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Conserved domains on  [gi|1039033371|gb|ANM77566|]
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polyamine ABC transporter, ATP-binding family protein [Serratia marcescens]

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 ...
 1-338 6.43e-178

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.54  E-value: 6.43e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNT 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV 240
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 241 VRSELAQR--------------------LLGESRTFSIRPEHIRLleqgGAAQDEIQVQGTLQEIHYQGAATRYEIALNG 300
Cdd:COG3842   242 LPGTVLGDegggvrtggrtlevpadaglAAGGPVTVAIRPEDIRL----SPEGPENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039033371 301 GEKLLVSQANpqwiAEGLQRQIGQPIVACWPRAAMVPL 338
Cdd:COG3842   318 GQELVVRVPN----RAALPLEPGDRVGLSWDPEDVVVL 351
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-338 6.43e-178

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.54  E-value: 6.43e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNT 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV 240
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 241 VRSELAQR--------------------LLGESRTFSIRPEHIRLleqgGAAQDEIQVQGTLQEIHYQGAATRYEIALNG 300
Cdd:COG3842   242 LPGTVLGDegggvrtggrtlevpadaglAAGGPVTVAIRPEDIRL----SPEGPENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039033371 301 GEKLLVSQANpqwiAEGLQRQIGQPIVACWPRAAMVPL 338
Cdd:COG3842   318 GQELVVRVPN----RAALPLEPGDRVGLSWDPEDVVVL 351
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-308 1.43e-134

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 387.77  E-value: 1.43e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSE 244
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 245 LAQRLLG-------ESRTFSI----------------RPEHIRLLEQGGAAQDEIQVqGTLQEIHYQGAATRYEIALNGG 301
Cdd:PRK09452  255 VIERLDEqrvranvEGRECNIyvnfavepgqklhvllRPEDLRVEEINDDEHAEGLI-GYVRERNYKGMTLDSVVELENG 333


                  ....*..
gi 1039033371 302 EKLLVSQ 308
Cdd:PRK09452  334 KMVMVSE 340
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.64e-132

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: 376.96  E-value: 1.64e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVG 236
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 9-315 1.48e-114

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: 336.24  E-value: 1.48e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALF 88
Cdd:TIGR03265   9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:TIGR03265  89 PNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSELAQ- 247
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGg 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 248 ----------------RLLGESRTFSIRPEHIRLLEQGGAAQ------DEIQVQG-----TLQEIHYQGAATRYEIALNG 300
Cdd:TIGR03265 249 srarvggltlacapglAQPGASVRLAVRPEDIRVSPAGNAANlllarvEDMEFLGafyrlRLRLEGLPGQALVADVSASE 328

                         330
                  ....*....|....*
gi 1039033371 301 GEKLLVSQANPQWIA 315
Cdd:TIGR03265 329 VERLGIRAGQPIWIE 343
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
23-306 7.03e-88

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 267.71  E-value: 7.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGLM 102
Cdd:NF040840   19 ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQR 182
Cdd:NF040840   99 LRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHR 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 183 QLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV------------------VRSE 244
Cdd:NF040840  179 EFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIiegvaekggegtildtgnIKIE 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 245 LAQRLLGESRtFSIRPEHIRLLEQGGAAQDEIQVQGTLQEIHYQGAATRyeIALNGGEKLLV 306
Cdd:NF040840  259 LPEEKKGKVR-IGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVK--LTLDVGIILVA 317
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-161 6.91e-46

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: 153.19  E-value: 6.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371  98 AYGLMVKGVAKRERLARAQEALESVALGFVAERK----PAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-205 1.40e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 101.16  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNtvfqdyALFPhMSV 93
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGLMVK----GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039033371 170 REQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRV 205
Cdd:NF040873  155 RERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
3-222 2.07e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 104.44  E-value: 2.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRdVNT 80
Cdd:NF033858  265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRRR-VGY 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAygLMVK--GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:NF033858  344 MSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRQLGITfIFV-THDQSEALSmSDRVAVFNNGRIEQVDTPREL 222
Cdd:NF033858  422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-226 2.56e-18

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 84.79  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTtclrliagfeqltSGSIRIH--GQEAANLP-------PY 74
Cdd:NF000106   13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALPAHv*GPDAGRRPwrf*twcAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  75 QRDVNTVFQDY-----ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:NF000106   80 RRALRRTIG*Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEA------LSMSDRVAVFNNGRIEQVDTP---R 220
Cdd:NF000106  160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238


                  ....*.
gi 1039033371 221 ELYMRP 226
Cdd:NF000106  239 TLQIRP 244
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-161 1.26e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.94  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlppyQRDVNTVFQ 83
Cdd:NF033858    1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYA---------LFPHMSVLENVA-----YGLmvkgvAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:NF033858   77 RIAympqglgknLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                         170
                  ....*....|..
gi 1039033371 150 VNRPRVLLLDEP 161
Cdd:NF033858  152 IHDPDLLILDEP 163
GguA NF040905
sugar ABC transporter ATP-binding protein;
9-217 6.49e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 78.29  E-value: 6.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG------FEqltsGSIRIHGQEAANlppyqRDVN--- 79
Cdd:NF040905    6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEVCRF-----KDIRdse 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 -----TVFQDYALFPHMSVLENVAYGlmvKGVAKR------ERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARA 148
Cdd:NF040905   77 algivIIHQELALIPYLSIAENIFLG---NERAKRgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR-IEQVD 217
Cdd:NF040905  154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRtIETLD 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-204 2.05e-10

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: 58.54  E-value: 2.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   30 GEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeaanlppyqrdvntvfqdyalfphmsvlenvayglmvkgvakr 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  110 erLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD-----LKLREQMQGELKKLQRQL 184
Cdd:smart00382  38 --GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLLLKSEK 115

                          170       180
                   ....*....|....*....|
gi 1039033371  185 GITFIFVTHDQSEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-213 8.03e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.56  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG--FEQLTSGSIRIHGQEAanlppyqrDVNTVFQ-------------- 83
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEV--------DVSTVSDaidaglayvtedrk 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENV-AYGLmvKGVAKRERLARAQEALesvalgfVAER--------------KPAHLSGGQRQRVALARA 148
Cdd:NF040905  348 GYGLNLIDDIKRNItLANL--GKVSRRGVIDENEEIK-------VAEEyrkkmniktpsvfqKVGNLSGGNQQKVVLSKW 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:NF040905  419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-338 6.43e-178

