIGETNLIEVP 245
Cdd:COG1135  229 FANPQSELTRRFLPTVLNDELP 250
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-223 1.83e-68

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 214.92  E-value: 1.83e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-----YRR 77
Cdd:COG3638    1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 PVNTVFQHYALFPHMTVLENVMFGlqRLG--------WGVVDAEGR--ARQALELVHLSAFLKRRPGQLSGGQQQRVALA 147
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNVLAG--RLGrtstwrslLGLFPPEDRerALEALERVGLADKAYQRADQLSGGQQQRVAIA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 148 RALAPEPRVLLLDEPLSALDLKLRQAVrME-LKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG3638  159 RALVQEPKLILADEPVASLDPKTARQV-MDlLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 6-225 4.32e-68

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: 213.35  E-value: 4.32e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI--APLPPYRRPVNTV 82
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQH--YALFpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG1122   81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 4-228 4.85e-67

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: 211.82  E-value: 4.85e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP----V 79
Cdd:COG0411    3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgiA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTvFQHYALFPHMTVLENVMFGLQ-RLGWGVV--------------DAEGRARQALELVHLSAFLKRRPGQLSGGQQQRV 144
Cdd:COG0411   83 RT-FQNPRLFPELTVLENVLVAAHaRLGRGLLaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRRL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 145 ALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:COG0411  162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241


                 ....
gi 384468733 225 ESPA 228
Cdd:COG0411  242 ADPR 245
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 6-235 2.57e-66

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 209.28  E-value: 2.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-----RRPVN 80
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlRRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQ---RLGWGVVDAegRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVL 157
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPLRehtRLSEEEIRE--IVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 158 LLDEPLSALDlKLRQAVRMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPaNRFVADF 235
Cdd:cd03261  159 LYDEPTAGLD-PIASGVIDDLiRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 5-223 5.51e-66

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: 208.74  E-value: 5.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTV 82
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRreLARRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQ--RLGWGVVDAEGR--ARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRYphLGLFGRPSAEDReaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG1120  161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-218 5.85e-65

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: 205.43  E-value: 5.85e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-----PY 75
Cdd:cd03257    1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHY--ALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHL---SAFLKRRPGQLSGGQQQRVALARAL 150
Cdd:cd03257   81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 151 APEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
20-228 8.42e-65

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: 8.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlPPYRRPVntVFQHYALFPHMTVLENVM 99
Cdd:COG4525   22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDNVA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 100 FGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELK 179
Cdd:COG4525   99 FGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 180 QIQRETGIAFVFVTHDQEEALTMSDRIAVMSD--GRVQQV------------GTPREIYESPA 228
Cdd:COG4525  179 DVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERleldfsrrflagEDARAIKSDPA 241
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 6-228 2.13e-64

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: 204.21  E-value: 2.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP---VNTV 82
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQR------LGWGVVDAEG----RARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:cd03219   81 FQIPRLFPELTVLENVMVAAQArtgsglLLARARREEReareRAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:cd03219  161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-218 6.55e-63

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 199.89  E-value: 6.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGT-FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL-----PPYRRP 78
Cdd:COG2884    1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPYLRRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG2884   81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 159 LDEPLSALDLKLRQAVrMEL-KQIQReTGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:COG2884  161 ADEPTGNLDPETSWEI-MELlEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 5-227 7.28e-63

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: 200.11  E-value: 7.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGT----FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI-----APLPPY 75
Cdd:cd03258    1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
5-236 1.35e-62

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 199.93  E-value: 1.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPYRRPVN 80
Cdd:PRK09493   1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkVDERLIRQEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFG-LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK09493  81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFI 236
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 20-213 4.43e-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: 197.30  E-value: 4.43e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQH--YALFpHMTVL 95
Cdd:cd03225   16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkeLRRKVGLVFQNpdDQFF-GPTVE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVR 175
Cdd:cd03225   95 EEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 384468733 176 MELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:cd03225  175 ELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 6-223 4.14e-61

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: 195.48  E-value: 4.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF------EPVSGgQIRLNGEDIAPLPP----Y 75
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEG-EVLLDGKDIYDLDVdvleL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHYALFPhMTVLENVMFGLQRLG-WGVVDAEGRARQALELVHLSAFLKRR--PGQLSGGQQQRVALARALAP 152
Cdd:cd03260   80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03260  159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-228 1.03e-59

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 200.13  E-value: 1.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRF--GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG---GQIRLNGEDIAPLPPYRRP 78
Cdd:COG1123    3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 --VNTVFQH--YALFPhMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:COG1123   83 rrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:COG1123  162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 6-225 2.98e-59

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: 191.24  E-value: 2.98e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGT-FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-----YRRPV 79
Cdd:cd03256    1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHYALFPHMTVLENVMFGlqRLG--------WGVVDAEG--RARQALELVHLSAFLKRRPGQLSGGQQQRVALARA 149
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSG--RLGrrstwrslFGLFPKEEkqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:cd03256  159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 18-224 2.24e-58

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: 189.97  E-value: 2.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP-----LPPYRRPVNTVFQH--YALFp 90
Cdd:TIGR04521  18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDLRKKVGLVFQFpeHQLF- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   91 HMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:TIGR04521  97 EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733  170 LRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-214 3.49e-58

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 187.33  E-value: 3.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVF 83
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPhMTVLENVMFGLQrLGWGVVDAEgRARQALELVHLSA-FLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG4619   81 QEPALWG-GTVRDNLPFPFQ-LRERKFDRE-RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:COG4619  158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 10-264 1.15e-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: 188.01  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   10 RVEKRFGTFTAlhGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP------LPPYRRPVNTVF 83
Cdd:TIGR02142   4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   84 QHYALFPHMTVLENVMFGLQRlgwgVVDAEGRARQA--LELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:TIGR02142  82 QEARLFPHLSVRGNLRYGMKR----ARPSERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVA-DFIGETN 240
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLArEDQGSLI 237

                         250       260
                  ....*....|....*....|....
gi 384468733  241 LIEVPVLNISNGLAEVSLPGGRAI 264
Cdd:TIGR02142 238 EGVVAEHDQHYGLTALRLGGGHLW 261
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 5-228 2.07e-56

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: 186.41  E-value: 2.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP---VSGGQIRLNGEDIAPLPP--- 74
Cdd:COG0444    1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEkel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 --YR-RPVNTVFQH-Y-ALFPHMTVLENVMFGLQR-LGWGVVDAEGRARQALELVHLS---AFLKRRPGQLSGGQQQRVA 145
Cdd:COG0444   81 rkIRgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 146 LARALAPEPRVLLLDEPLSALDLKLR-QAVRMeLKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:COG0444  161 IARALALEPKLLIADEPTTALDVTIQaQILNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239


                 ....
gi 384468733 225 ESPA 228
Cdd:COG0444  240 ENPR 243
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 6-214 2.07e-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: 2.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVFQ 84
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVmfglqrlgwgvvdaegrarqalelvhlsaflkrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd03230   81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 165 ALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 5-225 3.60e-56

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: 183.14  E-value: 3.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVF 83
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENV-MFGLQRLGWGVvDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG4555   81 DERGLYDRLTVRENIrYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 163 LSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG4555  160 TNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 1-216 4.30e-56

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: 182.63  E-value: 4.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-- 74
Cdd:COG4181    4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEda 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 ----YRRPVNTVFQHYALFPHMTVLENVMFGLQRLGwgVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARAL 150
Cdd:COG4181   84 rarlRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 151 APEPRVLLLDEPLSALDLKLRQAVrMEL-KQIQRETGIAFVFVTHDQEEALtMSDRIAVMSDGRVQQ 216
Cdd:COG4181  162 ATEPAILFADEPTGNLDAATGEQI-IDLlFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVE 226
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-228 5.75e-56

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 182.98  E-value: 5.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLppyRRPVN 80
Cdd:COG1121    2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYAL---FPhMTVLENVMFGLQ-RLGW----GVVDAEgRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:COG1121   79 YVPQRAEVdwdFP-ITVRDVVLMGRYgRRGLfrrpSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQvGTPREIYESPA 228
Cdd:COG1121  157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 5-245 1.24e-54

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 182.31  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-----Y 75
Cdd:PRK11153   1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:PRK11153  81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADF 235
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240

                        250
                 ....*....|
gi 384468733 236 IGETNLIEVP 245
Cdd:PRK11153 241 IQSTLHLDLP 250
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 4-236 5.87e-54

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 177.92  E-value: 5.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRC-------IAGFEpVSGgQIRLNGEDI----APL 72
Cdd:COG1117   10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR-VEG-EILLDGEDIydpdVDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  73 PPYRRPVNTVFQHYALFPhMTVLENVMFGLQRLGW---GVVDAegRARQALELVHL----SAFLKRRPGQLSGGQQQRVA 145
Cdd:COG1117   88 VELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkskSELDE--IVEESLRKAALwdevKDRLKKSALGLSGGQQQRLC 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 146 LARALAPEPRVLLLDEPLSALD----LKLRQAVRmELKQiqrETGIafVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPR 221
Cdd:COG1117  165 IARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK---DYTI--VIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238

                        250
                 ....*....|....*
gi 384468733 222 EIYESPANRFVADFI 236
Cdd:COG1117  239 QIFTNPKDKRTEDYI 253
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
5-236 1.44e-53

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 176.91  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIApLPPYR----RPVN 80
Cdd:COG4598    8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIR-LKPDRdgelVPAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 T------------VFQHYALFPHMTVLENVMFG-LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALA 147
Cdd:COG4598   87 RrqlqrirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 148 RALAPEPRVLLLDEPLSALDLKLRQAVrmeLKQIQR--ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG4598  167 RALAMEPEVMLFDEPTSALDPELVGEV---LKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243

                        250
                 ....*....|.
gi 384468733 226 SPANRFVADFI 236
Cdd:COG4598  244 NPKSERLRQFL 254
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 5-230 3.20e-53

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: 175.56  E-value: 3.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFT-ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP-----LPPYRRP 78
Cdd:TIGR02315   1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   79 VNTVFQHYALFPHMTVLENVMFGlqRLG--------WGVVDAEG--RARQALELVHLSAFLKRRPGQLSGGQQQRVALAR 148
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHG--RLGykptwrslLGRFSEEDkeRALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  149 ALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238


                  ..
gi 384468733  229 NR 230
Cdd:TIGR02315 239 RH 240
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 20-228 1.55e-52

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 176.46  E-value: 1.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-----PYRRPVNTVFQH-YA-LFPHM 92
Cdd:COG4608   33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrelrPLRRRMQMVFQDpYAsLNPRM 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFGL--QRLGwGVVDAEGRARQALELVHLSA-FLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:COG4608  113 TVGDIIAEPLriHGLA-SKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 170 LR-QAVRMeLKQIQRETGIAFVFVTHDqeeaLTM----SDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:COG4608  192 IQaQVLNL-LEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPL 250
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 5-236 1.82e-52

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: 174.02  E-value: 1.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-EPVSG----GQIRLNGEDI----APLPPY 75
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPGvrieGKVLFDGQDIydkkIDVVEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   76 RRPVNTVFQHYALFPhMTVLENVMFGLQRlgWGVVD---AEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALAR 148
Cdd:TIGR00972  81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRL--HGIKDkkeLDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQQRLCIAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  149 ALAPEPRVLLLDEPLSALD----LKLRQAVRmELKQiqretGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDpiatGKIEELIQ-ELKK-----KYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231

                         250
                  ....*....|..
gi 384468733  225 ESPANRFVADFI 236
Cdd:TIGR00972 232 TNPKEKRTEDYI 243
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
6-216 2.12e-52

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 174.12  E-value: 2.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlPPYRRPVntVFQH 85
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK11248  79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMS--DGRVQQ 216
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 21-206 8.23e-52

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 171.13  E-value: 8.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF--EPVSG-GQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLEN 97
Cdd:COG4136   17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQRlGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:COG4136   97 LAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175

                        170       180
                 ....*....|....*....|....*....
gi 384468733 178 LKQIQRETGIAFVFVTHDQEEALTMSDRI 206
Cdd:COG4136  176 VFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 6-223 9.66e-52

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: 171.08  E-value: 9.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP---VNTV 82
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQRLGwgvvdaEGRARQALELVH-----LSAFLKRRPGQLSGGQQQRVALARALAPEPRVL 157
Cdd:cd03224   81 PEGRRIFPELTVEENLLLGAYARR------RAKRKARLERVYelfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 158 LLDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03224  155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 21-230 1.50e-51

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: 171.11  E-value: 1.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRpvnTVFQHYALFPHMTVLENVMF 100
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  101 GLQRLGWGVVDAEGRA--RQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMEL 178
Cdd:TIGR01184  78 AVDRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 384468733  179 KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGtprEIYESPANR 230
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVPFPR 206
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 7-218 1.97e-51

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: 168.77  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   7 SIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPvntvfQHY 86
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-----RKI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALFPhmtvlenvmfglqrlgwgvvdaegrarQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:cd03214   76 AYVP---------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468733 167 DLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03214  129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
25-214 3.15e-51

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 170.15  E-value: 3.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  25 SVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLENVMFGLQ- 103
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 104 --RLgwgvvDAEGRA--RQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELK 179
Cdd:PRK10771  99 glKL-----NAAQREklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 384468733 180 QIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 6-214 3.92e-51

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: 169.21  E-value: 3.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTfTALHgVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03298    1 VRLDKIRFSYGE-QPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENVMFGLQ-RLGWGVVDaEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd03298   79 NNLFAHLTVEQNVGLGLSpGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03298  158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 6-223 4.02e-50

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


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 166.91  E-value: 4.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFG--TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-RRPVNTV 82
Cdd:cd03263    1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFgLQRLgWGVVDAEGRARQA--LELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:cd03263   81 PQFDALFDELTVREHLRF-YARL-KGLPKSEIKEEVEllLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETgiAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03263  159 EPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 4-228 7.98e-50

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: 166.70  E-value: 7.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP---VN 80
Cdd:COG0410    2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVmfglqRLGWGVVDAEGRARQALELVH-----LSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:COG0410   82 YVPEGRRIFPSLTVEENL-----LLGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:COG0410  157 LLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 25-218 1.93e-49

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 165.03  E-value: 1.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   25 SVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLENVMFGLQ- 103
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHp 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  104 RLGWGVVDAEgRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQR 183
Cdd:TIGR01277  98 GLKLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 384468733  184 ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
5-219 4.55e-49

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 171.74  E-value: 4.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP---YRRPVNT 81
Cdd:COG1129    4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGLQRLGWGVVD---AEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG1129   84 IHQELNLVPNLSVAENIFLGREPRRGGLIDwraMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 159 LDEPLSALDlklRQAVRMELKQIQ--RETGIAFVFVTHDQEEALTMSDRIAVMSDGRVqqVGT 219
Cdd:COG1129  164 LDEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 20-224 5.13e-49

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: 165.68  E-value: 5.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGgQIRLNGEDIAP---LPPYRRPVNTVFQHyalfPH---- 91
Cdd:TIGR04520  17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGlLLPTSG-KVTVDGLDTLDeenLWEIRKKVGMVFQN----PDnqfv 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   92 -MTVLENVMFGLQRLGwgVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:TIGR04520  92 gATVEDDVAFGLENLG--VPREEMRKRvdEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733  169 KLRQAVRMELKQIQRETGIAFVFVTHDQEEALtMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:TIGR04520 170 KGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIF 224
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 14-209 2.13e-48

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: 162.32  E-value: 2.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLPPYRRPVNTVFQHYAL---FP 90
Cdd:cd03235    8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 hMTVLENVMFGL-QRLGW-GVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:cd03235   85 -ISVRDVVLMGLyGHKGLfRRLSKADKAKvdEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 384468733 167 DLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVM 209
Cdd:cd03235  164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 5-213 2.73e-48

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: 162.03  E-value: 2.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGT-FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL-----PPYRRP 78
Cdd:TIGR02673   1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrqlPLLRRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   79 VNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:TIGR02673  81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733  159 LDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 13-227 6.90e-48

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 169.09  E-value: 6.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPvSGGQIRLNGEDIAPLP-----PYRRPVNTVFQH-Y 86
Cdd:COG4172  294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpF 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 A-LFPHMTVLENVMFGL--QRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG4172  373 GsLSPRMTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:COG4172  453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 7-213 7.92e-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: 158.95  E-value: 7.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   7 SIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVNTVFQ 84
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAklPLEELRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 hyalfphmtvlenvmfglqrlgwgvvdaegrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd00267   81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 384468733 165 ALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:cd00267  110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 5-199 1.30e-47

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: 159.95  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVF 83
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFgLQRLgWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:COG4133   82 HADGLKPELTVRENLRF-WAAL-YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 384468733 164 SALDlklRQAVRMELKQIQ--RETGIAFVFVTHDQEEA 199
Cdd:COG4133  160 TALD---AAGVALLAELIAahLARGGAVLLTTHQPLEL 194
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
6-222 2.42e-47

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 161.05  E-value: 2.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY----RRPVnt 81
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRAV-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYAL-FPhMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALA-------PE 153
Cdd:COG4559   80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 154 PRVLLLDEPLSALDLKLRQAVrMEL-KQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:COG4559  159 PRWLFLDEPTSALDLAHQHAV-LRLaRQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 6-236 3.20e-47

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 160.18  E-value: 3.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE-----------DIAPLpp 74
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIREL-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 yRRPVNTVFQHYALFPHMTVLENVMFGLQR-LGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPE 153
Cdd:PRK11124  81 -RRNVGMVFQQYNLWPHLTVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 154 PRVLLLDEPLSALDLKLRQAVRMELKQIQrETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTpREIYESPANRFVA 233
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237


                 ...
gi 384468733 234 DFI 236
Cdd:PRK11124 238 NYL 240
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
6-236 3.64e-46

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 157.48  E-value: 3.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE--------DIAPLPPYRR 77
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 PVNTVFQHYALFPHMTVLENVMFG-LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 157 LLLDEPLSALDLKLRQAVRMELKQIQrETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTpREIYESPANRFVADFI 236
Cdd:COG4161  163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
6-244 5.31e-46

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 161.35  E-value: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPV 79
Cdd:PRK10070  29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGET 239
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268


                 ....*
gi 384468733 240 NLIEV 244
Cdd:PRK10070 269 DISQV 273
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 6-225 7.95e-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: 166.16  E-value: 7.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFT--ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNT 81
Cdd:COG2274  474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIGV 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFpHMTVLENVMFGLQRlgwgvVDAEgRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARAL 150
Cdd:COG2274  554 VLQDVFLF-SGTIRENITLGDPD-----ATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 151 APEPRVLLLDEPLSALDLKLRQAVRMELKQIQRetGIAFVFVTHDqEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG2274  627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 11-206 1.36e-45

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: 154.70  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTVFQ 84
Cdd:TIGR03608   4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGYLFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   85 HYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:TIGR03608  84 NFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 384468733  165 ALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEAlTMSDRI 206
Cdd:TIGR03608 164 SLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRV 203
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 3-214 1.39e-45

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 156.38  E-value: 1.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIrLNGEdiAPLPPYRRPVNTV 82
Cdd:PRK11247  10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEAREDTRLM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLqRLGWgvvdaEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:PRK11247  87 FQDARLLPWKKVIDNVGLGL-KGQW-----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-164 1.99e-45

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: 152.42  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI--APLPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 MFGLQRLGWGVVDAEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 6-214 3.53e-45

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: 154.10  E-value: 3.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL-----PPYRRPV 79
Cdd:cd03292    1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:cd03292   81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQReTGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03292  161 DEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 19-233 3.67e-45

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 154.22  E-value: 3.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP---VNTVFQHYALFPHMTVL 95
Cdd:TIGR03410  14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQGREIFPRLTVE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   96 ENVMFGLQRLGwgvvdaeGRARQALELVH-----LSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:TIGR03410  94 ENLLTGLAALP-------RRSRKIPDEIYelfpvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733  171 RQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVA 233
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 4-227 8.42e-45

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 154.14  E-value: 8.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-------- 75
Cdd:PRK11264   2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglir 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 --RRPVNTVFQHYALFPHMTVLENVMFG-LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:PRK11264  82 qlRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGiAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
6-213 8.99e-45

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 152.95  E-value: 8.99e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFT----ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPpY------ 75
Cdd:NF038007   2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-Ysqkiil 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 -RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:NF038007  81 rRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQrETGIAFVFVTHdQEEALTMSDRIAVMSDGR 213
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTH-SDEASTYGNRIINMKDGK 217
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 6-223 1.67e-44

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: 152.52  E-value: 1.67e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-PYRRPVNTVFQ 84
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENV-MFG-LQRLGWGVvdAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:cd03265   81 DLSVDDELTGWENLyIHArLYGVPGAE--RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03265  159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 5-214 2.27e-44

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 152.10  E-value: 2.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFTA----LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIR-----LNGEDIAPLPPY 75
Cdd:TIGR02982   1 VISIRNLNHYYGHGSLrkqvLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqeLHGASKKQLVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   76 RRPVNTVFQHYALFPHMTVLENVMFGLQRL-GWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:TIGR02982  81 RRRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQeEALTMSDRIAVMSDGRV 214
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
20-224 2.65e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 154.05  E-value: 2.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPYRRPVNTVFQH--YALFPHmT 93
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKKVGLVFQYpeYQLFEE-T 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVMFGLQRLGWGVVDAEGRARQALELVHLS--AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 172 QAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
4-230 3.25e-44

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 153.30  E-value: 3.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTF---------TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP- 73
Cdd:PRK10419   2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  74 ----PYRRPVNTVFQHY--ALFPHMTVLENVMFGLQRL-GWGVVDAEGRARQALELVHLSA-FLKRRPGQLSGGQQQRVA 145
Cdd:PRK10419  82 aqrkAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 146 LARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV--QQVGTPREI 223
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLT 241


                 ....*..
gi 384468733 224 YESPANR 230
Cdd:PRK10419 242 FSSPAGR 248
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 5-227 6.69e-44

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 151.34  E-value: 6.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRR------- 77
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 -PvntvfQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:COG1137   83 lP-----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 157 LLLDEPLSALDLKlrqAVrMELKQI---QRETGIAfVFVT-HDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:COG1137  158 ILLDEPFAGVDPI---AV-ADIQKIirhLKERGIG-VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-236 1.03e-43

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 151.66  E-value: 1.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA---------- 70
Cdd:PRK10619   1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  71 -----PLPPYRRPVNTVFQHYALFPHMTVLENVMFG-LQRLGWGVVDAEGRARQALELVHLSAFLKRR-PGQLSGGQQQR 143
Cdd:PRK10619  81 vadknQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 144 VALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239

                        250
                 ....*....|...
gi 384468733 224 YESPANRFVADFI 236
Cdd:PRK10619 240 FGNPQSPRLQQFL 252
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-222 1.62e-43

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 151.08  E-value: 1.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY----RRPV 79
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 ntVFQHYAL-FPhMTVLENVMFGlqRLGWGVVDAEGRA--RQALELVHLSAFLKRRPGQLSGGQQQRVALARALA----- 151
Cdd:PRK13548  81 --LPQHSSLsFP-FTVEEVVAMG--RAPHGLSRAEDDAlvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 152 -PEPRVLLLDEPLSALDLKLRQAVrMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHV-LRLaRQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 14-238 1.86e-43

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 150.91  E-value: 1.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY---RRPVNTVFQHYALFP 90
Cdd:PRK11300  14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiaRMGVVRTFQHVRLFR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 HMTVLENVMFGLQR-LGWGVV--------------DAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:PRK11300  94 EMTVIENLLVAQHQqLKTGLFsgllktpafrraesEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPanRFVADF 235
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIKAY 251


                 ...
gi 384468733 236 IGE 238
Cdd:PRK11300 252 LGE 254
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 6-230 2.05e-43

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: 150.00  E-value: 2.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRR-------- 77
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgigyl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 PvntvfQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVL 157
Cdd:cd03218   81 P-----QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 158 LLDEPLSALDLKLRQAVRmELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANR 230
Cdd:cd03218  156 LLDEPFAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 6-228 2.69e-43

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 151.33  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFT-----ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP------LPP 74
Cdd:PRK13634   3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 YRRPVNTVFQhyalFP-HM----TVLENVMFGLQRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALAR 148
Cdd:PRK13634  83 LRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 149 ALAPEPRVLLLDEPLSALDLKLRQAVrMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEM-MEMfYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237


                 .
gi 384468733 228 A 228
Cdd:PRK13634 238 D 238
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 6-218 1.09e-42

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: 147.34  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIaDNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVFQ 84
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQkLRRRIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFglqrLGW--GVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:cd03264   80 EFGVYPNFTVREFLDY----IAWlkGIPSKEVKARvdEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETgiAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03264  156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-226 1.69e-42

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 149.01  E-value: 1.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRF--GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--R 76
Cdd:PRK13635   1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 RPVNTVFQHY-ALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:PRK13635  81 RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTmSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 6-214 2.12e-42

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 148.31  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF--GT---FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP-- 78
Cdd:COG1101    2 LELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNTVFQHYAL--FPHMTVLENVMFGLQR-----LGWGVVDAE-GRARQALELVHLS--AFLKRRPGQLSGGQQQRVALAR 148
Cdd:COG1101   82 IGRVFQDPMMgtAPSMTIEENLALAYRRgkrrgLRRGLTKKRrELFRELLATLGLGleNRLDTKVGLLSGGQRQALSLLM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 149 ALAPEPRVLLLDEPLSALDLKLRQAVrMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:COG1101  162 ATLTKPKLLLLDEHTAALDPKTAALV-LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-223 1.13e-41

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: 146.00  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFE-PVSGGQI-----RLNGEDIAPLppyrR 77
Cdd:COG1119    2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVrlfgeRRGGEDVWEL----R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 P----VNTVFQHYaLFPHMTVLENVM------FGLqrlgWGVVDAE--GRARQALELVHLSAFLKRRPGQLSGGQQQRVA 145
Cdd:COG1119   78 KriglVSPALQLR-FPRDETVLDVVLsgffdsIGL----YREPTDEqrERARELLELLGLAHLADRPFGTLSQGEQRRVL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 146 LARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG1119  153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 5-265 2.55e-41

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 146.41  E-value: 2.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYR-------R 77
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 pvntvfqhyALFPHMTVLENVMFgLQRL-GWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:COG4152   81 ---------GLYPKMKVGEQLVY-LARLkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 157 LLLDEPLSALD----LKLRQAVRmELKqiqrETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES-PANRF 231
Cdd:COG4152  151 LILDEPFSGLDpvnvELLKDVIR-ELA----AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTL 225

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 384468733 232 VADFIGET----NLIEVPVLNISNGLAEVSLPGGRAIQ 265
Cdd:COG4152  226 RLEADGDAgwlrALPGVTVVEEDGDGAELKLEDGADAQ 263
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 4-230 4.16e-41

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: 144.95  E-value: 4.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    4 TVISIDRVEKRFGT---------FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP 74
Cdd:TIGR02769   1 SLLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   75 -----YRRPVNTVFQ--HYALFPHMTVLENVMFGLQRLGwgVVDAEGRARQALELVHL----SAFLKRRPGQLSGGQQQR 143
Cdd:TIGR02769  81 kqrraFRRDVQLVFQdsPSAVNPRMTVRQIIGEPLRHLT--SLDESEQKARIAELLDMvglrSEDADKLPRQLSGGQLQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  144 VALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV--QQVGTPR 221
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQL 238


                  ....*....
gi 384468733  222 EIYESPANR 230
Cdd:TIGR02769 239 LSFKHPAGR 247
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 5-214 8.33e-41

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: 8.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFG----TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP-- 78
Cdd:TIGR02211   1 LLKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAkl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   79 ----VNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:TIGR02211  81 rnkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMsDRIAVMSDGRV 214
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 19-226 1.02e-40

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: 150.29  E-value: 1.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFpHMTVLE 96
Cdd:COG4988  351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIAWVPQNPYLF-AGTIRE 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  97 NVMFGLQrlgwgvvDA-EGRARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:COG4988  430 NLRLGRP-------DAsDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTA 502

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIafVFVTHDqEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:COG4988  503 HLDAETEAEILQALRRLAKGRTV--ILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 6-219 3.08e-40

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: 139.49  E-value: 3.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRrpvntvfqh 85
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 yalfphmtvlenvmfglqrlgwgvvdaegrARQA-LELVHlsaflkrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd03216   72 ------------------------------ARRAgIAMVY----------QLSVGERQMVEIARALARNARLLILDEPTA 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 165 ALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVqqVGT 219
Cdd:cd03216  112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV--VGT 163
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 6-214 1.25e-39

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


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 139.27  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQH 85
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHMTVLENvmFGLQRLGWGVVDAegRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03268   81 PGFYPNLTAREN--LRLLARLLGIRKK--RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 166 LD----LKLRQAVRMElkqiqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03268  157 LDpdgiKELRELILSL-----RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 20-213 1.51e-39

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: 137.90  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFpHMTVLEN 97
Cdd:cd03228   17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAYVPQDPFLF-SGTIREN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VmfglqrlgwgvvdaegrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:cd03228   96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 384468733 178 LKQIQRETGIafVFVTHDqEEALTMSDRIAVMSDGR 213
Cdd:cd03228  139 LRALAKGKTV--IVIAHR-LSTIRDADRIIVLDDGR 171
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 3-225 1.77e-39

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 146.83  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRF--GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRP 78
Cdd:COG4987  331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRR 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNTVFQHYALFpHMTVLENVMFGLQRLGwgvvDAEgrARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALA 147
Cdd:COG4987  411 IAVVPQRPHLF-DTTLRENLRLARPDAT----DEE--LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 148 RALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafVFVTHDQEEALTMsDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG4987  484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA 558
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 6-218 2.18e-39

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: 139.04  E-value: 2.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF----GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-PYRRPVN 80
Cdd:cd03266    2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMF-----GLQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:cd03266   82 FVSDSTGLYDRLTARENLEYfaglyGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQiQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03266  157 VLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 5-219 2.27e-39

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 145.55  E-value: 2.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP---YRRPVNT 81
Cdd:COG3845    5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrdaIALGIGM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGLQRLGWGVVD---AEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG3845   85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDrkaARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 159 LDEPLSALDLklrQAVRmELKQIQR---ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVqqVGT 219
Cdd:COG3845  165 LDEPTAVLTP---QEAD-ELFEILRrlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
cbiO PRK13650
energy-coupling factor transporter ATPase;
21-224 4.11e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 140.25  E-value: 4.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTVFQHY-ALFPHMTVLEN 97
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdiRHKIGMVFQNPdNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 384468733 178 LKQIQRETGIAFVFVTHDQEEaLTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 4-236 7.82e-39

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 138.51  E-value: 7.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-----EPVSGGQIRLNGEDI--APLPPYR 76
Cdd:PRK14247   2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 RPVNTVFQHYALFPHMTVLENVMFGLQ--RLGWGVVDAEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARAL 150
Cdd:PRK14247  82 RRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 151 APEPRVLLLDEPLSALD----LKLrQAVRMELKQiqretGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK14247 162 AFQPEVLLADEPTANLDpentAKI-ESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235

                        250
                 ....*....|
gi 384468733 227 PANRFVADFI 236
Cdd:PRK14247 236 PRHELTEKYV 245
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 6-218 3.67e-38

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 135.49  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE--------DIAPLPPYRr 77
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnRIGYLPEER- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 pvntvfqhyALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVL 157
Cdd:cd03269   80 ---------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 158 LLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03269  151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 5-238 1.04e-37

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: 135.09  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP---VNT 81
Cdd:TIGR04406   1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   82 VFQHYALFPHMTVLENVMFGLQRLgwGVVDAEGRARQA---LELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:TIGR04406  81 LPQEASIFRKLTVEENIMAVLEIR--KDLDRAEREERLealLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  159 LDEPLSALD----LKLRQAVRmelkqIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVad 234
Cdd:TIGR04406 159 LDEPFAGVDpiavGDIKKIIK-----HLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV-- 231


                  ....
gi 384468733  235 FIGE 238
Cdd:TIGR04406 232 YLGE 235
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
20-222 1.25e-37

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 141.84  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFpHMTVLEN 97
Cdd:COG1132  355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIGVVPQDTFLF-SGTIREN 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQrlgwgvvDA-EGRARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:COG1132  434 IRYGRP-------DAtDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSA 506

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 166 LDLKLRQAVRMELKQIQRE-TGIAfvfVTHdQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:COG1132  507 LDTETEALIQEALERLMKGrTTIV---IAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-236 3.15e-37

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 134.52  E-value: 3.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-----EPVSGGQIRLNGEDI-APLP- 73
Cdd:PRK14239   1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIySPRTd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  74 --PYRRPVNTVFQHYALFPhMTVLENVMFGLqRLGwGVVDAEgRARQALE--------------LVHLSAFlkrrpgQLS 137
Cdd:PRK14239  81 tvDLRKEIGMVFQQPNPFP-MSIYENVVYGL-RLK-GIKDKQ-VLDEAVEkslkgasiwdevkdRLHDSAL------GLS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 138 GGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafVFVTHDQEEALTMSDRIAVMSDGRVQQV 217
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEY 228

                        250
                 ....*....|....*....
gi 384468733 218 GTPREIYESPANRFVADFI 236
Cdd:PRK14239 229 NDTKQMFMNPKHKETEDYI 247
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 6-223 4.77e-37