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.54  E-value: 6.43e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNT 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV 240
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 241 VRSELAQR--------------------LLGESRTFSIRPEHIRLleqgGAAQDEIQVQGTLQEIHYQGAATRYEIALNG 300
Cdd:COG3842   242 LPGTVLGDegggvrtggrtlevpadaglAAGGPVTVAIRPEDIRL----SPEGPENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039033371 301 GEKLLVSQANpqwiAEGLQRQIGQPIVACWPRAAMVPL 338
Cdd:COG3842   318 GQELVVRVPN----RAALPLEPGDRVGLSWDPEDVVVL 351
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 4-335 2.75e-135

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 388.66  E-value: 2.75e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQ 83
Cdd:COG3839     3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:COG3839    83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 164 ALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTS--NVV 241
Cdd:COG3839   163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 242 RSELA-----------------QRLLGESRTFSIRPEHIRLLEQGGAAqdeiqVQGTLQEIHYQGAATRYEIALNGGEkl 304
Cdd:COG3839   243 PGTVEgggvrlggvrlplpaalAAAAGGEVTLGIRPEHLRLADEGDGG-----LEATVEVVEPLGSETLVHVRLGGQE-- 315

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1039033371 305 LVSQANPQwiaegLQRQIGQPIVACWPRAAM 335
Cdd:COG3839   316 LVARVPGD-----TRLRPGDTVRLAFDPERL 341
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-308 1.43e-134

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 387.77  E-value: 1.43e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSE 244
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 245 LAQRLLG-------ESRTFSI----------------RPEHIRLLEQGGAAQDEIQVqGTLQEIHYQGAATRYEIALNGG 301
Cdd:PRK09452  255 VIERLDEqrvranvEGRECNIyvnfavepgqklhvllRPEDLRVEEINDDEHAEGLI-GYVRERNYKGMTLDSVVELENG 333


                  ....*..
gi 1039033371 302 EKLLVSQ 308
Cdd:PRK09452  334 KMVMVSE 340
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.64e-132

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: 376.96  E-value: 1.64e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVG 236
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 1-333 3.09e-120

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 350.22  E-value: 3.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA-ANLPPYQRDVN 79
Cdd:COG1118     1 MSIEVR--NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG1118    79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSN 239
Cdd:COG1118   159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 240 VVRSEL--------------AQRLLGESRTFSIRPEHIRLLEQggaAQDEIQVQGTLQEIHYQGAATRYEIALNGGEKLL 305
Cdd:COG1118   239 VLRGRViggqleadgltlpvAEPLPDGPAVAGVRPHDIEVSRE---PEGENTFPATVARVSELGPEVRVELKLEDGEGQP 315

                         330       340
                  ....*....|....*....|....*...
gi 1039033371 306 VSQANPQWIAEGLQRQIGQPIVACWPRA 333
Cdd:COG1118   316 LEAEVTKEAWAELGLAPGDPVYLRPRPA 343
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 9-315 1.48e-114

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: 336.24  E-value: 1.48e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALF 88
Cdd:TIGR03265   9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:TIGR03265  89 PNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSELAQ- 247
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGg 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 248 ----------------RLLGESRTFSIRPEHIRLLEQGGAAQ------DEIQVQG-----TLQEIHYQGAATRYEIALNG 300
Cdd:TIGR03265 249 srarvggltlacapglAQPGASVRLAVRPEDIRVSPAGNAANlllarvEDMEFLGafyrlRLRLEGLPGQALVADVSASE 328

                         330
                  ....*....|....*
gi 1039033371 301 GEKLLVSQANPQWIA 315
Cdd:TIGR03265 329 VERLGIRAGQPIWIE 343
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-307 6.05e-112

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: 328.30  E-value: 6.05e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  35 MLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLAR 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 115 AQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHD 194
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 195 QSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSELAQRlLGESRTFS----------------- 257
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIER-KSEQVVLAgvegrrcdiytdvpvek 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 258 -------IRPEHIRLLEQGGAAQDEiQVQGTLQEIHYQGAATRYEIALNGGEKLLVS 307
Cdd:TIGR01187 240 dqplhvvLRPEKIVIEEEDEANSSN-AIIGHVIDITYLGMTLEVHVRLETGQKVLVS 295
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 5-217 6.52e-110

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: 319.08  E-value: 6.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
4-278 1.17e-101

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 303.30  E-value: 1.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVF 82
Cdd:PRK11650    3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:PRK11650   83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 163 GALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGT----- 237
Cdd:PRK11650  163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpamnl 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 238 ------SNVVRSELAQRL-----------LGESRTFSIRPEHIRLLEQGGAAQDEIQV 278
Cdd:PRK11650  243 ldgrvsADGAAFELAGGIalplgggyrqyAGRKLTLGIRPEHIALSSAEGGVPLTVDT 300
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 1-236 7.21e-101

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: 296.94  E-value: 7.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNT 80
Cdd:cd03296     1 MSIEVR--NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVKGVAKR----ERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVL 156
Cdd:cd03296    79 VFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVG 236
Cdd:cd03296   159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 5-217 2.44e-99

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: 292.24  E-value: 2.44e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
9-324 3.02e-99

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 297.02  E-value: 3.02e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALF 88
Cdd:PRK11432   11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK11432   91 PHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSN--------- 239
Cdd:PRK11432  171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANifpatlsgd 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 240 --------VVRSELAQRLLGESR-TFSIRPEHIRLLEQGGAAQdeiqvQGTLQEIHYQGAatRYEIALNGGEKLLVSQAN 310
Cdd:PRK11432  251 yvdiygyrLPRPAAFAFNLPDGEcTVGVRPEAITLSEQGEESQ-----RCTIKHVAYMGP--QYEVTVDWHGQELLLQVN 323

                         330
                  ....*....|....
gi 1039033371 311 PqwiaEGLQRQIGQ 324
Cdd:PRK11432  324 A----TQLQPDLGE 333
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-248 2.58e-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: 286.22  E-value: 2.58e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqr 76
Cdd:COG1116     4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DVNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVL 156
Cdd:COG1116    81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNN--GRI---EQVDTPrelymRPKTPFV 231
Cdd:COG1116   161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIveeIDVDLP-----RPRDREL 235

                         250       260
                  ....*....|....*....|
gi 1039033371 232 ---AEFVGTSNVVRSELAQR 248
Cdd:COG1116   236 rtsPEFAALRAEILDLLREE 255
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 5-241 1.14e-93