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 133.67  E-value: 4.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVF 83
Cdd:COG4604    2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  84 QHYALFPHMTVLENVMFG--------LQRLGWGVVDaegrarQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR 155
Cdd:COG4604   82 QENHINSRLTVRELVAFGrfpyskgrLTAEDREIID------EAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 156 VLLLDEPLSALDLKlrQAVRMeLKQIQR---ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG4604  156 YVLLDEPLNNLDMK--HSVQM-MKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 15-236 5.10e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 131.12  E-value: 5.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  15 FGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRC---------IAGFEpvsgGQIRLNG-----EDIAPLPpYRRPVN 80
Cdd:PRK14267  14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneEARVE----GEVRLFGrniysPDVDPIE-VRREVG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGLQ--RLGWGVVDAEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARALAPEP 154
Cdd:PRK14267  89 MVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVAD 234
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246


                 ..
gi 384468733 235 FI 236
Cdd:PRK14267 247 YV 248
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
4-214 5.61e-36

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 131.29  E-value: 5.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF---EPVSGGQIRLNGEDIA-------PLP 73
Cdd:PRK09984   3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQregrlarDIR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  74 PYRRPVNTVFQHYALFPHMTVLENVMFG------LQR--LGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVA 145
Cdd:PRK09984  83 KSRANTGYIFQQFNLVNRLSVLENVLIGalgstpFWRtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 146 LARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 7-214 7.40e-36

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: 129.30  E-value: 7.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   7 SIDRVEKRFGTFT-ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRpVNTVFQH 85
Cdd:cd03226    1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 --YALFPHmTVLENVMFGLQRLGwgvvDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:cd03226   80 vdYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384468733 164 SALDLKLRQAVRMELKQIQRETGIAFVfVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03226  155 SGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAI 204
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 20-227 2.46e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 129.81  E-value: 2.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPYRRPVNTVFQHY--ALF-Phm 92
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVGIVFQNPddQLFaP-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQ 172
Cdd:PRK13639  95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 173 AVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
36-247 2.54e-35

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 131.92  E-value: 2.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE---DIAP---LPPYRRPVNTVFQHYALFPHMTVLENVMFGLqrlgwgv 109
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM------- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 110 vdAEGRARQALELVHL---SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETG 186
Cdd:PRK11144 102 --AKSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 187 IAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFVADFIGETNLIEVPVL 247
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVL 240
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 6-225 3.94e-35

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: 134.16  E-value: 3.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRvekrfGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQ--IRLNGE--DIAPLPPYRRP--- 78
Cdd:TIGR03269 290 ISVDR-----GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGrak 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   79 --VNTVFQHYALFPHMTVLENVMfglQRLGWGVVDAEGRaRQALELVHLSAF--------LKRRPGQLSGGQQQRVALAR 148
Cdd:TIGR03269 365 ryIGILHQEYDLYPHRTVLDNLT---EAIGLELPDELAR-MKAVITLKMVGFdeekaeeiLDKYPDELSEGERHRVALAQ 440

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733  149 ALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-228 5.34e-35

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: 134.04  E-value: 5.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGT----FTALHGVSVDIADNEFFTLLGPSGCGKT----TLLRCIAGFEPVSGGQIRLNGEDIAPL 72
Cdd:COG4172    2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  73 PPYR------RPVNTVFQH--YALFPHMTVLENVMFGLQR-LGWGVVDAEGRARQALELVHL---SAFLKRRPGQLSGGQ 140
Cdd:COG4172   82 SERElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 141 QQRVALARALAPEPRVLLLDEPLSALD-------LKLrqavrmeLKQIQRETGIAFVFVTHDqeeaLT----MSDRIAVM 209
Cdd:COG4172  162 RQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLDL-------LKDLQRELGMALLLITHD----LGvvrrFADRVAVM 230

                        250
                 ....*....|....*....
gi 384468733 210 SDGRVQQVGTPREIYESPA 228
Cdd:COG4172  231 RQGEIVEQGPTAELFAAPQ 249
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
15-223 7.53e-35

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 128.21  E-value: 7.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  15 FGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPyrrpvNTVFQHYALFP--HM 92
Cdd:PRK11231  12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARRLALLPqhHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 T-----VLENVMFG------LqrlgWGVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK11231  87 TpegitVRELVAYGrspwlsL----WGRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 160 DEPLSALDLKlRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK11231 163 DEPTTYLDIN-HQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
cbiO PRK13649
energy-coupling factor transporter ATPase;
20-225 1.11e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 128.32  E-value: 1.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP------LPPYRRPVNTVFQhyalFPHM- 92
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 ----TVLENVMFGLQRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK13649  98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 168 LKLRQAVrMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:PRK13649 178 PKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 17-227 3.51e-34

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 128.29  E-value: 3.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  17 TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI-----APLPPYRRPVNTVFQH--YALF 89
Cdd:PRK15079  33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAVRSDIQMIFQDplASLN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  90 PHMTVLENVMFGLQ----RLGWGVVDAEGRArQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK15079 113 PRMTIGEIIAEPLRtyhpKLSRQEVKDRVKA-MMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 6-236 7.89e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 125.53  E-value: 7.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG-----GQIRLNGEDI----APLPPYR 76
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 RPVNTVFQHYALFPhMTVLENVMFGLQRLGW-------GVVDAegrARQALEL-------VHLSAFlkrrpgQLSGGQQQ 142
Cdd:PRK14258  88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrpkleidDIVES---ALKDADLwdeikhkIHKSAL------DLSGGQQQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 143 RVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVM--SDGRVQQV--- 217
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvef 237

                        250
                 ....*....|....*....
gi 384468733 218 GTPREIYESPANRFVADFI 236
Cdd:PRK14258 238 GLTKKIFNSPHDSRTREYV 256
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 20-214 9.26e-34

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: 122.93  E-value: 9.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVF------QHYALFPHMT 93
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVMFGLQrlgwgvvdaegrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQA 173
Cdd:cd03215   95 VAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 384468733 174 VRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03215  143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 18-259 1.80e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 125.97  E-value: 1.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL----------------PPY------ 75
Cdd:PRK13651  20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqKTRfkkikk 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 ----RRPVNTVFQ--HYALFpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALAR 148
Cdd:PRK13651 100 ikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 149 ALAPEPRVLLLDEPLSALDlklRQAVRMELKQIQR--ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNlnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255

                        250       260       270
                 ....*....|....*....|....*....|...
gi 384468733 227 panrfvADFIGETNLIEVPVLNISNGLAEVSLP 259
Cdd:PRK13651 256 ------NKFLIENNMEPPKLLNFVNKLEKKGID 282
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 5-236 2.79e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 124.00  E-value: 2.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE------DIAPLPP--YR 76
Cdd:PRK14246  10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 RPVNTVFQHYALFPHMTVLENVMFGLQRLGWG-------VVDAEGRARQALELVHLSafLKRRPGQLSGGQQQRVALARA 149
Cdd:PRK14246  90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKekreikkIVEECLRKVGLWKEVYDR--LNSPASQLSGGQQQRLTIARA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtgIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPAN 229
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245


                 ....*..
gi 384468733 230 RFVADFI 236
Cdd:PRK14246 246 ELTEKYV 252
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 20-214 4.03e-33

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: 122.31  E-value: 4.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTVFQHYALFpHMTVLEN 97
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQrlgwgVVDAEgRARQALELVHLSAFLKRRP----------GQ-LSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:cd03245   98 ITLGAP-----LADDE-RILRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLNDPPILLLDEPTSAM 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 384468733 167 DLKLRQAVRMELKQIQRetGIAFVFVTHDQeEALTMSDRIAVMSDGRV 214
Cdd:cd03245  172 DMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 4-236 1.10e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 122.58  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRC-------IAGFEpVSGGQI----RLNGEDIAPL 72
Cdd:PRK14243   9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR-VEGKVTfhgkNLYAPDVDPV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  73 PpYRRPVNTVFQHYALFPHmTVLENVMFGLQRLGW-GVVD--AEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARA 149
Cdd:PRK14243  88 E-VRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYkGDMDelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafVFVTHDQEEALTMSDRIAVMS---------DGRVQQVGTP 220
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRT 243

                        250
                 ....*....|....*.
gi 384468733 221 REIYESPANRFVADFI 236
Cdd:PRK14243 244 EKIFNSPQQQATRDYV 259
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 16-227 1.80e-32

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 123.54  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-----YRRPVNTVFQH-YA-L 88
Cdd:PRK11308  26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  89 FPHMTV---LENVMFGLQRLgwgvvDAEGRARQALEL---VHLSA-FLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK11308 106 NPRKKVgqiLEEPLLINTSL-----SAAERREKALAMmakVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 12-255 1.84e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 123.42  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  12 EKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-----------EPVSGGQIRLNGEDIAPLPP------ 74
Cdd:PRK13631  33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgDIYIGDKKNNHELITNPYSKkiknfk 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  75 -YRRPVNTVFQ--HYALFPHmTVLENVMFGLQRLGWGVVDAEGRARQALELVHL-SAFLKRRPGQLSGGQQQRVALARAL 150
Cdd:PRK13631 113 eLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGIL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 151 APEPRVLLLDEPLSALDLKLRQAVrMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPanr 230
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ--- 267

                        250       260
                 ....*....|....*....|....*
gi 384468733 231 fvaDFIGETNLIEVPVLNISNGLAE 255
Cdd:PRK13631 268 ---HIINSTSIQVPRVIQVINDLIK 289
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 3-246 1.97e-32

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 124.95  E-value: 1.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYR--RPVN 80
Cdd:PRK09536   1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFG----LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:PRK09536  81 SVPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 157 LLLDEPLSALDLKlRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRfvADFI 236
Cdd:PRK09536 161 LLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR--AAFD 237

                        250
                 ....*....|
gi 384468733 237 GETNLIEVPV 246
Cdd:PRK09536 238 ARTAVGTDPA 247
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 8-213 2.17e-32

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 120.59  E-value: 2.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   8 IDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQH 85
Cdd:PRK10247  10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 YALFPHmTVLENVMFGLQRLGwgvvDAEGRARQALELVHLS---AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:PRK10247  90 PTLFGD-TVYDNLIFPWQIRN----QQPDPAIFLDDLERFAlpdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEE------ALTMSDRIAVMSDGR 213
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEinhadkVITLQPHAGEMQEAR 221
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 4-213 3.24e-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: 120.23  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRF-------GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE----DIAPL 72
Cdd:COG4778    3 TLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  73 PPY------RRPVNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQAL-------ELVHLSaflkrrPGQLSGG 139
Cdd:COG4778   83 SPReilalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLarlnlpeRLWDLP------PATFSGG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 140 QQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRmELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:COG4778  157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVV-ELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
18-227 4.21e-32

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 121.10  E-value: 4.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLPP----YR-RPVNTVFQH--YALFP 90
Cdd:COG4167   26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYgdykYRcKHIRMIFQDpnTSLNP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 HMTV---------LENVMFGLQRlgwgvvdaEGRARQALELVHLS---AFLKrrPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:COG4167  103 RLNIgqileeplrLNTDLTAEER--------EERIFATLRLVGLLpehANFY--PHMLSSGQKQRVALARALILQPKIII 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 159 LDEPLSALDLKLR-QAVRMELKqIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:COG4167  173 ADEALAALDMSVRsQIINLMLE-LQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 21-214 5.30e-32

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: 118.09  E-value: 5.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFPHmTVLENV 98
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYLPQDDELFSG-SIAENI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 mfglqrlgwgvvdaegrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMEL 178
Cdd:cd03246   97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 384468733 179 KQIqRETGIAFVFVTHdQEEALTMSDRIAVMSDGRV 214
Cdd:cd03246  140 AAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
cbiO PRK13641
energy-coupling factor transporter ATPase;
21-227 6.47e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 121.09  E-value: 6.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP------LPPYRRPVNTVFQhyalFPHM-- 92
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknLKKLRKKVSLVFQ----FPEAql 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 ---TVLENVMFGLQRLGWGVVDAEGRARQALELVHLS-AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PRK13641  99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 169 KLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-224 9.97e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 120.58  E-value: 9.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNG---EDIAPLPPYRRPVNTVFQHyalfPH---- 91
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiv 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 -MTVLENVMFGLQRLGwgVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PRK13633 100 aTIVEEDVAFGPENLG--IPPEEIRERvdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 169 KLRQAVRMELKQIQRETGIAFVFVTHDQEEALTmSDRIAVMSDGRVQQVGTPREIY 224
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 20-225 1.06e-31

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 119.26  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVNTVFQHYALFpHMTVLEN 97
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDTVAEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQrlgwGVVDAEgrARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:cd03251   96 IAYGRP----GATREE--VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 167 DLKLRQAVRMELKQIQRETGiafVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:cd03251  170 DTESERLVQAALERLMKNRT---TFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 20-214 1.90e-31

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


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 124.98  E-value: 1.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTVFQHYALFpHMTVLEN 97
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   98 VMFGLQrlgwGVVDAEgrARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:TIGR03375 559 IALGAP----YADDEE--ILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 384468733  167 DLKLRQAVRMELKQ-IQRETgiaFVFVTHDQeEALTMSDRIAVMSDGRV 214
Cdd:TIGR03375 633 DNRSEERFKDRLKRwLAGKT---LVLVTHRT-SLLDLVDRIIVMDNGRI 677
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 20-229 2.24e-31

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: 118.24  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP----VSGGQIRLNGEDIAPLPPYRRPVNTVFQH--YALFPHMT 93
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   94 VLENVMFGLQRLGWGVVDAEGRARQALELVHL---SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733  171 RQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPAN 229
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 20-226 3.25e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 118.70  E-value: 3.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQH-YALFPHMTVLE 96
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQNpDNQFVGSIVKY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  97 NVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRM 176
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 177 ELKQIQRETGIAFVFVTHDQEEALTmSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-226 6.55e-31

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 119.14  E-value: 6.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-RRPV 79
Cdd:PRK13537   3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHaRQRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK13537  83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQrETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
21-216 9.99e-31

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 116.45  E-value: 9.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTVFQHYALFPHMTV 94
Cdd:PRK11629  25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  95 LENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAV 174
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 384468733 175 RMELKQIQRETGIAFVFVTHDQEEALTMSdRIAVMSDGRVQQ 216
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-200 1.06e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 115.41  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGediaplppyRRPVNTVFQHYAL---FP 90
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 hMTVLENVMFGL-QRLG-WGVVDAEGRAR--QALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:NF040873  72 -LTVRDLVAMGRwARRGlWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 384468733 167 DLKLRQAVRMELKQIqRETGIAFVFVTHDQEEAL 200
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVR 183
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 10-225 1.06e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 116.72  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  10 RVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLppyrrPVNTVFQhyalf 89
Cdd:COG1134   31 RRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH----- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  90 PHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:COG1134  101 PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 170 LRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:COG1134  181 FQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
cbiO PRK13643
energy-coupling factor transporter ATPase;
20-225 1.37e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 117.91  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNgeDIA--------PLPPYRRPVNTVFQhyalFPH 91
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVvsstskqkEIKPVRKKVGVVFQ----FPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 M-----TVLENVMFGLQRLGWGVVDAEGRARQALELVHLSA-FLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK13643  95 SqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 166 LDLKLRQAVrMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:PRK13643 175 LDPKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 6-225 1.41e-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: 121.45  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTL---LRCIAGFEPVSG------------GQIRLNGEDIA 70
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGriiyhvalcekcGYVERPSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   71 PLP------------------PYRRPVN----TVFQH-YALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSA 127
Cdd:TIGR03269  81 PCPvcggtlepeevdfwnlsdKLRRRIRkriaIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  128 FLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIA 207
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250
                  ....*....|....*...
gi 384468733  208 VMSDGRVQQVGTPREIYE 225
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 20-227 1.44e-30

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 122.27  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-----PYRRPVNTVFQ--HYALFPHM 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQdpYASLDPRQ 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFGLQRlgWGVVDAEGRARQALELVHLSAFLK----RRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PRK10261 419 TVGDSIMEPLRV--HGLLPGKAAAARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 169 KLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 20-221 2.76e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 116.37  E-value: 2.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTVFQHY--ALFPhMTVL 95
Cdd:PRK13647  20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVFS-STVW 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVR 175
Cdd:PRK13647  99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 384468733 176 MELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPR 221
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
5-214 1.26e-29

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 113.43  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL-----PPYRRP 78
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:PRK10908  81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQReTGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
cbiO PRK13645
energy-coupling factor transporter ATPase;
18-226 1.56e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 114.72  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQ-------IRLNGEDIAPLPPYRRPVNTVFQ--HYAL 88
Cdd:PRK13645  24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVKRLRKEIGLVFQfpEYQL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  89 FPHmTVLENVMFGLQRLGWGVVDAEGRARQALELVHL-SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 168 LKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 16-247 2.05e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 114.13  E-value: 2.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI--APLPPYRRPVNTVFQHY--ALFPh 91
Cdd:PRK13652  15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFVGLVFQNPddQIFS- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 MTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:PRK13652  94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 172 QAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPanrfvaDFIGETNLiEVPVL 247
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP------DLLARVHL-DLPSL 242
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 19-214 2.16e-29

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 117.82  E-value: 2.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVF------QHYALFPHM 92
Cdd:COG3845  272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDM 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFGLQRLG----WGVVDAEGRARQALELVhlSAF------LKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG3845  352 SVAENLILGRYRRPpfsrGGFLDRKAIRAFAEELI--EEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQP 429

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468733 163 LSALDLKLRQAVRMELKQiQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:COG3845  430 TRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 20-226 2.22e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 113.93  E-value: 2.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGgQIRLNGEDI--APLPPYRRPVNTVFQHY-ALFPHMTVL 95
Cdd:PRK13632  24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQSG-EIKIDGITIskENLKEIRKKIGIIFQNPdNQFIGATVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRlgwGVVDAEGRARQALEL---VHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQ 172
Cdd:PRK13632 103 DDIAFGLEN---KKVPPKKMKDIIDDLakkVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384468733 173 AVRMELKQIQRETGIAFVFVTHDQEEALtMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
cbiO PRK13646
energy-coupling factor transporter ATPase;
18-226 2.62e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 114.11  E-value: 2.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP------LPPYRRPVNTVFQhyalFPH 91
Cdd:PRK13646  20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 MTVLEN-----VMFGLQRLGWGVVDAEGRARQAL-ELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK13646  96 SQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 8-195 3.10e-29

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 117.86  E-value: 3.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   8 IDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRL-NGEDIAPLPpyrrpvntvfQHY 86
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP----------QEP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALFPHMTVLENVMFGLQRL-----------------------------------GWgvvDAEGRARQALELVHLS-AFLK 130
Cdd:COG0488   71 PLDDDLTVLDTVLDGDAELraleaeleeleaklaepdedlerlaelqeefealgGW---EAEARAEEILSGLGFPeEDLD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 131 RRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLklrQAVR-MElKQIQRETGiAFVFVTHD 195
Cdd:COG0488  148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEwLE-EFLKNYPG-TVLVVSHD 208
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 21-225 5.55e-29

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 111.86  E-value: 5.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFPhMTVLENV 98
Cdd:cd03249   19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTIAENI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 MFGlqRLGWGVVDAEGRARQAlelvHLSAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:cd03249   98 RYG--KPDATDEEVEEAAKKA----NIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 168 LKLRQAVRMELKQIQRetGIAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:cd03249  172 AESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 6-209 7.97e-29

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 116.62  E-value: 7.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRF-GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTV 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   83 FQHYALFPHmTVLENVmfglqRLGWGVVDAEgRARQALELVHLSAFLKRRPGQ-----------LSGGQQQRVALARALA 151
Cdd:TIGR02857 402 PQHPFLFAG-TIAENI-----RLARPDASDA-EIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFL 474

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733  152 PEPRVLLLDEPLSALDLKLRQAVRMELKQIQRetGIAFVFVTHDQEEALTMsDRIAVM 209
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 5-216 2.00e-28

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 110.25  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFG----TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRP-- 78
Cdd:PRK10584   6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 ----VNTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEP 154
Cdd:PRK10584  86 rakhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEAlTMSDRIAVMSDGRVQQ 216
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
20-244 2.31e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 111.23  E-value: 2.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNG---EDIAPLPPYRRPVNTVFQH-YALFPHMTVL 95
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVGRTVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVR 175
Cdd:PRK13644  97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 176 MELKQIQREtGIAFVFVTHDQEEaLTMSDRIAVMSDGRVQQVGTPREIYESPANRFVAdfIGETNLIEV 244
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPSLIEL 241
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 21-223 5.92e-28

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 114.46  E-value: 5.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRR-------PvntvfQHYALFPHmT 93
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhigylP-----QDVELFDG-T 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVmfglQRLGwgVVDAEgRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:COG4618  422 IAENI----ARFG--DADPE-KVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 163 LSALD----LKLRQAVRmELKqiqrETGIAFVFVTHDQeEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG4618  495 NSNLDdegeAALAAAIR-ALK----ARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
cbiO PRK13642
energy-coupling factor transporter ATPase;
21-226 8.21e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 109.80  E-value: 8.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTVFQHY-ALFPHMTVLEN 97
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIGMVFQNPdNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 384468733 178 LKQIQRETGIAFVFVTHDQEEALTmSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 16-214 1.03e-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: 107.25  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG---FEPVSGgQIRLNGEDIaPLPPYRRPVNTVFQHYALFPHM 92
Cdd:cd03213   20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrtGLGVSG-EVLINGRPL-DKRSFRKIIGYVPQDDILHPTL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFglqrlgwgvvdaegrarqalelvhlSAFLKrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQ 172
Cdd:cd03213   98 TVRETLMF-------------------------AAKLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 384468733 173 AVrMELKQIQRETGIAFVFVTHD-QEEALTMSDRIAVMSDGRV 214
Cdd:cd03213  149 QV-MSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-214 1.05e-27

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 113.19  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP-------------LPPYRRpvntvfqHY 86
Cdd:COG1129  267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVPEDRK-------GE 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALFPHMTVLENVMFG-LQRLG-WGVVDAEGRARQALELVHL----SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:COG1129  340 GLVLDLSIRENITLAsLDRLSrGGLLDRRRERALAEEYIKRlrikTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 161 EPLSALDLKLRQAVrmeLKQIQR--ETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:COG1129  420 EPTRGIDVGAKAEI---YRLIRElaAEGKAVIVISSELPELLGLSDRILVMREGRI 472
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 6-218 1.07e-27

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: 108.00  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLppyrrPVNTVFQh 85
Cdd:cd03220   23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 yalfPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03220   97 ----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIaFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03220  173 GDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 24-219 1.11e-27

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 113.79  E-value: 1.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGgQIRLNGEDIAPLPP--YRRPVNTVFQHYALFpHMTVLENVMFG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNVLLG 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 102 LQRLGwgvvdaEGRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:PRK11174 447 NPDAS------DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 171 RQAVRMELKQI-QRETGIafvFVTHdQEEALTMSDRIAVMSDGRVQQVGT 219
Cdd:PRK11174 521 EQLVMQALNAAsRRQTTL---MVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 21-194 1.19e-27

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 107.65  E-value: 1.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIaPLPPYRRPVntvfqHY-----ALFPHMTVL 95
Cdd:PRK13539  18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEAC-----HYlghrnAMKPALTVA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRLGwgvvDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDlklRQAVR 175
Cdd:PRK13539  92 ENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD---AAAVA 164

                        170       180
                 ....*....|....*....|.
gi 384468733 176 M--ELKQIQRETGIAFVFVTH 194
Cdd:PRK13539 165 LfaELIRAHLAQGGIVIAATH 185
cbiO PRK13640
energy-coupling factor transporter ATPase;
11-227 1.34e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 109.50  E-value: 1.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFT-------ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEP---------VSGgqIRLNGEDIAPLp 73
Cdd:PRK13640   6 VEFKHVSFTypdskkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskitVDG--ITLTAKTVWDI- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  74 pyRRPVNTVFQHY-ALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:PRK13640  83 --REKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEAlTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 20-226 2.17e-27

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: 107.31  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP--PYRRPVNTVFQHYALFPHmTVLEN 97
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVVLQDTFLFSG-TIMEN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VmfglqRLGWGVVDAEgRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:cd03254   97 I-----RLGRPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 167 DLKLRQAVRMELKQIQRetGIAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:cd03254  171 DTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 1-224 2.65e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 108.78  E-value: 2.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFT-ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPY 75
Cdd:PRK13636   1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  76 RRPVNTVFQH--YALFPhMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAfLKRRPGQ-LSGGQQQRVALARALAP 152
Cdd:PRK13636  81 RESVGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 18-222 3.28e-27

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: 107.32  E-value: 3.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVNTVFQHYALFpHMTVL 95
Cdd:cd03253   14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTVLF-NDTIG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGlqRLGWGVVDAEGRARQAlelvHLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd03253   93 YNIRYG--RPDATDEEVIEAAKAA----QIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 165 ALDLKLRQAVRMELKQI-QRETGIafvFVTHDQEEALTmSDRIAVMSDGRVQQVGTPRE 222
Cdd:cd03253  167 ALDTHTEREIQAALRDVsKGRTTI---VIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 6-223 4.28e-27

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: 112.53  E-value: 4.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    6 ISIDRVEKRFG-TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY--RRPVNTV 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   83 FQHYALFPHmTVLENVMFGLQRlgwGVvdAEGRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARALA 151
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKE---NV--SQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALL 627

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733  152 PEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIafvFVTHDQEEAlTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 15-238 5.06e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 107.87  E-value: 5.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  15 FGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-EPVSG----GQIRLNGEDI---APLPPYRRPVNTVFQHY 86
Cdd:PRK14271  31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIfnyRDVLEFRRRVGMLFQRP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALFPhMTVLENVMFGLqRLGWGVVDAE--GRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:PRK14271 111 NPFP-MSIMDNVLAGV-RAHKLVPRKEfrGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQREtgIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPAN----RFVADFI 236
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYVAGLS 266


                 ..
gi 384468733 237 GE 238
Cdd:PRK14271 267 GD 268
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-212 8.39e-27

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 110.64  E-value: 8.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP---YRR 77
Cdd:PRK09700   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 PVNTVFQHYALFPHMTVLENVMFG--LQRLGWGV--VD-AEGRARQALELVHLSafLKRRP----GQLSGGQQQRVALAR 148
Cdd:PRK09700  81 GIGIIYQELSVIDELTVLENLYIGrhLTKKVCGVniIDwREMRVRAAMMLLRVG--LKVDLdekvANLSISHKQMLEIAK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 149 ALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDG 212
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-214 9.99e-27

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 106.12  E-value: 9.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP---YRR 77
Cdd:PRK11614   1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  78 PVNTVFQHYALFPHMTVLENVMFGlqrlgwGVVDAEGRARQALELVH-----LSAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:PRK11614  81 AVAIVPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYelfprLHERRIQRAGTMSGGEQQMLAIGRALMS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
36-236 1.55e-26

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 106.39  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP-----PYRRPVNTVFQHYALFPHMTVLENVMFGLQ---RLGW 107
Cdd:PRK11831  38 IMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMSMLFQSGALFTDMNVFDNVAYPLRehtQLPA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 108 GVVDAEgrARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDlKLRQAVRMEL-KQIQRETG 186
Cdd:PRK11831 118 PLLHST--VMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD-PITMGVLVKLiSELNSALG 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 187 IAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRfVADFI 236
Cdd:PRK11831 195 VTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 24-223 2.00e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 105.36  E-value: 2.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY---RRPVNTVFQHYALFPHMTVLENVMF 100
Cdd:PRK10895  22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQEASIFRRLSVYDNLMA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 101 GLQ-RLGWGVVDAEGRARQALELVHLSaFLKRRPGQ-LSGGQQQRVALARALAPEPRVLLLDEPLSALDlklrQAVRMEL 178
Cdd:PRK10895 102 VLQiRDDLSAEQREDRANELMEEFHIE-HLRDSMGQsLSGGERRRVEIARALAANPKFILLDEPFAGVD----PISVIDI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 384468733 179 KQI---QRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK10895 177 KRIiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
21-214 5.42e-26

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 109.04  E-value: 5.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP------YRRPVNTVFQHYALFPHMTV 94
Cdd:PRK10535  24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLTA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  95 LENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAV 174
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 384468733 175 RMELKQIqRETGIAFVFVTHDQEEAlTMSDRIAVMSDGRV 214
Cdd:PRK10535 184 MAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 10-223 1.10e-25

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 107.88  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   10 RVEKRFGTFT-------ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVN 80
Cdd:TIGR02203 330 DVEFRNVTFRypgrdrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVA 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   81 TVFQHYALFPHmTVLENVMFGLQRlgwGVVDAegRARQALELVHLSAFLKRRP-----------GQLSGGQQQRVALARA 149
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIAYGRTE---QADRA--EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARA 483

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733  150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRE-TGIAFVFVTHDQEEAltmsDRIAVMSDGRVQQVGTPREI 223
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGrTTLVIAHRLSTIEKA----DRIVVMDDGRIVERGTHNEL 554
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 19-231 1.81e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 107.10  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTT----LLRCIAgfepvSGGQIRLNGEDIAPLP-----PYRRPVNTVFQ--HYA 87
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSS 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFPHMTVLENVMFGLQ--RLGWGVVDAEGRARQALELVHLSAFLKRR-PGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 165 ALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRF 231
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 13-219 4.25e-25

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 105.78  E-value: 4.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVS--GGQIRLNGEdiaPLPPY------RRPVNTVFQ 84
Cdd:PRK13549  13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGE---ELQASnirdteRAGIAIIHQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVDAEG---RARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK13549  90 ELALVKELSVLENIFLGNEITPGGIMDYDAmylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 162 PLSALDlklRQAVRMELKQIQ--RETGIAFVFVTHDQEEALTMSDRIAVMSDGRvqQVGT 219
Cdd:PRK13549 170 PTASLT---ESETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 21-223 4.29e-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: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFPHmTVLENV 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRetFGKHIGYLPQDVELFPG-TVAENI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 M-FGLQRLGWGVVDAeGRARQALELVhLS------AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:TIGR01842 413 ArFGENADPEKIIEA-AKLAGVHELI-LRlpdgydTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 384468733  172 QAVRMELKQIQREtGIAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:TIGR01842 491 QALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 12-213 1.06e-24

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: 99.47  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  12 EKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdIAplppYrrpvntVFQhYALFPH 91
Cdd:cd03250   12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA----Y------VSQ-EPWIQN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 MTVLENVMFGLQrlgwgvVDAEgRARQALELVHLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLD 160
Cdd:cd03250   80 GTIRENILFGKP------FDEE-RYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLD 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 161 EPLSALDLK-----LRQAVRMELKQiqretGIAFVFVTHdQEEALTMSDRIAVMSDGR 213
Cdd:cd03250  153 DPLSAVDAHvgrhiFENCILGLLLN-----NKTRILVTH-QLQLLPHADQIVVLDNGR 204
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 1-215 1.58e-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: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   1 MIGTVISIDRVEKRfgTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDiaplpPYRRPVN 80
Cdd:cd03267   19 LIGSLKSLFKRKYR--EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMT-------VLENvmFGLQRLGWGVVDAEGRARQA--LELVHLSAFLKRRPGQLSGGQQQRVALARALA 151
Cdd:cd03267   92 FLRRIGVVFGQKTqlwwdlpVIDS--FYLLAAIYDLPPARFKKRLDelSELLDLEELLDTPVRQLSLGQRMRAEIAAALL 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 152 PEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQ 215
Cdd:cd03267  170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-225 1.84e-24

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 102.22  E-value: 1.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLPPY----RRPV 79
Cdd:PRK13536  40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARarlaRARI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHYALFPHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLL 159
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 160 DEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 11-219 2.32e-24

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: 103.75  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG--GQIRLNGEDIAP---LPPYRRPVNTVFQH 85
Cdd:TIGR02633   7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKAsniRDTERAGIVIIHQE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   86 YALFPHMTVLENVMFG--LQRLGWGVVDAEG--RARQALELVHLSAFLKRRP-GQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:TIGR02633  87 LTLVPELSVAENIFLGneITLPGGRMAYNAMylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733  161 EPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGrvQQVGT 219
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 2-263 2.83e-24

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 101.32  E-value: 2.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   2 IGTVISIDRVEKRfgTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPvSGGQIRLNGEDiaplpPYRRPVN 80
Cdd:COG4586   21 KGALKGLFRREYR--EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYV-----PFKRRKE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 ------TVF-QHYALFPHMTVLENvmFGLQRLGWGVVDAEGRARQAL--ELVHLSAFLKRRPGQLSGGQQQRVALARALA 151
Cdd:COG4586   93 farrigVVFgQRSQLWWDLPAIDS--FRLLKAIYRIPDAEYKKRLDElvELLDLGELLDTPVRQLSLGQRMRCELAAALL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 152 PEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQE--EALtmSDRIAVMSDGRVqqvgtpreIYESPAN 229
Cdd:COG4586  171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRI--------IYDGSLE 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 384468733 230 RFVADFIGETNLI-----EVPVLNISNGLAEVSLPGGRA 263
Cdd:COG4586  241 ELKERFGPYKTIVlelaePVPPLELPRGGEVIEREGNRV 279
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 6-223 4.74e-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: 98.71  E-value: 4.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFG--TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNT 81
Cdd:cd03252    1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVH-----LSAFLKRRPGQLSGGQQQRVALARALAPEPRV 156
Cdd:cd03252   81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISelpegYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 157 LLLDEPLSALDLKLRQAVRMELKQIQreTGIAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 7-218 5.35e-24