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 278.61  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVV 241
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
5-329 2.99e-92

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 279.61  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQD 84
Cdd:PRK11000    4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:PRK11000   84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGT------- 237
Cdd:PRK11000  164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkmnflp 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 238 -------SNVVRSELAQRLL------------GESRTFSIRPEHirLLEqggAAQDEIQVQGTLQEIHYQGAATRYEIAL 298
Cdd:PRK11000  244 vkvtataIEQVQVELPNRQQvwlpvegrgvqvGANMSLGIRPEH--LLP---SDIADVTLEGEVQVVEQLGNETQIHIQI 318

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1039033371 299 NGGEKLLV-SQANPQWIAEGLQRQIGQPIVAC 329
Cdd:PRK11000  319 PAIRQNLVyRQNDVVLVEEGATFAIGLPPERC 350
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 5-213 1.17e-90

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: 270.11  E-value: 1.17e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGD----VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqrDVNT 80
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNN--GRI 213
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
9-330 3.39e-90

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 274.79  E-value: 3.39e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALF 88
Cdd:PRK11607   24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK11607  104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNVVRSELAQR 248
Cdd:PRK11607  184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKER 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 249 ----LLGESR--------------------TFSIRPEHIRLLEQGGAAQDEIQVqGTLQEIHYQGAATRYEIALNGGEKL 304
Cdd:PRK11607  264 qedgLVIDSPglvhplkvdadasvvdnvpvHVALRPEKIMLCEEPPADGCNFAV-GEVIHIAYLGDLSIYHVRLKSGQMI 342

                         330       340
                  ....*....|....*....|....*.
gi 1039033371 305 LVSQANPQWIAEGLQRQiGQPIVACW 330
Cdd:PRK11607  343 SAQLQNAHRYRKGLPTW-GDEVRLCW 367
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 6-243 3.46e-90

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 272.35  E-value: 3.46e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGD-VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVF 82
Cdd:COG1125     3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVAL--GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:COG1125    83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV 240
Cdd:COG1125   163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGADRG 242


                  ...
gi 1039033371 241 VRS 243
Cdd:COG1125   243 LRR 245
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 20-240 1.77e-89

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: 268.05  E-value: 1.77e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAY 99
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 100 GLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKK 179
Cdd:cd03299    95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 180 LQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV 240
Cdd:cd03299   175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
23-306 7.03e-88

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 267.71  E-value: 7.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGLM 102
Cdd:NF040840   19 ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQR 182
Cdd:NF040840   99 LRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHR 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 183 QLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSNV------------------VRSE 244
Cdd:NF040840  179 EFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIiegvaekggegtildtgnIKIE 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 245 LAQRLLGESRtFSIRPEHIRLLEQGGAAQDEIQVQGTLQEIHYQGAATRyeIALNGGEKLLV 306
Cdd:NF040840  259 LPEEKKGKVR-IGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVK--LTLDVGIILVA 317
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1-245 4.92e-87

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 265.79  E-value: 4.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNT 80
Cdd:PRK10851    1 MSIEIA--NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLMVkgVAKRERLARA------QEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:PRK10851   79 VFQHYALFRHMTVFDNIAFGLTV--LPRRERPNAAaikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEF 234
Cdd:PRK10851  157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236

                         250
                  ....*....|.
gi 1039033371 235 VGTSNVVRSEL 245
Cdd:PRK10851  237 MGEVNRLQGTI 247
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 9-235 1.51e-81

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: 248.71  E-value: 1.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ------RDVNTVF 82
Cdd:cd03294    29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVF 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:cd03294   109 QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 163 GALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFV 235
Cdd:cd03294   189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 15-235 2.99e-81

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 252.33  E-value: 2.99e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ------RDVNTVFQDYALF 88
Cdd:COG4175    38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:COG4175   118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFV 235
Cdd:COG4175   198 IRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-214 4.85e-81

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 246.11  E-value: 4.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGD----VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR 76
Cdd:COG1136     1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DV--NT----VFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:COG1136    81 ARlrRRhigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQsEALSMSDRVAVFNNGRIE 214
Cdd:COG1136   161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 5-236 3.17e-79

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: 241.82  E-value: 3.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTV 81
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVAL--GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVG 236
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 5-213 4.12e-77

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 235.85  E-value: 4.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGD----VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRD--- 77
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 ---VNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:cd03255    81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEAlSMSDRVAVFNNGRI 213
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 20-302 1.23e-76

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: 239.51  E-value: 1.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQL--TSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:TIGR03258  21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRGLALLFQNYALFPHLKVEDNV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGEL 177
Cdd:TIGR03258 101 AFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMREEI 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 178 KKLQRQL-GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTSN----------------- 239
Cdd:TIGR03258 181 AALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANilpaialgiteapglvd 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 240 ------VVRSELAQRLLGESRTFSIRPEHIRLLEQGGAaqdEIQVQGTLQEIHYQGAATRYEIALNGGE 302
Cdd:TIGR03258 261 vscggaVIFAFGDGRHDGRDKLACIRPEHLALTPRPAG---EGRFHATIASVEWHGAALHLLCDLDAAC 326
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 5-212 1.75e-75

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: 230.15  E-value: 1.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ----EAANLPPYQRDVNT 80
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdLEDELPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLmvkgvakrerlaraqealesvalgfvaerkpahlSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:cd03229    81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 5-237 1.03e-71

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 222.56  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE----AANLPPYQRDVNT 80
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdsKKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLM-VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 160 EPLGALDlklrEQMQGE----LKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFV 235
Cdd:COG1126   162 EPTSALD----PELVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236


                  ..
gi 1039033371 236 GT 237
Cdd:COG1126   237 SK 238
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 5-229 1.24e-71

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: 230.95  E-value: 1.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-----AANLPPY 74
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsRRSLREL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  75 QRDVNTVFQD--YALFPHMSVLENVAYGLMVKGVA-KRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALV 150
Cdd:COG1123   341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-222 2.14e-70

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 219.16  E-value: 2.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQ 83
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 164 ALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 29-217 5.01e-69

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: 214.85  E-value: 5.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  29 DGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG------QEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGLm 102
Cdd:cd03297    22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 vKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQR 182
Cdd:cd03297   101 -KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039033371 183 QLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03297   180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
22-237 4.83e-67