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 98.84  E-value: 5.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   7 SIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-------RRPV 79
Cdd:PRK11701   8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerRRLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NT----VFQHYA--LFPHMTVLENVMFGLQRLGWgvvDAEGRARQA----LELVHL-SAFLKRRPGQLSGGQQQRVALAR 148
Cdd:PRK11701  88 RTewgfVHQHPRdgLRMQVSAGGNIGERLMAVGA---RHYGDIRATagdwLERVEIdAARIDDLPTTFSGGMQQRLQIAR 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733 149 ALAPEPRVLLLDEPLSALDLKLrQAVRMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSV-QARLLDLlRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 5-214 6.87e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 102.44  E-value: 6.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP---YRRPVNT 81
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHMTVLENVMFGLQRlgwgVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK15439  91 VPQEPLLFPNLSVKENILFGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 162 PLSALD----LKLRQAVRMELKQiqretGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK15439 167 PTASLTpaetERLFSRIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMRDGTI 218
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 5-227 7.65e-24

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: 98.36  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY-------RR 77
Cdd:TIGR02323   3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYqlseaerRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   78 PVNT----VFQHYALFPHMTVLENVMFGLQRLGWGVvDAEGRARQA----LELVHLS-AFLKRRPGQLSGGQQQRVALAR 148
Cdd:TIGR02323  83 LMRTewgfVHQNPRDGLRMRVSAGANIGERLMAIGA-RHYGNIRATaqdwLEEVEIDpTRIDDLPRAFSGGMQQRLQIAR 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733  149 ALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-220 1.06e-23

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: 102.78  E-value: 1.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI-APLPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    99 MFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMEL 178
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 384468733   179 kqIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTP 220
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
15-223 1.09e-23

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 98.52  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  15 FGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYR--RPVNTVFQHYALFPHM 92
Cdd:PRK10253  17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFG-------LQRLGWGVVDAEGRARQALELVHLSAflkRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK10253  97 TVQELVARGryphqplFTRWRKEDEEAVTKAMQATGITHLAD---QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
22-194 1.36e-23

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 96.41  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  22 HGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP-YRRPVNTVFQHYALFPHMTVLENVMF 100
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQDLLYLGHQPGIKTELTALENLRF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 101 gLQRLGwGVVDAEgRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDlklRQAVRMELKQ 180
Cdd:PRK13538  98 -YQRLH-GPGDDE-ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID---KQGVARLEAL 171

                        170
                 ....*....|....*..
gi 384468733 181 IQRET---GIAfVFVTH 194
Cdd:PRK13538 172 LAQHAeqgGMV-ILTTH 187
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 21-222 1.91e-23

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 101.44  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFpHMTVLENV 98
Cdd:COG5265  374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAIGIVPQDTVLF-NDTIAYNI 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 MFGlqRlgWGVVDAEgrARQALELVHLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:COG5265  453 AYG--R--PDASEEE--VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 168 LKLRQAVRMELKQIQRETG---IAFVFVThdqeeaLTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:COG5265  527 SRTERAIQAALREVARGRTtlvIAHRLST------IVDADEILVLEAGRIVERGTHAE 578
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
24-222 2.11e-23

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 101.01  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPY------------RRPVNTVFQHYALFPH 91
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavkkgmayiteSRRDNGFFPNFSIAQN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  92 MTVLENVMFGLQRLGWGVVDA--EGR-ARQALELVHLS-AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK09700 362 MAISRSLKDGGYKGAMGLFHEvdEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 168 LklrqAVRMELKQIQR---ETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:PRK09700 442 V----GAKAEIYKVMRqlaDDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 19-176 2.79e-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: 95.50  E-value: 2.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHY-ALFPHMTVLEN 97
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLpGLKPELSALEN 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733   98 VMFgLQRLGWGvvdAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDlklRQAVRM 176
Cdd:TIGR01189  94 LHF-WAAIHGG---AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD---KAGVAL 165
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
3-227 2.94e-23

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 97.17  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPL--PPYRRPVN 80
Cdd:PRK10575   9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFGlqRLGW-------GVVDAEgRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPE 153
Cdd:PRK10575  89 YLPQQLPAAEGMTVRELVAIG--RYPWhgalgrfGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 154 PRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 21-214 3.43e-23

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 96.19  E-value: 3.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG---GQIRLNGEdiaPLPPY--RRPVNTVFQHYALFPHMTVL 95
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDqfQKCVAYVRQDDILLPGLTVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 EN----VMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:cd03234  100 ETltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 384468733 172 QAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03234  180 LNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 20-195 4.22e-23

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 100.13  E-value: 4.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP--PYRRPVNTVFQHYALFpHMTVLEN 97
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVCAQDAHLF-DTTVREN 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   98 VMFGLQrlgwGVVDAEgrARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:TIGR02868 429 LRLARP----DATDEE--LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502

                         170       180
                  ....*....|....*....|....*....
gi 384468733  167 DLKLRQAVRMELkqIQRETGIAFVFVTHD 195
Cdd:TIGR02868 503 DAETADELLEDL--LAALSGRTVVLITHH 529
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-223 5.61e-23

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 96.43  E-value: 5.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG--------GQIRLNGEDIAPLPPYR----RPVNTVFQHYAl 88
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRlarlRAVLPQAAQPA- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  89 FPhMTVLENVMFG----LQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALA---------PEPR 155
Cdd:PRK13547  96 FA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 156 VLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 21-214 5.72e-23

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: 95.62  E-value: 5.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLPPY-----RRPVNTVFQHYALFPHmTVL 95
Cdd:cd03248   30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYehkylHSKVSLVGQEPVLFAR-SLQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGLQRLGWGVVDAEGRARQALELVHLSAF-----LKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKL 170
Cdd:cd03248  106 DNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 384468733 171 RQAVRMELKQIQRETGiafVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03248  186 EQQVQQALYDWPERRT---VLVIAHRLSTVERADQILVLDGGRI 226
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 21-223 1.08e-22

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 95.29  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPvSGGQIRLNGEDIAPLPP-----YR---------RPVNTVFQHY 86
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaelarHRaylsqqqspPFAMPVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALF-PHMTVLENVMFGLQRLgwgvvdaegrarqaLELVHLSAFLKRRPGQLSGGQQQRVALARALA-------PEPRVLL 158
Cdd:COG4138   91 ALHqPAGASSEAVEQLLAQL--------------AEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:COG4138  157 LDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 21-194 1.65e-22

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.34  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRL-NGEDIAPLP--PYrrpvntvfqhyalFPHMTVLEN 97
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrPY-------------LPLGTLREA 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQRLGWGvvDAEgrARQALELVHLSAFLKR------RPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:COG4178  446 LLYPATAEAFS--DAE--LREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521

                        170       180
                 ....*....|....*....|....
gi 384468733 172 QAVrmeLKQIQRET-GIAFVFVTH 194
Cdd:COG4178  522 AAL---YQLLREELpGTTVISVGH 542
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 21-225 2.11e-22

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 93.36  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFE--PVSGGQIRLNGEDIAPLPPYRRPVNTV---FQHYALFPHMTVL 95
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIflaFQYPPEIPGVKNA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFglqrlgwgvVDaEGrarqalelvhlsaflkrrpgqLSGGQQQRVALARALAPEPRVLLLDEPLSALDLklrQAVR 175
Cdd:cd03217   96 DFLRY---------VN-EG---------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALR 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 176 MELKQIQ--RETGIAFVFVTHDQEEALTM-SDRIAVMSDGRVQQVGtPREIYE 225
Cdd:cd03217  142 LVAEVINklREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELAL 193
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 6-220 2.81e-22

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: 93.33  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRF--GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPP--YRRPVNT 81
Cdd:cd03244    3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhdLRSRISI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYALFPHmTVLENVmfglqrlgwgvvDAEGRA-----RQALELVHLSAFLKRRPGQL-----------SGGQQQRVA 145
Cdd:cd03244   83 IPQDPVLFSG-TIRSNL------------DPFGEYsdeelWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 146 LARALAPEPRVLLLDEPLSALDL----KLRQAVRMELKQIqreTGIAfvfVTHdQEEALTMSDRIAVMSDGRVQQVGTP 220
Cdd:cd03244  150 LARALLRKSKILVLDEATASVDPetdaLIQKTIREAFKDC---TVLT---IAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-215 3.93e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.06  E-value: 3.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLnGE--DIAPLPpyrrpvnt 81
Cdd:COG0488  314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvKIGYFD-------- 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 vfQHYALF-PHMTVLENvmfgLQRLGWGvvDAEGRARQALElvhlsAFL------KRRPGQLSGGQQQRVALARALAPEP 154
Cdd:COG0488  385 --QHQEELdPDKTVLDE----LRDGAPG--GTEQEVRGYLG-----RFLfsgddaFKPVGVLSGGEKARLALAKLLLSPP 451

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQretGiAFVFVTHDQE--EALTmsDRIAVMSDGRVQ 215
Cdd:COG0488  452 NVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYflDRVA--TRILEFEDGGVR 508
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 21-220 5.72e-22

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 93.21  E-value: 5.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFE--PVSGGQIRLNGEDIAPLPPY---RRPVNTVFQHYALFPHMTV- 94
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDeraRAGIFLAFQYPVEIPGVSVs 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  95 --LENVMFGLQRLGWGVVDAEGRARQALELVHLSA-FLKRR--PGqLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:COG0396   96 nfLRTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYvnEG-FSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384468733 170 LRQAVRMELKQIqRETGIAFVFVTHdQEEALTM--SDRIAVMSDGRVQQVGTP 220
Cdd:COG0396  175 ALRIVAEGVNKL-RSPDRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-226 3.18e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 95.19  E-value: 3.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE-----DIAPlppyRRPVNTVFQHYA 87
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDIAT----RRRVGYMSQAFS 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFPHMTVLENVM-----FGLQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:NF033858 350 LYGELTVRQNLElharlFHLPA-----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 163 LSALDLKLRQAVRMELKQIQRETGIAfVFV-THDQEEALTmSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
14-224 1.60e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 89.68  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI----APLPPYRRPVNTVFQ--HYA 87
Cdd:PRK13638  10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRQQVATVFQdpEQQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFlKRRPGQ-LSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:PRK13638  90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 167 DLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
7-213 1.75e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 92.28  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   7 SIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaplpPYRRP-------- 78
Cdd:PRK11288   6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFAsttaalaa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 -VNTVFQHYALFPHMTVLENVMFGL--QRLGWgVVDAEGRARQALELVHL------SAFLKRrpgqLSGGQQQRVALARA 149
Cdd:PRK11288  80 gVAIIYQELHLVPEMTVAENLYLGQlpHKGGI-VNRRLLNYEAREQLEHLgvdidpDTPLKY----LSIGQRQMVEIAKA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 150 LAPEPRVLLLDEPLSALDLK----LRQAVRmELkqiqRETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAReieqLFRVIR-EL----RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 21-214 2.23e-20

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 91.99  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVF------QHYALFPHMTV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVyisedrKRDGLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  95 LENV-MFGLQRLGwgvvDAEGRARQALELVHLSAFLK----RRP------GQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:PRK10762 348 KENMsLTALRYFS----RAGGSLKHADEQQAVSDFIRlfniKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384468733 164 SALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 6-213 4.36e-20

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: 85.19  E-value: 4.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   6 ISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGGqirlngediaplppYRRPVNTVFQ 84
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGI--------------VTWGSTVKIG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYAlfphmtvlenvmfglqrlgwgvvdaegrarqalelvhlsaflkrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:cd03221   67 YFE-----------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 384468733 165 ALDLKLRQAVRMELKQIQRetgiAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:cd03221  100 HLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 21-227 1.03e-19

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 90.55  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLPPY-----RRPVNTVFQHYALFPHmTVL 95
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYdhhylHRQVALVGQEPVLFSG-SVR 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   96 ENVMFGLQRlgwgVVDAEGRARQALELVHlsAFLKRRP-----------GQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:TIGR00958 573 ENIAYGLTD----TPDEEIMAAAKAANAH--DFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATS 646

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733  165 ALDLKLRQAVRMELKQIQRetgiAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:TIGR00958 647 ALDAECEQLLQESRSRASR----TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 16-228 1.41e-19

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 88.24  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF---EPVSGGQIRLNGEDIAPLPPYR------RPVNTVFQH- 85
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQDp 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 -YALFPHMTVLENVMFGLQ-RLGWGVVDAEGRARQALELVHLSAFLKRR---PGQLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 161 EPLSALDLKLrQAVRMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:PRK09473 187 EPTTALDVTV-QAQIMTLlNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 19-218 1.76e-19

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: 84.67  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:cd03247   16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDTTLRNNL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 mfglqrlgwgvvdaeGRarqalelvhlsaflkrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMEL 178
Cdd:cd03247   96 ---------------GR-------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 384468733 179 KQIQRETGIafVFVTHdQEEALTMSDRIAVMSDGRVQQVG 218
Cdd:cd03247  142 FEVLKDKTL--IWITH-HLTGIEHMDKILFLENGKIIMQG 178
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 19-167 2.62e-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: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA-PLPPYRRPVNTVFQHYALFPHMTVLEN 97
Cdd:cd03231   14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfQRDSIARGLLYLGHAPGIKTTLSVLEN 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFglqrlgWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:cd03231   94 LRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 21-236 2.63e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 88.95  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP---VSGGQIRLNGEDIApLPPYRRPVNTVFQHYALFPHMTVLEN 97
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   98 VMFGLQ-RLGWGVVDAEGRAR--QALELVHLSAFLKRRPGQ------LSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:TIGR00955 120 LMFQAHlRMPRRVTKKEKRERvdEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733  169 KLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI--------YESPANRFVADFI 236
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNPADFY 275
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 22-228 2.83e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 85.91  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  22 HGVSVDIADNEFFTLLGPSGCGKTtlLRCIA--GFEP----VSGGQIRLNGEDIAPLPPYRRPVNTVFQH--YALFPHMT 93
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAalGILPagvrQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVMFGLQRLGWGVVDAegRARQALELVHLS---AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLkL 170
Cdd:PRK10418  98 MHTHARETCLALGKPADDA--TLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV-V 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 171 RQAVRMEL-KQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPA 228
Cdd:PRK10418 175 AQARILDLlESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
16-227 3.16e-19

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 87.27  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP----VSGGQIRLNGEDIAPLPPY------RRPVNTVFQH 85
Cdd:COG4170   18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRerrkiiGREIAMIFQE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 --YALFPHMTVLENVMFGL----------QRLGWgvvdaegRARQALELVHL------SAFLKRRPGQLSGGQQQRVALA 147
Cdd:COG4170   98 psSCLDPSAKIGDQLIEAIpswtfkgkwwQRFKW-------RKKRAIELLHRvgikdhKDIMNSYPHELTEGECQKVMIA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 148 RALAPEPRVLLLDEPLSALDLKLR-QAVRM--ELKQIQretGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIY 224
Cdd:COG4170  171 MAIANQPRLLIADEPTNAMESTTQaQIFRLlaRLNQLQ---GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247


                 ...
gi 384468733 225 ESP 227
Cdd:COG4170  248 KSP 250
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 11-223 7.70e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 84.60  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFTAlhgvsvDIADNEFFTLLGPSGCGKTTLLRCIAGFEPvSGGQIRLNGEDIAPLPP-----YR-------RP 78
Cdd:PRK03695   8 VSTRLGPLSA------EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelarHRaylsqqqTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNT--VFQHYALfpHMTVLENvmfglqrlgwgVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALA-------RA 149
Cdd:PRK03695  81 PFAmpVFQYLTL--HQPDKTR-----------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPD 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 150 LAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
16-219 8.76e-19

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 87.32  E-value: 8.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIA-GFEPvSGGQIRLNGEDIA--PLPPYRRPVNTVFQHYALFpHM 92
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDP-QSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLF-NR 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVmfglqRLGW-GVVDAEGRArqALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLD 160
Cdd:PRK13657 424 SIEDNI-----RVGRpDATDEEMRA--AAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILD 496

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 161 EPLSALDL----KLRQAVRmELKQiQRETgiafvFVTHDQEEALTMSDRIAVMSDGRVQQVGT 219
Cdd:PRK13657 497 EATSALDVeteaKVKAALD-ELMK-GRTT-----FIIAHRLSTVRNADRILVFDNGRVVESGS 552
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 16-254 8.89e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.60  E-value: 8.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKT----TLLRCI--AGFEPVSGGQ---------IRLNGEDIAPLPPYR-RPV 79
Cdd:PRK10261  27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMllrrrsrqvIELSEQSAAQMRHVRgADM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQH--YALFPHMTVLENVMFGLqRL--GWGVVDAEGRARQALELVHL---SAFLKRRPGQLSGGQQQRVALARALAP 152
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESI-RLhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 153 EPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRFV 232
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265