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 210.38  E-value: 4.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  22 RVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGL 101
Cdd:COG3840    17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 102 MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV-NRPrVLLLDEPLGALDLKLREQMQGELKKL 180
Cdd:COG3840    97 RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVDEL 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 181 QRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGT 237
Cdd:COG3840   176 CRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-235 4.97e-67

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: 210.61  E-value: 4.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRD--- 77
Cdd:COG1127     2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 --VNTVFQDYALFPHMSVLENVAYGL-MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:COG1127    82 rrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 155 VLLLDEPLGALD-------LKLreqmqgeLKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELyMRPK 227
Cdd:COG1127   162 ILLYDEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASD 233


                  ....*...
gi 1039033371 228 TPFVAEFV 235
Cdd:COG1127   234 DPWVRQFL 241
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 5-228 6.95e-67

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: 209.88  E-value: 6.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTV 81
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitKKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQ--DYALFpHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG1122    81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT 228
Cdd:COG1122   160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-217 4.13e-66

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 207.60  E-value: 4.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANL-----PPYQRDV 78
Cdd:COG2884     2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRqLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVD 217
Cdd:COG2884   162 DEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
15-213 4.19e-66

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 208.95  E-value: 4.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlPPYQRDVntVFQDYALFPHMSVL 94
Cdd:COG4525    18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  95 ENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQ 174
Cdd:COG4525    95 DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQ 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039033371 175 GELKKLQRQLGITFIFVTHDQSEALSMSDRVAVF--NNGRI 213
Cdd:COG4525   175 ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-274 7.42e-66

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 211.09  E-value: 7.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ----- 75
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 156 LLLDEPLGALD-------LKLreqmqgeLKKLQRQLGITFIFVTHDqsealsMS------DRVAVFNNGRIEQVDTPREL 222
Cdd:COG1135   162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 223 YMRPKTPFVAEFVGTsnVVRSELAQRLLGESRTFSIRPEHIRLLEQGGAAQD 274
Cdd:COG1135   229 FANPQSELTRRFLPT--VLNDELPEELLARLREAAGGGRLVRLTFVGESADE 278
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-213 1.01e-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: 206.97  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-----PYQ 75
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQDY--ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGF---VAERKPAHLSGGQRQRVALARALV 150
Cdd:cd03257    82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 9-238 1.81e-64

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: 204.27  E-value: 1.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFG----DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA--ANLPPYQRDVNTVF 82
Cdd:COG1124     6 NLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFRRRVQMVF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDY--ALFPHMSVLENVAYGLMVKGVAKRERlaRAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG1124    86 QDPyaSLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLD 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTS 238
Cdd:COG1124   164 EPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLAAS 242
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 37-226 3.54e-64

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: 207.26  E-value: 3.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  37 GPSGSGKTTCLRLIAGFEQLTSGSIRIHG---QEAA---NLPPYQRDVNTVFQDYALFPHMSVLENVAYGLmvKGVAKRE 110
Cdd:COG4148    32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSArgiFLPPHRRRIGYVFQEARLFPHLSVRGNLLYGR--KRAPRAE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 111 RLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIF 190
Cdd:COG4148   110 RRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILY 189

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039033371 191 VTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:COG4148   190 VSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 5-227 2.16e-62

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 198.57  E-value: 2.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGD----VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-----AANLPPYQ 75
Cdd:cd03258     2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsGKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPK 227
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 5-213 5.36e-62

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: 196.98  E-value: 5.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE----AANLPPYQRDVNT 80
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddKKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYGLM-VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 160 EPLGALDlklrEQMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03262   161 EPTSALD----PELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 9-213 7.28e-61

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: 195.26  E-value: 7.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRD----VNTvFQD 84
Cdd:COG0411     9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgiART-FQN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVK-------------GVAKRER--LARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:COG0411    88 PRLFPELTVLENVLVAAHARlgrgllaallrlpRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG0411   168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 5-234 5.46e-60

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: 192.33  E-value: 5.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ-----RDVN 79
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHMSVLENVAYGLMVKGVAKRERL-ARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIrEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELyMRPKTPFVAEF 234
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 11-229 2.80e-59

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 193.79  E-value: 2.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  11 SRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-----PYQRDVNTVFQD- 84
Cdd:COG4608    25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrelrPLRRRMQMVFQDp 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YA-LFPHMSVLENVAYGLMVKGVA-KRERLARAQEALESVALG-FVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:COG4608   105 YAsLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLGITFIFVTHDqseaLSM----SDRVAVFNNGRI-EQVDTpRELYMRPKTP 229
Cdd:COG4608   185 VSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIvEIAPR-DELYARPLHP 252
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 6-222 3.66e-59

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: 190.45  E-value: 3.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQD 84
Cdd:COG4555     3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:COG4555    83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 165 LDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG4555   163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-223 7.45e-58

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 187.57  E-value: 7.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-----YQRD 77
Cdd:COG3638     2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHMSVLENVAYGL---------MVKGVAKRERlARAQEALESVALGFVAERKPAHLSGGQRQRVALARA 148
Cdd:COG3638    82 IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI------EQVDTP--R 220
Cdd:COG3638   161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVvfdgppAELTDAvlR 240


                  ...
gi 1039033371 221 ELY 223
Cdd:COG3638   241 EIY 243
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 9-213 8.21e-57

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: 184.18  E-value: 8.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDY 85
Cdd:cd03219     5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVA--------YGLMVKGVAKRER--LARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:cd03219    85 RLFPELTVLENVMvaaqartgSGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03219   165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 9-220 1.56e-56

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 184.50  E-value: 1.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRihgQEAANLPPYQRDVNTVFQDYALF 88
Cdd:PRK11247   17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPLAEAREDTRLMFQDARLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLmvKGVAKrerlARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK11247   94 PWKKVIDNVGLGL--KGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIE---QVDTPR 220
Cdd:PRK11247  168 TRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGldlTVDLPR 222
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 18-235 2.67e-56

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: 184.19  E-value: 2.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAA-----NLPPYQRDVNTVFQ--DYALFpH 90
Cdd:TIGR04521  19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQfpEHQLF-E 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:TIGR04521  98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 170 REQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT--------PFVAEFV 235
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDElekigldvPEITELA 251
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
5-234 9.22e-56

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 181.83  E-value: 9.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE----AANLPPYQRDVNT 80
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYG-LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 160 EPLGALDLKLREqmqgELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEF 234
Cdd:PRK09493  162 EPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 9-222 1.77e-55