                        250       260
                 ....*....|....*....|..
gi 384468733 233 adfigETNLIEVPVLNISNGLA 254
Cdd:PRK10261 266 -----RALLAAVPQLGAMKGLD 282
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 20-219 1.17e-18

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 87.19  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP--PYRRPVNTVFQHYALFPHmTVLEN 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaALRQAISVVSQRVHLFSA-TLRDN 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQRLGwgvvdaEGRARQALELVHLSAFLKRRPG----------QLSGGQQQRVALARAL---APeprVLLLDEPLS 164
Cdd:PRK11160 434 LLLAAPNAS------DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALlhdAP---LLLLDEPTE 504

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 165 ALDLKL-RQAVRMELKQIQRETgiaFVFVTHdQEEALTMSDRIAVMSDGRVQQVGT 219
Cdd:PRK11160 505 GLDAETeRQILELLAEHAQNKT---VLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 11-197 1.62e-18

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 83.08  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLngeDIAPLPPYRRpvntvfqhyalfp 90
Cdd:COG2401   36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFGRE------------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 hMTVLENvmfglqrlgwgvVDAEGRARQALELVH---LS--AFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:COG2401  100 -ASLIDA------------IGRKGDFKDAVELLNavgLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 384468733 166 LDLKLRQAVRMELKQIQRETGIAFVFVTHDQE 197
Cdd:COG2401  167 LDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
20-239 1.82e-18

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 84.07  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaPLP----PYR-RPVNTVFQ--HYALFPHM 92
Cdd:PRK15112  28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHfgdySYRsQRIRMIFQdpSTSLNPRQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVLENVMFGLqRLGWGVvDAEGRARQALELVHLSAFLKRR----PGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PRK15112 105 RISQILDFPL-RLNTDL-EPEQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733 169 KLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP----ANRFVADFIGET 239
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 5-227 2.35e-18

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 84.41  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFG----TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF----EPVSGGQIRLNGEDIAPLPPYR 76
Cdd:PRK11022   3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  77 R------PVNTVFQH--YALFPHMTVLENVMFGLQRLGWGvvDAEGRARQALELVHL------SAFLKRRPGQLSGGQQQ 142
Cdd:PRK11022  83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 143 RVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240


                 ....*
gi 384468733 223 IYESP 227
Cdd:PRK11022 241 IFRAP 245
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 2-215 3.34e-18

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 85.37  E-value: 3.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   2 IGTVISidRVEKrfgtFTALHGVS--VDIADNEFFTL-----LGPSG---CGKTTLLRCIAGFEP-VSGGQIRLNGED-- 68
Cdd:PRK13549 255 IGEVIL--EVRN----LTAWDPVNphIKRVDDVSFSLrrgeiLGIAGlvgAGRTELVQCLFGAYPgRWEGEIFIDGKPvk 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  69 -----------IAPLPPYRRpvntvfqHYALFPHMTVLENVMFG-LQRL-GWGVVDAegrarqALELVHLSAFLKR---- 131
Cdd:PRK13549 329 irnpqqaiaqgIAMVPEDRK-------RDGIVPVMGVGKNITLAaLDRFtGGSRIDD------AAELKTILESIQRlkvk 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 132 ------RPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDR 205
Cdd:PRK13549 396 taspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDR 474

                        250
                 ....*....|
gi 384468733 206 IAVMSDGRVQ 215
Cdd:PRK13549 475 VLVMHEGKLK 484
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
21-226 9.84e-18

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 84.38  E-value: 9.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLP--PYRRPVNTVFQHyalfPhmTVLENV 98
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQD----P--VVLADT 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 MFGLQRLGWGVvdAEGRARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK10790 431 FLANVTLGRDI--SEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANID 508

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 168 LKLRQAVRMELKQIQRETgiAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PRK10790 509 SGTEQAIQQALAAVREHT--TLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
5-225 1.14e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.41  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlppyRRPVNTVFQ 84
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYA---------LFPHMTVLENV-----MFGLqrlgwgvvDAEGRARQALELVH---LSAFLKRRPGQLSGGQQQRVALA 147
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLdffgrLFGQ--------DAAERRRRIDELLRatgLAPFADRPAGKLSGGMKQKLGLC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 148 RALAPEPRVLLLDEPLSALD-LKLRQAvrMEL-KQIQRETGIAFVFV-THDQEEALTMsDRIAVMSDGRVQQVGTPREIY 224
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDpLSRRQF--WELiDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225


                 .
gi 384468733 225 E 225
Cdd:NF033858 226 A 226
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 4-246 1.53e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 83.51  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA---PLPPYRRPVN 80
Cdd:PRK10762   3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  81 TVFQHYALFPHMTVLENVMFG------LQRLGWGVVDAEGRARQA-LELVHLSaflKRRPGQLSGGQQQRVALARALAPE 153
Cdd:PRK10762  83 IIHQELNLIPQLTIAENIFLGrefvnrFGRIDWKKMYAEADKLLArLNLRFSS---DKLVGELSIGEQQMVEIAKVLSFE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 154 PRVLLLDEPLSAL-DLKLRQ--AVRMELkqiqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVqqvgtpreIYESPanr 230
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETESlfRVIREL----KSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--------IAERE--- 224

                        250
                 ....*....|....*.
gi 384468733 231 fVADfIGETNLIEVPV 246
Cdd:PRK10762 225 -VAD-LTEDSLIEMMV 238
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 27-233 2.45e-17

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: 80.14  E-value: 2.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  27 DIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRRPVNTvfqhyalfphMTVLENVMFGLQRLG 106
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYE----------GTVRDLLSSITKDFY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 107 wgvVDAEGRARQALELvHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQ-IQRET 185
Cdd:cd03237   91 ---THPYFKTEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfAENNE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 186 GIAFVfVTHDQEEALTMSDRIAVMsDGR--VQQVGTPREIYESPANRFVA 233
Cdd:cd03237  167 KTAFV-VEHDIIMIDYLADRLIVF-EGEpsVNGVANPPQSLRSGMNRFLK 214
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 36-194 2.60e-17

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: 78.35  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGFEPVSGGQI-RLNGEDIAPLPpyrrpvntvfQHyalfPHMTVlenvmfglqrlgwgvvdaeG 114
Cdd:cd03223   32 ITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLP----------QR----PYLPL-------------------G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 115 RARQALelvhlsaflkRRPGQ--LSGGQQQRVALARALAPEPRVLLLDEPLSALDlklrQAVRMELKQIQRETGIAFVFV 192
Cdd:cd03223   79 TLREQL----------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLYQLLKELGITVISV 144


                 ..
gi 384468733 193 TH 194
Cdd:cd03223  145 GH 146
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 14-265 3.21e-17

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 83.07  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    14 RFGTFT-------ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdIAPLPpyrrpvntvfqHY 86
Cdd:TIGR00957  640 HNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVP-----------QQ 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    87 ALFPHMTVLENVMFGLQRlgwgvvdAEGRARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPR 155
Cdd:TIGR00957  708 AWIQNDSLRENILFGKAL-------NEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNAD 780

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   156 VLLLDEPLSALDLKLRQAVrmeLKQIQRETGI----AFVFVTHDQeEALTMSDRIAVMSDGRVQQVGTPREIYESpaNRF 231
Cdd:TIGR00957  781 IYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQR--DGA 854

                          250       260       270
                   ....*....|....*....|....*....|....
gi 384468733   232 VADFIGETNLIEVPVLNISNGLAEVSLPGGRAIQ 265
Cdd:TIGR00957  855 FAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKL 888
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 19-231 3.45e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 82.45  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKT----TLLRCIAGfEPVS--GGQIRLNGEDI--APLPPYRR----PVNTVFQH- 85
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS-PPVVypSGDIRFHGESLlhASEQTLRGvrgnKIAMIFQEp 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  86 -YALFPHMTV---LENVMfGLQRlGWGVVDAEGRARQALELV---HLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:PRK15134 102 mVSLNPLHTLekqLYEVL-SLHR-GMRREAARGEILNCLDRVgirQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRF 231
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 4-195 4.47e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 79.77  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGF-EPVSGGQIRLNGEDIAPLPpyrrpvntv 82
Cdd:PRK09544   3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGKLRIGYVP--------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 fQHYALFPHMTV-LENVMfglqRLGWGVVDAEgrARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK09544  74 -QKLYLDTTLPLtVNRFL----RLRPGTKKED--ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHD 195
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 24-215 9.19e-17

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: 81.02  E-value: 9.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVS-GGQIRLNGEDIAplppYRRPVNTVFQHYALFPH----------M 92
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVD----IRNPAQAIRAGIAMVPEdrkrhgivpiL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   93 TVLENVMFG-LQRL-GWGVVDAE------GRARQALELVHLSAFLKrrPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:TIGR02633 355 GVGKNITLSvLKSFcFKMRIDAAaelqiiGSAIQRLKVKTASPFLP--IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 384468733  165 ALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQ 215
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-219 1.18e-16

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: 81.60  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlppyrrPVNTVFQHYALFPHMTVLENVM 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLL 2027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   100 FGLQRL-------GWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQ 172
Cdd:TIGR01257 2028 TGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 384468733   173 AVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGT 219
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
17-225 1.53e-16

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 80.83  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  17 TFT-------ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVNTVFQHYA 87
Cdd:PRK11176 348 TFTypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVH 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFpHMTVLENVMFGLQrlgwgvvDAEGRAR--QALELVHLSAFLKRRP-------GQ----LSGGQQQRVALARALAPEP 154
Cdd:PRK11176 428 LF-NDTIANNIAYART-------EQYSREQieEAARMAYAMDFINKMDngldtviGEngvlLSGGQRQRIAIARALLRDS 499

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 155 RVLLLDEPLSALDLKLRQAVRMELKQIQRETG---IAFVFVTHDQeealtmSDRIAVMSDGRVQQVGTPREIYE 225
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTslvIAHRLSTIEK------ADEILVVEDGEIVERGTHAELLA 567
GguA NF040905
sugar ABC transporter ATP-binding protein;
13-213 2.81e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 79.83  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPvSG---GQIRLNGE-----DIAPlpPYRRPVNTVFQ 84
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEvcrfkDIRD--SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 HYALFPHMTVLENVMFGLQRLGWGVVD---AEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:NF040905  86 ELALIPYLSIAENIFLGNERAKRGVIDwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 162 PLSALD-------LKLrqavRMELKqiqrETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:NF040905 166 PTAALNeedsaalLDL----LLELK----AQGITSIIISHKLNEIRRVADSITVLRDGR 216
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 24-214 4.76e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 78.94  E-value: 4.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRR-PVNTVF-----QHYALFPHMTVLEN 97
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VM-FGLQRLGWGVvdAEGRARQALELVHLSAFLK----RRP-GQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLR 171
Cdd:PRK15439 362 VCaLTHNRRGFWI--KPARENAVLERYRRALNIKfnhaEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 384468733 172 QAVRMELKQIQrETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK15439 440 NDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 8-214 5.03e-16

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: 75.76  E-value: 5.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   8 IDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG----FEPVSgGQIRLNGEDIAP-LPPYRRPVNTV 82
Cdd:cd03233   10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEfAEKYPGEIIYV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHYALFPHMTVLENVMFGLQRLGwgvvdaegrarqalelvhlSAFLKrrpgQLSGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:cd03233   89 SEEDVHFPTLTVRETLDFALRCKG-------------------NEFVR----GISGGERKRVSIAEALVSRASVLCWDNS 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 163 LSALD----LKLRQAVRMeLKQIQRETgiAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:cd03233  146 TRGLDsstaLEILKCIRT-MADVLKTT--TFVSLYQASDEIYDLFDKVLVLYEGRQ 198
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
24-214 1.53e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 77.64  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPlppyRRPVNTVFQHYAL----------FPHMT 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI----RSPRDAIRAGIMLcpedrkaegiIPVHS 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVMFGLQR--LGWG-VVDAEGRARQALELVHLSAFLKRRPGQ----LSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:PRK11288 348 VADNINISARRhhLRAGcLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384468733 167 DLklrqAVRMELKQI---QRETGIAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK11288 428 DV----GAKHEIYNViyeLAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 20-220 5.15e-15

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: 72.83  E-value: 5.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIA--PLPPYRRPVNTVFQHYALFPHmTVLEN 97
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 vmfglqrlgwgvVDAEGRARQalelVHLSAFLKRRPG--QLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVR 175
Cdd:cd03369  102 ------------LDPFDEYSD----EEIYGALRVSEGglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 384468733 176 melKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTP 220
Cdd:cd03369  166 ---KTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-229 5.90e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.15  E-value: 5.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaplpPYRRPVNTVFQHYA--------LFP 90
Cdd:PRK15056  21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQALQKNLVAYVpqseevdwSFP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 hMTVLENVMFG-LQRLGWgVVDAEGRARQ----ALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK15056  95 -VLVEDVVMMGrYGHMGW-LRRAKKRDRQivtaALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 166 LDLKLRQAVRMELKQIqRETGIAFVFVTHDQEEALTMSDrIAVMSDGRVQQVGtPREIYESPAN 229
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG-PTETTFTAEN 233
PLN03130 PLN03130
ABC transporter C family member; Provisional
 21-223 1.19e-14

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 75.54  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGGQIRLNGEdIAPLPPyrrpVNTVFqhyalfpHMTVLENVM 99
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-VAYVPQ----VSWIF-------NATVRDNIL 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  100 FGLQrlgwgvVDAEgRARQALELVHLSAFLKRRPG-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PLN03130  701 FGSP------FDPE-RYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  169 KLRQAV-----RMELKQIQRetgiafVFVThDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PLN03130  774 HVGRQVfdkciKDELRGKTR------VLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
16-227 2.78e-14

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 72.91  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP----VSGGQIRLNGEDIAPLPPYRR------PVNTVFQ- 84
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQe 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  85 -HYALFPHMTVLENVMFGL----------QRLGWgvvdaegRARQALELVHLSAF------LKRRPGQLSGGQQQRVALA 147
Cdd:PRK15093  98 pQSCLDPSERVGRQLMQNIpgwtykgrwwQRFGW-------RKRRAIELLHRVGIkdhkdaMRSFPYELTEGECQKVMIA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 148 RALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 21-204 5.45e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 69.98  E-value: 5.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP-LPPYRRPVNTVFQHYALFPHMTVLENVM 99
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 100 FGLQrlgwgvvdAEGRARQALELV---HLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDlKLRQAVRM 176
Cdd:PRK13540  97 YDIH--------FSPGAVGITELCrlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLTII 167

                        170       180
                 ....*....|....*....|....*...
gi 384468733 177 ELKQIQRETGIAFVFVTHdQEEALTMSD 204
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSH-QDLPLNKAD 194
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-207 5.72e-14

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: 72.66  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLnGEDIAplppyrrpVNTVFQ 84
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   85 -HYALFPHMTVLENVMFGLQRLGWGVVDAEGRArqalelvHLSAF------LKRRPGQLSGGQQQRVALARALAPEPRVL 157
Cdd:TIGR03719 393 sRDALDPNKTVWEEISGGLDIIKLGKREIPSRA-------YVGRFnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 384468733  158 LLDEPLSALDLKLRQAVRMELKQIqreTGIAFVfVTHDQeealTMSDRIA 207
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNF---AGCAVV-ISHDR----WFLDRIA 507
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
19-227 6.32e-14

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 72.82  E-value: 6.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHmTVLE 96
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVAN 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  97 NVMFGlqRLGWGVVDAEGRARqaLELVHLSAF---------LKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK10789 408 NIALG--RPDATQQEIEHVAR--LASVHDDILrlpqgydteVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 168 LKLRQAVRMELKQIQRETGiafVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PRK10789 484 GRTEHQILHNLRQWGEGRT---VIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 17-194 7.04e-14

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: 72.86  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   17 TFTALHGVSVDIadnefftlLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGE-DIAPLPpyRRPVNTV--FQHYALFPhMT 93
Cdd:TIGR00954 472 SFEVPSGNNLLI--------CGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QRPYMTLgtLRDQIIYP-DS 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   94 VLEnvmfgLQRLGWGVVDAEgrarQALELVHLSAFLKRRPG---------QLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:TIGR00954 541 SED-----MKRRGLSDKDLE----QILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190
                  ....*....|....*....|....*....|..
gi 384468733  165 ALdlklrqAVRME--LKQIQRETGIAFVFVTH 194
Cdd:TIGR00954 612 AV------SVDVEgyMYRLCREFGITLFSVSH 637
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 21-199 9.71e-14

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 71.97  E-value: 9.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEP-------VSGGQIRLNGEDIAPLP------------PYRrpVNT 81
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndlTLFGRRRGSGETIWDIKkhigyvssslhlDYR--VST 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 VFQHYAL---FPHMTVLENVMFGLQRLgwgvvdaegrARQALELVHLSAFLKRRPGQ-LSGGQQQRVALARALAPEPRVL 157
Cdd:PRK10938 354 SVRNVILsgfFDSIGIYQAVSDRQQKL----------AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLL 423