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


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 180.45  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----TSGSIRIHGQEAANLPP----YQRDVN 79
Cdd:cd03260     5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVdvleLRRRVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPhMSVLENVAYGLMVKGVAKRERL-ARAQEALESVAL-GFVAER-KPAHLSGGQRQRVALARALVNRPRVL 156
Cdd:cd03260    85 MVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANEPEVL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQlgITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03260   164 LLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 9-212 2.45e-55

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: 179.59  E-value: 2.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQ- 83
Cdd:cd03225     4 NLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQn 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 -DYALFpHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:cd03225    84 pDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039033371 163 GALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:cd03225   163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-227 2.62e-55

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: 188.19  E-value: 2.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTF--GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG---FEQLTSGSIRIHGQEAANLPPYQ 75
Cdd:COG1123     1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 R--DVNTVFQD--YALFPhMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVN 151
Cdd:COG1123    81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPK 227
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 9-202 3.17e-55

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 179.21  E-value: 3.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF--EQLT-SGSIRIHGQEAANLPPYQRDVNTVFQDY 85
Cdd:COG4136     6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRIGILFQDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGLmVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:COG4136    86 LLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 166 DLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMS 202
Cdd:COG4136   165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 20-220 4.47e-55

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 179.58  E-value: 4.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqrDVNTVFQDYALFPHMSVLENVAy 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 100 gLMVKGV----AKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQG 175
Cdd:TIGR01184  77 -LAVDRVlpdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 176 ELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNN------GRIEQVDTPR 220
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 5-213 1.99e-54

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: 176.05  E-value: 1.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQ 83
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENVayglmvkgvakrerlaraqealesvalgfvaerkpaHLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039033371 164 ALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 1-221 5.09e-54

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: 176.86  E-value: 5.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFI----DVSRTFGD----VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP 72
Cdd:COG4181     1 MSSSSAPIielrGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  73 PYQR------DVNTVFQDYALFPHMSVLENVAYGLMVKGVakRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALA 146
Cdd:COG4181    81 EDARarlrarHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 147 RALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEAlSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:COG4181   159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 9-229 1.69e-53

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: 178.32  E-value: 1.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LTSGSIRIHGQEAANLPPYQ------ 75
Cdd:COG0444     6 NLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQD-Y-ALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVALGFVAERK---PAHLSGGQRQRVALARAL 149
Cdd:COG0444    86 REIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDTpRELYMRPKT 228
Cdd:COG0444   166 ALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEEGPV-EELFENPRH 244


                  .
gi 1039033371 229 P 229
Cdd:COG0444   245 P 245
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 22-213 6.92e-53

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: 173.45  E-value: 6.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  22 RVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGL 101
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 102 MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQ 181
Cdd:cd03298    96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039033371 182 RQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03298   176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 9-222 9.15e-53

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: 174.46  E-value: 9.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQDYA 86
Cdd:COG1120     6 NLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQEPP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  87 LFPHMSVLENVAYGLM----VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:COG1120    86 APFGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 163 GALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG1120   166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 12-229 2.73e-52

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: 180.65  E-value: 2.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  12 RTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTC----LRLIAgfeqlTSGSIRIHGQEAANLP-----PYQRDVNTVF 82
Cdd:COG4172   294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSrralrPLRRRMQVVF 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QD-YA-LFPHMSVLENVAYGLMV--KGVAKRERLARAQEALESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLL 157
Cdd:COG4172   369 QDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDTpRELYMRPKTP 229
Cdd:COG4172   449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQHP 520
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-222 2.87e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 172.97  E-value: 2.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP------PY 74
Cdd:COG1121     3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  75 QRDVNtvfqdyALFPhMSVLENVAYGLMVK----GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:COG1121    83 RAEVD------WDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI-----EQVDTPREL 222
Cdd:COG1121   156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPENL 231
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
10-202 3.58e-52

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 172.96  E-value: 3.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlPPYQRDVntVFQDYALFP 89
Cdd:PRK11248    7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEGLLP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:PRK11248   84 WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039033371 170 REQMQGELKKLQRQLGITFIFVTHDQSEALSMS 202
Cdd:PRK11248  164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 5-206 6.84e-52

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: 170.89  E-value: 6.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ-----RDV 78
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDqseaLSMSDRVA 206
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHD----LSLVDRVA 204
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
2-238 1.50e-51

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 171.52  E-value: 1.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   2 TIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE------------AA 69
Cdd:COG4598     6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrdgelvPA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  70 NLPPYQR---DVNTVFQDYALFPHMSVLENVAYG-LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVAL 145
Cdd:COG4598    86 DRRQLQRirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 146 ARALVNRPRVLLLDEPLGALDLKLreqmQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG4598   166 ARALAMEPEVMLFDEPTSALDPEL----VGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241

                         250
                  ....*....|....*.
gi 1039033371 223 YMRPKTPFVAEFVGTS 238
Cdd:COG4598   242 FGNPKSERLRQFLSSS 257
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 22-216 4.09e-51

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: 168.89  E-value: 4.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  22 RVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGL 101
Cdd:TIGR01277  16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 102 MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQ 181
Cdd:TIGR01277  96 HPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039033371 182 RQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQV 216
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 8-232 5.49e-51

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: 172.99  E-value: 5.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVrAVDrVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG---QEAAN---LPPYQRDVNTV 81
Cdd:TIGR02142   3 ARFSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLmvKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:TIGR02142  81 FQEARLFPHLSVRGNLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVA 232
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 5-213 4.94e-50

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: 166.04  E-value: 4.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANL-----PPYQRDV 78
Cdd:cd03292     1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03292   161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 6-213 5.43e-50

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 166.97  E-value: 5.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGD-VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-----YQRDVN 79
Cdd:cd03256     2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHMSVLENVAYGL---------MVKGVAKRERLaRAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:cd03256    82 MIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03256   161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-213 7.55e-50

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 165.37  E-value: 7.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQ 83
Cdd:COG4619     2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVPQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPhMSVLENVAYGLMVKGvaKRERLARAQEALESVALG-FVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:COG4619    82 EPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 163 GALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG4619   159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-235 1.38e-49