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 384468733 158 LLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEA 199
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 28-206 1.74e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 71.52  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  28 IADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI-APL---PPyRRPVNTVF-----------QHYALFPHM 92
Cdd:PRK11147  26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvARLqqdPP-RNVEGTVYdfvaegieeqaEYLKRYHDI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  93 TVL------ENVMFGLQRL--------GWGVvdaEGRARQALELVHLSAflKRRPGQLSGGQQQRVALARALAPEPRVLL 158
Cdd:PRK11147 105 SHLvetdpsEKNLNELAKLqeqldhhnLWQL---ENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQRetgiAFVFVTHDQEEALTMSDRI 206
Cdd:PRK11147 180 LDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 21-212 1.78e-13

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 68.90  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYA----LFPHMTVL 95
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAaqkpWLLNATVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  96 ENVMFGL----QRLGwGVVDAeGRARQALELVHL--SAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:cd03290   97 ENITFGSpfnkQRYK-AVTDA-CSLQPDIDLLPFgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 384468733 170 LRQAVRME-LKQIQRETGIAFVFVTHdQEEALTMSDRIAVMSDG 212
Cdd:cd03290  175 LSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-227 4.45e-13

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 70.58  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIrLNGEDIAPLPpyrrpvntvfqHYALFPHMTVLENVMF 100
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVP-----------QQAWIMNATVRGNILF 743

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  101 glqrlgwgvVDAEGRARQA-------LE--LVHLSAFLKRRPGQ----LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PTZ00243  744 ---------FDEEDAARLAdavrvsqLEadLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  168 LKLRQAVRMELKqIQRETGIAFVFVTHdQEEALTMSDRIAVMSDGRVQQVGTPREIYESP 227
Cdd:PTZ00243  815 AHVGERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
13-219 4.80e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 69.38  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  13 KRFGTFTALHGVSVDIADNEFFTLLGPSGCG--KTTLLRCI----AGFEPVSGGQIRLNGEDIAPLPPYRRPVNTVFQHy 86
Cdd:NF000106  21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*gpdAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRE- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 alfpHMTVLENVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
Cdd:NF000106 100 ----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 167 DLKLRQAVRMELKQIQREtGIAFVFVTHDQEEA------LTMSDRIAVMSDGRVQQVGT 219
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKT 233
PLN03211 PLN03211
ABC transporter G-25; Provisional
 19-222 5.43e-13

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 69.91  E-value: 5.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSG--GQIRLNGEDIAplPPYRRPVNTVFQHYALFPHMTVLE 96
Cdd:PLN03211  82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQDDILYPHLTVRE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  97 NVMF-GLQRL------------GWGVVDAEGRARQALELVHlSAFLKrrpgQLSGGQQQRVALARALAPEPRVLLLDEPL 163
Cdd:PLN03211 160 TLVFcSLLRLpksltkqekilvAESVISELGLTKCENTIIG-NSFIR----GISGGERKRVSIAHEMLINPSLLILDEPT 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 164 SALDLKLRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPRE 222
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
38-168 7.42e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 66.80  E-value: 7.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  38 GPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaplpPYRRPVNTVFQHY-----ALFPHMTVLENVMF--GLQRLgwgvv 110
Cdd:PRK13543  44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLENLHFlcGLHGR----- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468733 111 daegRARQ----ALELVHLSAFLKRRPGQLSGGQQQRVALARA-LAPEPrVLLLDEPLSALDL 168
Cdd:PRK13543 113 ----RAKQmpgsALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLDL 170
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 60-223 1.20e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 69.29  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   60 GQIRLNGEDIAP--LPPYRRPVNTVFQHYALFpHMTVLENVMFGLQrlgwgvvDAEGR-ARQALELVHLSAFLKRRPGQ- 135
Cdd:PTZ00265 1277 GKILLDGVDICDynLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE-------DATREdVKRACKFAAIDEFIESLPNKy 1348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  136 ----------LSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHdQEEALTMSDR 205
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427

                         170       180
                  ....*....|....*....|...
gi 384468733  206 IAVMSD-----GRVQQVGTPREI 223
Cdd:PTZ00265 1428 IVVFNNpdrtgSFVQAHGTHEEL 1450
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 31-208 2.04e-12

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: 64.32  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    31 NEFFTLLGPSGCGKTTLLRCIAGF-EPVSGGQIRLNGEDIaplppyrrpvntvfqhyalfphmtvlenvmfglqrlgwgv 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDI---------------------------------------- 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   110 vdaegraRQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME-----LKQIQRE 184
Cdd:smart00382  42 -------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 384468733   185 TGIAFVFVTHDQEEALTMSDRIAV 208
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
PLN03232 PLN03232
ABC transporter C family member; Provisional
 21-231 3.24e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 68.08  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHmtvleNV 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-----TV 1326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 MFGLQRLGwgvVDAEGRARQALELVHLSAFLKRRPGQL-----------SGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PLN03232 1327 RFNIDPFS---EHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733  168 LKLRQAVRmelKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRF 231
Cdd:PLN03232 1404 VRTDSLIQ---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
4-234 4.11e-12

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 67.14  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTaLHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGgqiRLNGE-DIAPLPPYRRPVnt 81
Cdd:PRK13409 339 TLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDEG---EVDPElKISYKPQYIKPD-- 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  82 vfqhyalfPHMTVLENVMFGLQRLGWGVVDAEgrARQALELVHLsafLKRRPGQLSGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK13409 413 --------YDGTVEDLLRSITDDLGSSYYKSE--IIKPLQLERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733 162 PLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDqeeaLTM----SDRIAVMSD--GRVQQVGTPREIYESpANRFVAD 234
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVFEGepGKHGHASGPMDMREG-MNRFLKE 553
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 24-222 8.61e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 66.15  E-value: 8.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  24 VSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSgGQIRLNGEDIAPLPP--YRRPVNTVFQHYALFPHMTVLEN--- 97
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQS-GEILLDGKPVTAEQPedYRKLFSAVFTDFHLFDQLLGPEGkpa 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 ----VMFGLQRLGwgvvdaegrARQALELVHlsafLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQA 173
Cdd:PRK10522 421 npalVEKWLERLK---------MAHKLELED----GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 174 VRMELKQIQRETGIAFVFVTHDqEEALTMSDRIAVMSDGRVQQV-GTPRE 222
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSELtGEERD 536
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 21-167 1.21e-11

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: 63.03  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVS--GGQIRLNGEdiaPLPP-YRRPVNTVFQHYALFPHMTVLEN 97
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKnFQRSTGYVEQQDVHSPNLTVREA 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFglqrlgwgvvdaegrarqalelvhlSAFLKrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:cd03232  100 LRF-------------------------SALLR----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 11-213 1.87e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 65.14  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDI---APLPPYRRPVNTVFQHYA 87
Cdd:PRK10982   4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFPHMTVLENVMFGLQRLGWGVVDAEGRARQA---LELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:PRK10982  84 LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTkaiFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384468733 165 ALDLKlrqAVRMELKQIQ--RETGIAFVFVTHDQEEALTMSDRIAVMSDGR 213
Cdd:PRK10982 164 SLTEK---EVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
PLN03073 PLN03073
ABC transporter F family; Provisional
 36-214 2.60e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 64.88  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAG-FEPVSGGQIRLNGEDIAplppyrrpvntVF-QHyalfpHMTVLE---NVMFGLQRLGWGVV 110
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMA-----------VFsQH-----HVDGLDlssNPLLYMMRCFPGVP 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 111 DAEGRArqalelvHLSAF-----LKRRPG-QLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQre 184
Cdd:PLN03073 604 EQKLRA-------HLGSFgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ-- 674

                        170       180       190
                 ....*....|....*....|....*....|
gi 384468733 185 TGIafVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PLN03073 675 GGV--LMVSHDEHLISGSVDELWVVSEGKV 702
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-231 2.85e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 64.80  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHmTVLENV 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 MFGLQRLG---WGVVDAEG-RARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPR-VLLLDEPLSALDLKLRqa 173
Cdd:PTZ00243 1405 DPFLEASSaevWAALELVGlRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALD-- 1482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733  174 vrmelKQIQRETGIAF----VFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREIYESPANRF 231
Cdd:PTZ00243 1483 -----RQIQATVMSAFsaytVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 4-208 2.92e-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: 64.42  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   4 TVISIDRVEKRFGTFTalhgVSVD---IADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGGqirLNGE-DIAPLPPYRRP 78
Cdd:COG1245  340 TLVEYPDLTKSYGGFS----LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGvLKPDEGE---VDEDlKISYKPQYISP 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 vntvfqhyalfphmtvlenvmfglqrlgwgvvDAEGRARQALELVHLSAF------------------LKRRPGQLSGGQ 140
Cdd:COG1245  413 --------------------------------DYDGTVEEFLRSANTDDFgssyykteiikplgleklLDKNVKDLSGGE 460

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 141 QQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTHDqeeaLTM----SDRIAV 208
Cdd:COG1245  461 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMV 528
PLN03232 PLN03232
ABC transporter C family member; Provisional
 21-226 4.49e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 64.23  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSGGQIRLNGEdIAPLPPyrrpVNTVFqhyalfpHMTVLENVM 99
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-VAYVPQ----VSWIF-------NATVRENIL 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  100 FGlqrlgwgvVDAE----GRARQALELVH-LSAFLKR-------RPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PLN03232  701 FG--------SDFEseryWRAIDVTALQHdLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733  168 LKLRQAV-----RMELKQIQRetgiafVFVThDQEEALTMSDRIAVMSDGRVQQVGTPREIYES 226
Cdd:PLN03232  773 AHVAHQVfdscmKDELKGKTR------VLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 3-167 5.87e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.60  E-value: 5.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   3 GTVISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLnGEdiaplppyrrpvnTV 82
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-------------TV 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  83 FQHY------ALFPHMTVLENVMFGLQRLGWGVVDAEGRArqalelvHLSAF-LK-----RRPGQLSGGQQQRVALARAL 150
Cdd:PRK11819 388 KLAYvdqsrdALDPNKTVWEEISGGLDIIKVGNREIPSRA-------YVGRFnFKggdqqKKVGVLSGGERNRLHLAKTL 460

                        170
                 ....*....|....*..
gi 384468733 151 APEPRVLLLDEPLSALD 167
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLD 477
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 21-223 7.39e-11

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: 63.81  E-value: 7.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSGSLRMNLD 1381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    99 MFGLQrlgwgvvdAEGRARQALELVHLSAFLKRRPGQL-----------SGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:TIGR00957 1382 PFSQY--------SDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733   168 LKLRQAVRMELKQiQRETGIAFVfVTHDQEEALTMSdRIAVMSDGRVQQVGTPREI 223
Cdd:TIGR00957 1454 LETDNLIQSTIRT-QFEDCTVLT-IAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
PLN03130 PLN03130
ABC transporter C family member; Provisional
 21-223 1.74e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.45  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHmtvleNV 98
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGIIPQAPVLFSG-----TV 1329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   99 MFGLQRLGWGVvDAEgrARQALELVHLSAFLKRRPGQL-----------SGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PLN03130 1330 RFNLDPFNEHN-DAD--LWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733  168 LKLRQAVRmelKQIQRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PLN03130 1407 VRTDALIQ---KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 134-214 1.87e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 62.05  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 134 GQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLklrqAVRMELKQI-----QRETGIafVFVTHDQEEALTMSDRIAV 208
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV----GAKFEIYQLiaelaKKDKGI--IIISSEMPELLGITDRILV 463


                 ....*.
gi 384468733 209 MSDGRV 214
Cdd:PRK10982 464 MSNGLV 469
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
17-235 1.98e-10

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 60.60  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  17 TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiaplppyrrpVNTVFQHYALFPHMTVLE 96
Cdd:PRK13546  36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  97 NVMFGLQRLGWGVVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVrm 176
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC-- 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 177 eLKQIQ--RETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI---YEspanRFVADF 235
Cdd:PRK13546 183 -LDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYE----AFLNDF 241
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 110-223 2.00e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 61.95  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 110 VDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQREtGIAF 189
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITL 188

                         90       100       110
                 ....*....|....*....|....*....|....
gi 384468733 190 VFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK10938 189 VLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 36-209 4.82e-10

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: 60.57  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGfepvsggQIRLNgediapLPPYRRPVN--TVFQHYA---LFPHMTVLEN------------- 97
Cdd:COG1245  104 ILGPNGIGKSTALKILSG-------ELKPN------LGDYDEEPSwdEVLKRFRgteLQDYFKKLANgeikvahkpqyvd 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 ----VMFG-----LQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDl 168
Cdd:COG1245  171 lipkVFKGtvrelLEK-----VDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD- 244

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 384468733 169 kLRQAVRMElKQIQR--ETGIAFVFVTHDqeeaLT----MSDRIAVM 209
Cdd:COG1245  245 -IYQRLNVA-RLIRElaEEGKYVLVVEHD----LAildyLADYVHIL 285
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 36-167 5.14e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAG-FEPVSgGQIRLNGE-DIAPLPPYRRpvntvfqhyALFPHMTVLENVMFGLQRlgwgvVDAE 113
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGqLQADS-GRIHCGTKlEVAYFDQHRA---------ELDPEKTVMDNLAEGKQE-----VMVN 414

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 114 GRARQALElvHLSAFL---KR--RPGQ-LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:PRK11147 415 GRPRHVLG--YLQDFLfhpKRamTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 36-195 5.71e-10

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: 60.33  E-value: 5.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   36 LLGPSGCGKTTLLRCIAGFEPVSGGQIRLN-GEDIAPLPpyrrpvntvfQHYALFPHMTVLENVMFGLQRlgwgVVDAEG 114
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLP----------QEPQLDPTKTVRENVEEGVAE----IKDALD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  115 R-------------------ARQAlEL---------------VHLSAFLKRRP------GQLSGGQQQRVALARALAPEP 154
Cdd:TIGR03719 102 RfneisakyaepdadfdklaAEQA-ELqeiidaadawdldsqLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKP 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 384468733  155 RVLLLDEPLSALDlklRQAVRMELKQIQRETGiAFVFVTHD 195
Cdd:TIGR03719 181 DMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 41-161 1.06e-09

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: 59.81  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  41 GCGKTTLLRCIAGFEPVSGGQIRLNGEDIAP--LPPYRRPVNTVFQHYALFPHmtvlenvMFGLQrlgwGVVDAEgRARQ 118
Cdd:COG4615  368 GSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREAYRQLFSAVFSDFHLFDR-------LLGLD----GEADPA-RARE 435

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 384468733 119 ALELVHLSAFLKRRPG-----QLSGGQQQRVALARALApEPR-VLLLDE 161
Cdd:COG4615  436 LLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALL-EDRpILVFDE 483
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 20-167 1.15e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 57.19  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFF----TLL--------GPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPpyrRPVNTVFQH-Y 86
Cdd:PRK13541   3 SLHQLQFNIEQKNLFdlsiTFLpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA---KPYCTYIGHnL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  87 ALFPHMTVLENVMFglqrlgWG-VVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK13541  80 GLKLEMTVFENLKF------WSeIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153


                 ..
gi 384468733 166 LD 167
Cdd:PRK13541 154 LS 155
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
36-195 1.37e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.44  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGfepvsggQIRLNgediapLPPYRRPVN--TVFQHYA---LFPHMTVLEN------------- 97
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSG-------ELIPN------LGDYEEEPSwdEVLKRFRgteLQNYFKKLYNgeikvvhkpqyvd 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 ----VMFG-----LQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDl 168
Cdd:PRK13409 171 lipkVFKGkvrelLKK-----VDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD- 244

                        170       180
                 ....*....|....*....|....*...
gi 384468733 169 kLRQAVRMElKQIQRET-GIAFVFVTHD 195
Cdd:PRK13409 245 -IRQRLNVA-RLIRELAeGKYVLVVEHD 270
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 36-167 1.56e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 58.98  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  36 LLGPSGCGKTTLLRCIAGFEPVSGGQIRL-NGEDIAPLPpyrrpvntvfQHYALFPHMTVLENVMFGLQrlgwGVVDAEG 114
Cdd:PRK11819  38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLP----------QEPQLDPEKTVRENVEEGVA----EVKAALD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 115 R-------------------ARQA-LE--LVHLSAF-LKRR-----------PG-----QLSGGQQQRVALARALAPEPR 155
Cdd:PRK11819 104 RfneiyaayaepdadfdalaAEQGeLQeiIDAADAWdLDSQleiamdalrcpPWdakvtKLSGGERRRVALCRLLLEKPD 183

                        170
                 ....*....|..
gi 384468733 156 VLLLDEPLSALD 167
Cdd:PRK11819 184 MLLLDEPTNHLD 195
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 16-219 1.63e-09