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 166.37  E-value: 1.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlTSGSIRIHGQE--AANL 71
Cdd:COG1117     8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDiyDPDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  72 PPYQ--RDVNTVFQDYALFPhMSVLENVAYGLMVKGVAKRERL-ARAQEALESVAL-GFVAER--KPA-HLSGGQRQRVA 144
Cdd:COG1117    86 DVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELdEIVEESLRKAALwDEVKDRlkKSAlGLSGGQQQRLC 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 145 LARALVNRPRVLLLDEPLGALD----LKLREQMQgELKKlqrqlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPR 220
Cdd:COG1117   165 IARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238

                         250
                  ....*....|....*
gi 1039033371 221 ELYMRPKTPFVAEFV 235
Cdd:COG1117   239 QIFTNPKDKRTEDYI 253
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 9-222 4.86e-49

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: 163.69  E-value: 4.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-PYQRDVNTVFQDYAL 87
Cdd:cd03265     5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQDLSV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 FPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL 167
Cdd:cd03265    85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 168 KLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03265   165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
22-213 5.12e-49

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 163.98  E-value: 5.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  22 RVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGL 101
Cdd:PRK10771   17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 102 ---MVKGVAKRERLaraQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELK 178
Cdd:PRK10771   97 npgLKLNAAQREKL---HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039033371 179 KLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK10771  174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 5-263 1.65e-48

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 163.76  E-value: 1.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF--GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE---AANLPPYQRDVN 79
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtldEENLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDyalfPH-----MSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:TIGR04520  81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALsMSDRVAVFNNGRIEQVDTPRELYMRPKT------ 228
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELlkeigl 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039033371 229 --PFVaefvgtsnvvrSELAQRLlgESRTFSIRPEHI 263
Cdd:TIGR04520 236 dvPFI-----------TELAKAL--KKRGIPLPPDIL 259
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 5-250 2.58e-48

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 165.74  E-value: 2.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ----- 75
Cdd:PRK11153    2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK11153   82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 156 LLLDEPLGALD-------LKLreqmqgeLKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT 228
Cdd:PRK11153  162 LLCDEATSALDpattrsiLEL-------LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234

                         250       260
                  ....*....|....*....|..
gi 1039033371 229 PFVAEFVGTsnVVRSELAQRLL 250
Cdd:PRK11153  235 PLTREFIQS--TLHLDLPEDYL 254
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 9-211 3.04e-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: 161.55  E-value: 3.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP------PYQRDVNTvf 82
Cdd:cd03235     4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSIDR-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 qdyaLFPhMSVLENVAYGLMVKGV----AKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:cd03235    82 ----DFP-ISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNG 211
Cdd:cd03235   157 DEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 1-234 1.47e-47

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 160.56  E-value: 1.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSrtFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE---AANLPPYQ-- 75
Cdd:PRK11124    1 MSIQLNGINCF--YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAir 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 ---RDVNTVFQDYALFPHMSVLENVAYGLM-VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVN 151
Cdd:PRK11124   79 elrRNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDtpRELYMRPKTPF 230
Cdd:PRK11124  159 EPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIvEQGD--ASCFTQPQTEA 235


                  ....
gi 1039033371 231 VAEF 234
Cdd:PRK11124  236 FKNY 239
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
19-234 4.21e-47

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 164.05  E-value: 4.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ------RDVNTVFQDYALFPHMS 92
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 173 MQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEF 234
Cdd:PRK10070  203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-234 8.77e-47

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 158.64  E-value: 8.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIavQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE---AANLPPYQ-- 75
Cdd:COG4161     1 MSI--QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAir 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 ---RDVNTVFQDYALFPHMSVLEN-VAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVN 151
Cdd:COG4161    79 llrQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDTprELYMRPKTPF 230
Cdd:COG4161   159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA--SHFTQPQTEA 235


                  ....
gi 1039033371 231 VAEF 234
Cdd:COG4161   236 FAHY 239
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 9-213 1.00e-46

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 157.35  E-value: 1.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGeFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRD-VNTVFQDYAL 87
Cdd:cd03264     5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 FPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL 167
Cdd:cd03264    84 YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039033371 168 KLREQMQGELKKLQRqlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03264   164 EERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKL 207
cbiO PRK13650
energy-coupling factor transporter ATPase;
20-225 2.28e-46

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 158.74  E-value: 2.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDY-ALFPHMSVLEN 96
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLltEENVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039033371 177 LKKLQRQLGITFIFVTHDQSEaLSMSDRVAVFNNGRIEQVDTPRELYMR 225
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 5-223 5.62e-46

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: 156.69  E-value: 5.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFG-DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN-----LPPYQRDV 78
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGL--------MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-161 6.91e-46

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: 153.19  E-value: 6.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371  98 AYGLMVKGVAKRERLARAQEALESVALGFVAERK----PAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 8-205 1.20e-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: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-----YQRD-VNTV 81
Cdd:TIGR03608   2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskFRREkLGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:TIGR03608  82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQlGITFIFVTHDQsEALSMSDRV 205
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 16-213 1.32e-45

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 154.82  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE----AANLPPYQRDVNT--VFQDYALFP 89
Cdd:TIGR02211  17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlsklSSNERAKLRNKKLgfIYQFHHLLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:TIGR02211  97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 170 REQMQGELKKLQRQLGITFIFVTHDQSEALSMsDRVAVFNNGRI 213
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-212 1.75e-44

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: 149.70  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQ 83
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 dyalfphmsvlenvayglmvkgvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:cd00267    81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039033371 164 ALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 9-213 9.65e-44

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: 148.74  E-value: 9.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRdvntvfqdyalf 88
Cdd:cd03214     4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL------------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 phmsvlenvayglmvkgvAKRerLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:cd03214    72 ------------------ARK--IAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03214   132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 12-237 1.03e-43

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 151.06  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  12 RTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIH----------GQEAANLPPYQRDVNTV 81
Cdd:PRK11264   11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLIRQLRQHVGFV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYG-LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:PRK11264   91 FQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLreqmQGELKKLQRQLG---ITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP----FVAE 233
Cdd:PRK11264  171 PTSALDPEL----VGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPrtrqFLEK 246


                  ....
gi 1039033371 234 FVGT 237
Cdd:PRK11264  247 FLLQ 250
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 5-222 1.51e-43

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: 149.58  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVR--AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-AANLPPYQRDVNTV 81
Cdd:cd03263     1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLgiTFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
18-223 1.76e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 151.35  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG----QEAANLPPYQRDVNTVFQ--DYALFPHm 91
Cdd:PRK13637   21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVKLSDIRKKVGLVFQypEYQLFEE- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYGLMVKGVAKRERLARAQEALESVALGF--VAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:PRK13637  100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 170 REQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13637  180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 15-222 1.89e-43