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 57.73  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  16 GTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGfEP---VSGGQIRLNGEDIAPLPPYRRP---VNTVFQHYALF 89
Cdd:CHL00131  18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  90 PHMTVLENVM--FGLQRLGWGVVDAEGRA-----RQALELVHLSA-FLKRRPGQ-LSGGQQQRVALARALAPEPRVLLLD 160
Cdd:CHL00131  97 PGVSNADFLRlaYNSKRKFQGLPELDPLEfleiiNEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384468733 161 EPLSALDLKLRQAVRMELKQIQRETGiAFVFVTHDQEeaL---TMSDRIAVMSDGRVQQVGT 219
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQR--LldyIKPDYVHVMQNGKIIKTGD 235
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 10-208 2.12e-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: 56.04  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  10 RVEKRFGTFTALHGVSvDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEDIAPLPPYRrpvntvfqhyalf 89
Cdd:cd03222    5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  90 phmtvlenvmfglqrlgwgvvdaegrarqalelvhlsaflkrrpgQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLK 169
Cdd:cd03222   71 ---------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 384468733 170 LRQAVRMELKQIQRETGIAFVFVTHDQEEALTMSDRIAV 208
Cdd:cd03222  106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 17-230 2.94e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 2.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    17 TFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIA----GFEPVSGGQIRLNG---EDIapLPPYRRPVNTVFQHYALF 89
Cdd:TIGR00956   73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEI--KKHYRGDVVYNAETDVHF 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    90 PHMTVLENVMF-----GLQRLGWGV---VDAEGRARQALELVHLSAFLKRRPGQ-----LSGGQQQRVALARALAPEPRV 156
Cdd:TIGR00956  151 PHLTVGETLDFaarckTPQNRPDGVsreEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468733   157 LLLDEPLSALDlklrQAVRME----LKQIQRET-GIAFVFVTHDQEEALTMSDRIAVMSDGrvqqvgtpREIYESPANR 230
Cdd:TIGR00956  231 QCWDNATRGLD----SATALEfiraLKTSANILdTTPLVAIYQCSQDAYELFDKVIVLYEG--------YQIYFGPADK 297
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 5-215 4.69e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 57.87  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   5 VISIDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPVSG-----GQIRLnGEDIAPLPPYRRP 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGeiglaKGIKL-GYFAQHQLEFLRA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  79 VNTVFQHYA-LFPHmtVLENVM------FGLQrlGWGVVDAEGRarqalelvhlsaflkrrpgqLSGGQQQRVALARALA 151
Cdd:PRK10636 391 DESPLQHLArLAPQ--ELEQKLrdylggFGFQ--GDKVTEETRR--------------------FSGGEKARLVLALIVW 446

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384468733 152 PEPRVLLLDEPLSALDLKLRQAVRMELkqIQRETgiAFVFVTHDQEEALTMSDRIAVMSDGRVQ 215
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEG--ALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 21-218 5.05e-09

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 56.34  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFE--PVSGGQIRLNGEDIAPLPPYRRPVNTVFQHYALFPHMTVLENV 98
Cdd:PRK09580  17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVSNQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  99 MFgLQRlgwgVVDA--EGRARQALELVHLSAFLKRRPGQL---------------SGGQQQRVALARALAPEPRVLLLDE 161
Cdd:PRK09580  97 FF-LQT----ALNAvrSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 162 PLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDQE-EALTMSDRIAVMSDGRVQQVG 218
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 21-223 1.11e-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: 56.84  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPvSGGQIRLNGE-DIAPLPPYRRPvntvfqhyalfphMTVLENV 98
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP-SEGKIKHSGRiSFSPQTSWIMP-------------GTIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    99 MFGLQRlgwgvvdAEGRARQALELVHLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
Cdd:TIGR01271  508 IFGLSY-------DEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733   168 LKLRQAV--RMELKQIQRETGIafvfVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:TIGR01271  581 VVTEKEIfeSCLCKLMSNKTRI----LVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
GguA NF040905
sugar ABC transporter ATP-binding protein;
134-214 1.18e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 56.34  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 134 GQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLklrqAVRMELKQIQRE---TGIAFVFVTHDQEEALTMSDRIAVMS 210
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV----GAKYEIYTIINElaaEGKGVIVISSELPELLGMCDRIYVMN 478


                 ....
gi 384468733 211 DGRV 214
Cdd:NF040905 479 EGRI 482
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 21-223 1.93e-08

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: 54.86  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAG-FEPvSGGQIRLNGEdiaplppyrrpVNTVFQHYALFPHmTVLENVM 99
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEP-SEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENII 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 100 FGLQRlgwgvvdAEGRARQALELVHLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:cd03291  120 FGVSY-------DEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384468733 169 KLRQAV--RMELKQIQRETGIafvFVTHDQEEaLTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:cd03291  193 FTEKEIfeSCVCKLMANKTRI---LVTSKMEH-LKKADKILILHEGSSYFYGTFSEL 245
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 14-209 2.06e-08

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 54.29  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  14 RFG--TFtALHGVSVdIADNEFFTLLGPSGCGKTTLLRCIAG------------------------------FEPVSGGQ 61
Cdd:cd03236    9 RYGpnSF-KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeildefrgselqnyFTKLLEGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  62 IRlngediaplpPYRRPvntvfQHYALFPHmTVLENVMFGLQRlgwgvVDAEGRARQALELVHLSAFLKRRPGQLSGGQQ 141
Cdd:cd03236   87 VK----------VIVKP-----QYVDLIPK-AVKGKVGELLKK-----KDERGKLDELVDQLELRHVLDRNIDQLSGGEL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 142 QRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGiAFVFVTHDQEEALTMSDRIAVM 209
Cdd:cd03236  146 QRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 19-216 1.52e-07

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 52.16  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  19 TALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGgQIRLNGE--DIAPLPPYRRPVNTVFQHYALFP---HMT 93
Cdd:cd03289   18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVswNSVPLQKWRKAFGVIPQKVFIFSgtfRKN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  94 VLENVMFGLQRLgWGVVDAEGrarqalelvhLSAFLKRRPGQL-----------SGGQQQRVALARALAPEPRVLLLDEP 162
Cdd:cd03289   97 LDPYGKWSDEEI-WKVAEEVG----------LKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 163 LSALDLKLRQAVRMELKQiqretgiAF----VFVTHDQEEALTMSDRIAVMSDGRVQQ 216
Cdd:cd03289  166 SAHLDPITYQVIRKTLKQ-------AFadctVILSEHRIEAMLECQRFLVIEENKVRQ 216
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 278-352 1.79e-07

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: 48.00  E-value: 1.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468733  278 LSVRPERIDLCAPSEAdLIATAGAQVYLGTDIQLKAHLAGGEQMTVRLQNAAAtVLPQSGARLGLRLEAGAARLL 352
Cdd:pfam08402   1 LAIRPEKIRLAAAANG-LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHA-RPPAPGDRVGLGWDPEDAHVL 73
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 20-219 3.73e-07

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: 49.63  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLlrCIAGFEPVsgGQIRLNGediAPLPPYRRPVNTVFQhyalfphmtvlenvm 99
Cdd:cd03238   10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYAS--GKARLIS---FLPKFSRNKLIFIDQ--------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 100 fgLQRLgwgvvdaegrarQALELVHLSafLKRRPGQLSGGQQQRVALARALA--PEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:cd03238   68 --LQFL------------IDVGLGYLT--LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEV 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 384468733 178 LKQIqRETGIAFVFVTHDqEEALTMSDRIAVMSDGRVQQVGT 219
Cdd:cd03238  132 IKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 11-209 4.96e-07

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: 48.90  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  11 VEKRFGTFtaLHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAgfepvsggqirlngediaplppyrrpvntvfqhYALFP 90
Cdd:cd03227    3 VLGRFPSY--FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGG 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  91 HMTVLENVMFGLQRlgwgvvdaEGRARQALELVHLSaflkrrpGQLSGGQQQRVALARALA---PEPRVL-LLDEPLSAL 166
Cdd:cd03227   48 AQSATRRRSGVKAG--------CIVAAVSAELIFTR-------LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGL 112

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 384468733 167 DLKLRQAV-RMELKQIQRetGIAFVFVTHDQEEALtMSDRIAVM 209
Cdd:cd03227  113 DPRDGQALaEAILEHLVK--GAQVIVITHLPELAE-LADKLIHI 153
PLN03073 PLN03073
ABC transporter F family; Provisional
 112-168 5.95e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 5.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384468733 112 AEGRARQALELVHLSAFL-KRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDL 168
Cdd:PLN03073 320 AEARAASILAGLSFTPEMqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-214 1.10e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 50.28  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   8 IDRVEKRFGTFTALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNgeDIAPLPPYRRpvntvfQHYA 87
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANIGYYAQ------DHAY 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  88 LFPH-MTVLEnVMFGLQRLGwgvvDAEGRARQAL-ELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
Cdd:PRK15064 394 DFENdLTLFD-WMSQWRQEG----DDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 384468733 166 LDLKLRQAVRMELKQIQretGiAFVFVTHDQEEALTMSDRIAVMSDGRV 214
Cdd:PRK15064 469 MDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGV 513
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 32-197 4.18e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.83  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  32 EFFTLL----GPSGCGKTTLLRCI--AGFepvsgGQIRLNGEDIAPLPPYRRP------VNTVFQH-----YALFPHMTV 94
Cdd:cd03240   19 EFFSPLtlivGQNGAGKTTIIEALkyALT-----GELPPNSKGGAHDPKLIREgevraqVKLAFENangkkYTITRSLAI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  95 LENVMFglqrlgwgvvdaegrarqalelVH---LSAFLKRRPGQLSGGQQQ------RVALARALAPEPRVLLLDEPLSA 165
Cdd:cd03240   94 LENVIF----------------------CHqgeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 384468733 166 LD-----LKLRQAVRMELKQIQRETGIafvfVTHDQE 197
Cdd:cd03240  152 LDeenieESLAEIIEERKSQKNFQLIV----ITHDEE 184
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 135-194 4.79e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 48.49  E-value: 4.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRMELKQIQRETGIAFVFVTH 194
Cdd:PTZ00265  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 21-180 1.82e-05

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: 46.83  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    21 LHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSgGQIRLNGE--DIAPLPPYRRPVNTVFQHYALFP---HMTVL 95
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVswNSVTLQTWRKAFGVIPQKVFIFSgtfRKNLD 1313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733    96 ENVMFGLQRLgWGVVDAEGrarqalelvhLSAFLKRRPGQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLS 164
Cdd:TIGR01271 1314 PYEQWSDEEI-WKVAEEVG----------LKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSA 1382

                          170
                   ....*....|....*.
gi 384468733   165 ALDLKLRQAVRMELKQ 180
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQ 1398
PLN03140 PLN03140
ABC transporter G family member; Provisional
 36-230 3.15e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 45.99  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733   36 LLGPSGCGKTTLLRCIAGfEPVSG---GQIRLNG-----EDIAPLPPYRRpvntvfQHYALFPHMTVLENVMF-GLQRLG 106
Cdd:PLN03140  911 LMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGfpkkqETFARISGYCE------QNDIHSPQVTVRESLIYsAFLRLP 983

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  107 WGVVDAEGR--ARQALELVHLSAfLKRR----PG--QLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKlRQAVRMEL 178
Cdd:PLN03140  984 KEVSKEEKMmfVDEVMELVELDN-LKDAivglPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR-AAAIVMRT 1061

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733  179 KQIQRETGIAFVFVTH----DQEEALtmsDRIAVMSDGrvQQVgtpreIYESPANR 230
Cdd:PLN03140 1062 VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG--GQV-----IYSGPLGR 1107
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 120-246 7.32e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.82  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  120 LELVHLSafLKRRPGQLSGGQQQRVALARALAPEPR--VLLLDEPlsALDLKLRQAVR-MELKQIQRETGIAFVFVTHDq 196
Cdd:PRK00635  463 LGLPYLT--PERALATLSGGEQERTALAKHLGAELIgiTYILDEP--SIGLHPQDTHKlINVIKKLRDQGNTVLLVEHD- 537

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733  197 EEALTMSDRI------AVMSDGRVQQVGTPREIYESpANRFVADFIGETNLIEVPV 246
Cdd:PRK00635  538 EQMISLADRIidigpgAGIFGGEVLFNGSPREFLAK-SDSLTAKYLRQELTIPIPE 592
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 38-220 1.27e-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: 42.97  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  38 GPSGCGKTTL----LRCIAGFEpvsgGQIRLNGEDIAPLPPY--RRPVNTVFQHYALFPHmtvleNVMFGLqrlgwgvvD 111
Cdd:cd03288   54 GRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILFSG-----SIRFNL--------D 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 112 AE-----GRARQALELVHLSAFLKRRPGQL-----------SGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAvr 175
Cdd:cd03288  117 PEckctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI-- 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468733 176 melkqIQRETGIAF-----VFVTHDQEEALTmSDRIAVMSDGRVQQVGTP 220
Cdd:cd03288  195 -----LQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 129-245 2.26e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 43.08  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  129 LKRRPGQLSGGQQQRVALARALAPE-PRVL-LLDEPlsALDLKLRQAVRM--ELKQIqRETGIAFVFVTHDqEEALTMSD 204
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEP--SIGLHQRDNRRLinTLKRL-RDLGNTLIVVEHD-EDTIRAAD 557

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 384468733  205 RI------AVMSDGRVQQVGTPREIYESPaNRFVADFIGETNLIEVP 245
Cdd:TIGR00630 558 YVidigpgAGEHGGEVVASGTPEEILANP-DSLTGQYLSGRKKIEVP 603
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 20-223 6.38e-04

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 41.41  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  20 ALHGVSVDIADNEFFTLLGPSGCGKTTLLRCIAGFEPVSGGQIRLNGEdiAPLPPYRRPVNTvfqhyalfpHMTVLENVM 99
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALIAISSGLNG---------QLTGIENIE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733 100 fgLQRLGWGVVDAEGR--ARQALELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRVLLLDEPLSALDLKLRQAVRME 177
Cdd:PRK13545 108 --LKGLMMGLTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 384468733 178 LKQIqRETGIAFVFVTHDQEEALTMSDRIAVMSDGRVQQVGTPREI 223
Cdd:PRK13545 186 MNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 21-206 7.15e-04

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: 40.32  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  21 LHGVSVDIADNEFFTLLGPSGCGKTTLlrciaGFEPV-SGGQIRLNgEDIAP-----LPPYRRP---------------V 79
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTIyAEGQRRYV-ESLSAyarqfLGQMDKPdvdsieglspaiaidQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  80 NTVFQHyalfPHMTV-----LENVMfglqRLGWGVVDAEGRARQALE--LVHLSafLKRRPGQLSGGQQQRVALARALAP 152
Cdd:cd03270   85 KTTSRN----PRSTVgtvteIYDYL----RLLFARVGIRERLGFLVDvgLGYLT--LSRSAPTLSGGEAQRIRLATQIGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 153 EPRVLL--LDEPLSALDLKLRQAVRMELKQIqRETGIAFVFVTHDqEEALTMSDRI 206
Cdd:cd03270  155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHV 208
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 18-212 1.48e-03

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: 39.56  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  18 FTALHGvsvdiadNEFFTLLGPSGCGKTTLLRCIAgfepvsggqIRLNGEDIAplppYRRPVNTvfqhYALFPHMTVLEN 97
Cdd:cd03279   22 FTGLDN-------NGLFLICGPTGAGKSTILDAIT---------YALYGKTPR----YGRQENL----RSVFAPGEDTAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468733  98 VMFGLQrLGWGV--------VDAEGRARQA-LELVHLSAFLKRRPGQLSGGQQQRVALARALAPEPRV----------LL 158
Cdd:cd03279   78 VSFTFQ-LGGKKyrversrgLDYDQFTRIVlLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEVLqnrggarleaLF 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384468733 159 LDEPLSALDLKLRQAVRMELKQIQREtGIAFVFVTHDQEEALTMSDRIAVMSDG 212
Cdd:cd03279  157 IDEGFGTLDPEALEAVATALELIRTE-NRMVGVISHVEELKERIPQRLEVIKTP 209
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 38-90 6.99e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 36.70  E-value: 6.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468733  38 GPSGCGKTTLLRCIA---GFEPVSGGQIRLN-----GEDIAPLPPYRRPVNTVFQHYALFP 90
Cdd:cd02020    6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTEevgklASEVAAIPEVRKALDERQRELAKKP 66
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 135-185 7.43e-03

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 37.62  E-value: 7.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384468733 135 QLSGGQQQRVALARALA-----PEPRVlLLDEPLSALDLKLRQAVRMELKQIQRET 185
Cdd:cd03272  158 QLSGGQKSLVALALIFAiqkcdPAPFY-LFDEIDAALDAQYRTAVANMIKELSDGA 212
 
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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