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: 149.12  E-value: 1.89e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDYALFPHM 91
Cdd:cd03224    11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYGlmvkgvAKRERLARAQEALESV-----ALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD 166
Cdd:cd03224    91 TVEENLLLG------AYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 167 LKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03224   165 PKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 4-222 5.26e-43

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: 157.69  E-value: 5.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVN 79
Cdd:COG2274   473 DIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIG 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFpHMSVLENVAYGlmvkgvAKRERLARAQEALESVALGFVAERKP-----------AHLSGGQRQRVALARA 148
Cdd:COG2274   553 VVLQDVFLF-SGTIRENITLG------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG2274   626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEEL 696
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 20-225 5.70e-43

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: 149.57  E-value: 5.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-----YQRDVNTVFQDY--ALFPHMS 92
Cdd:TIGR02769  27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLM-VKGVAKRERLARAQEALESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLR 170
Cdd:TIGR02769 107 VRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 171 EQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDTPRELYMR 225
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLLSFK 242
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 9-213 1.00e-42

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: 146.98  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQDYALF 88
Cdd:cd03268     5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMVKGVAKRerlaRAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:cd03268    85 PNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039033371 169 LREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03268   161 GIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
19-223 1.64e-42

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 148.62  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDY-ALFPHMSVLE 95
Cdd:PRK13635   22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlsEETVWDVRRQVGMVFQNPdNQFVGATVQD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  96 NVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQG 175
Cdd:PRK13635  102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039033371 176 ELKKLQRQLGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13635  182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
10-213 2.37e-42

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 147.91  E-value: 2.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-----PYQRDVNTVFQD 84
Cdd:PRK10419   18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 Y--ALFPHMSVLENVAYGLM-VKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:PRK10419   98 SisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK10419  178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 9-222 2.44e-42

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 147.44  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ---RDVNTVFQDY 85
Cdd:PRK11300   10 GLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLEN--VAYGLMVK-GV------------AKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:PRK11300   90 RLFREMTVIENllVAQHQQLKtGLfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMV 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK11300  170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-213 3.33e-42

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 152.87  E-value: 3.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqRD--- 77
Cdd:COG1129     1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDaqa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 --VNTVFQDYALFPHMSVLENVAYGLMVKG---VAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNR 152
Cdd:COG1129    79 agIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 153 PRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG1129   159 ARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1-198 3.40e-42

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: 145.70  E-value: 3.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVN 79
Cdd:COG4133     1 MMLEAE--NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHMSVLENVAYGLMVKGVAKRErlARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG4133    79 YLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039033371 160 EPLGALDLKLREQMQGELKKlQRQLGITFIFVTHDQSEA 198
Cdd:COG4133   157 EPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 23-213 1.41e-41

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: 144.39  E-value: 1.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-----AANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:TIGR02982  24 INLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQElhgasKKQLVQLRRRIGYIFQAHNLLGFLTARQNV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AYGL-MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:TIGR02982 104 QMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVEL 183

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 177 LKKLQRQLGITFIFVTHDqSEALSMSDRVAVFNNGRI 213
Cdd:TIGR02982 184 MQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 9-213 1.81e-41

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: 144.05  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVR----AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-PYQRDVNTVFQ 83
Cdd:cd03266     6 ALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLGFVSD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:cd03266    86 STGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039033371 164 ALDLKLREQMQgELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03266   166 GLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 5-212 3.87e-41

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: 141.75  E-value: 3.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNT 80
Cdd:cd03228     1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFpHMSVLENVayglmvkgvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGR 212
Cdd:cd03228   123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 5-213 6.89e-41

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: 142.42  E-value: 6.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPpyQRDVNTVFQD 84
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039033371 165 LDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03269   159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 9-213 2.12e-40

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 142.53  E-value: 2.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFG-----DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR--DVNTV 81
Cdd:COG1101     6 NLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYAL--FPHMSVLENVA--------YGLmVKGVAKRERlARAQEALESVALGFvAER---KPAHLSGGQRQRVALARA 148
Cdd:COG1101    86 FQDPMMgtAPSMTIEENLAlayrrgkrRGL-RRGLTKKRR-ELFRELLATLGLGL-ENRldtKVGLLSGGQRQALSLLMA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQ-MqgEL-KKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG1101   163 TLTKPKLLLLDEHTAALDPKTAALvL--ELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 15-222 4.30e-40

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: 140.89  E-value: 4.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDYALFPHM 91
Cdd:COG0410    14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENvaygLMVkGVAKRERLARAQEALESV-ALgF--VAERK--PA-HLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:COG0410    94 TVEEN----LLL-GAYARRDRAEVRADLERVyEL-FprLKERRrqRAgTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 166 DLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG0410   168 APLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
4-222 6.29e-39

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 145.31  E-value: 6.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSrtF---GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDV 78
Cdd:COG1132   339 EIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQI 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFpHMSVLENVAYGlmvKGVAKRERLaraQEALESVALGFVAERKP-----------AHLSGGQRQRVALAR 147
Cdd:COG1132   417 GVVPQDTFLF-SGTIRENIRYG---RPDATDEEV---EEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 148 ALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:COG1132   490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEEL 561
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 18-226 8.12e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 139.38  E-value: 8.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI------HGQEAANLPPYQRDVNTVFQ--DYALFP 89
Cdd:PRK13634   21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HmSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK13634  101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:PRK13634  180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 4-213 1.72e-38

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: 136.18  E-value: 1.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPY--QRDVN 79
Cdd:cd03245     2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFpHMSVLENVAYGlmvKGVAKRERLARAQE---ALESVAL---GF---VAERKpAHLSGGQRQRVALARALV 150
Cdd:cd03245    82 YVPQDVTLF-YGTLRDNITLG---APLADDERILRAAElagVTDFVNKhpnGLdlqIGERG-RGLSGGQRQAVALARALL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRI 213
Cdd:cd03245   157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
23-205 1.94e-38

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 136.48  E-value: 1.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE------AANLPPYQRDVNTVFQDYALFPHMSVLEN 96
Cdd:PRK11629   28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssAAKAELRNQKLGFIYQFHHLLPDFTALEN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:PRK11629  108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187

                         170       180
                  ....*....|....*....|....*....
gi 1039033371 177 LKKLQRQLGITFIFVTHDQSEALSMSDRV 205
Cdd:PRK11629  188 LGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 15-229 2.29e-38

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: 142.90  E-value: 2.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKT----TCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ------RDVNTVFQD 84
Cdd:COG4172    21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 --YALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVALGfVAERK----PAHLSGGQRQRVALARALVNRPRVLL 157
Cdd:COG4172   101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIP-DPERRldayPHQLSGGQRQRVMIAMALANEPDLLI 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI-EQVDTpRELYMRPKTP 229
Cdd:COG4172   180 ADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIvEQGPT-AELFAAPQHP 251
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 9-223 2.49e-38

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: 136.13  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDY 85
Cdd:cd03218     5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:cd03218    85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 166 DLKLREQMQGELKKLqRQLGITfIFVT-HDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:cd03218   165 DPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
8-238 3.38e-38

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 136.64  E-value: 3.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE---------------AANLP 72
Cdd:PRK10619    9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadKNQLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  73 PYQRDVNTVFQDYALFPHMSVLENVAYG-LMVKGVAKRERLARAQEALESVALGFVAERK-PAHLSGGQRQRVALARALV 150
Cdd:PRK10619   89 LLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 151 NRPRVLLLDEPLGALDlklrEQMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPK 227
Cdd:PRK10619  169 MEPEVLLFDEPTSALD----PELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244

                         250
                  ....*....|.
gi 1039033371 228 TPFVAEFVGTS 238
Cdd:PRK10619  245 SPRLQQFLKGS 255
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-213 3.92e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 137.55  E-value: 3.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQeaanlpPYQRDVNTVFq 83
Cdd:COG4152     1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE------PLDPEDRRRI- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DY-----ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:COG4152    74 GYlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG4152   154 DEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
9-221 1.00e-37

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 135.24  E-value: 1.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ----RDVntVFQD 84
Cdd:COG4559     6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YAL-FPhMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV-------NRPRVL 156
Cdd:COG4559    84 SSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:COG4559   163 FLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 4-221 2.05e-37

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: 141.93  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTF-GDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPY--QRDVN 79
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIG 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFpHMSVLENVAYGlmvKGVAKRERLARAQEA------LESVALGF---VAERKpAHLSGGQRQRVALARALV 150
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG---APYADDEEILRAAELagvtefVRRHPDGLdmqIGERG-RSLSGGQRQAVALARALL 617

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMqgeLKKLQRQL-GITFIFVTHDQSeALSMSDRVAVFNNGRIeQVDTPRE 221
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTHRTS-LLDLVDRIIVMDNGRI-VADGPKD 684
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-223 3.37e-37

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 133.62  E-value: 3.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---D 77
Cdd:COG1137     2 MTLEAE--NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLL 157
Cdd:COG1137    80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKL-QRQLGitfIFVT-HDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:COG1137   160 LDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-222 4.73e-37

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: 139.17  E-value: 4.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   7 FIDVSRtfGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIH-GQEAANLPP--------YQRD 77
Cdd:TIGR03269 289 YISVDR--GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKpgpdgrgrAKRY 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHMSVLENVAYGLmvkGVAKRERLARAQEALESVALGF-------VAERKPAHLSGGQRQRVALARALV 150
Cdd:TIGR03269 367 IGILHQEYDLYPHRTVLDNLTEAI---GLELPDELARMKAVITLKMVGFdeekaeeILDKYPDELSEGERHRVALAQVLI 443

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-213 5.42e-37

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 140.63  E-value: 5.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--- 73
Cdd:PRK10535    1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdal 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  74 --YQRD-VNTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:PRK10535   81 aqLRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEAlSMSDRVAVFNNGRI 213
Cdd:PRK10535  161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-227 5.55e-37

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 133.36  E-value: 5.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAV-QFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----TSGSIRIHGQEA----AN 70
Cdd:PRK14239    1 MTEPIlQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysprTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  71 LPPYQRDVNTVFQDYALFPhMSVLENVAYGLMVKGVAKRERLARAQEA--------------LESVALGfvaerkpahLS 136
Cdd:PRK14239   81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKslkgasiwdevkdrLHDSALG---------LS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 137 GGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLgiTFIFVTHDQSEALSMSDRVAVFNNGRIEQV 216
Cdd:PRK14239  151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEY 228

                         250
                  ....*....|.
gi 1039033371 217 DTPRELYMRPK 227
Cdd:PRK14239  229 NDTKQMFMNPK 239
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 3-223 8.42e-37

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: 139.12  E-value: 8.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGD-VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVN 79
Cdd:COG4988   335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIA 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFpHMSVLENVaygLMVKGVAKRERLaraQEALESVALGFVAERKP-----------AHLSGGQRQRVALARA 148
Cdd:COG4988   415 WVPQNPYLF-AGTIRENL---RLGRPDASDEEL---EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSEALSMsDRVAVFNNGRIEQVDTPRELY 223
Cdd:COG4988   488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELL 559
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
8-230 9.46e-37

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 135.39  E-value: 9.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVRAvdRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ------EAANLPPYQRDVNTV 81
Cdd:PRK11144    4 LNFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaeKGICLPPEKRRIGYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLmvkgvaKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK11144   82 FQDARLFPHYKVRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 162 LGALDL-KLREQMQgELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY----MRPKTPF 230
Cdd:PRK11144  156 LASLDLpRKRELLP-YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWassaMRPWLPK 228
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 18-230 4.74e-36

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 132.91  E-value: 4.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR-----DVNTVFQD--YALFPH 90
Cdd:PRK15079   35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYGLMV--KGVAKRERLARAQEALESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL 167
Cdd:PRK15079  115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 168 KLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PRK15079  195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-222 5.30e-36

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 135.92  E-value: 5.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqRD--- 77
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDaia 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 --VNTVFQDYALFPHMSVLENVAYGlMVKGVAKRERLARAQEALESVA--LGFV--AERKPAHLSGGQRQRVALARALVN 151
Cdd:COG3845    80 lgIGMVHQHFMLVPNLTVAENIVLG-LEPTKGGRLDRKAARARIRELSerYGLDvdPDAKVEDLSVGEQQRVEILKALYR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR-IEQVD----TPREL 222
Cdd:COG3845   159 GARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKvVGTVDtaetSEEEL 233
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 5-213 5.59e-36

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 127.93  E-value: 5.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPY---QRDVNTV 81
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQdyalfphmsvlenvayglmvkgvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:cd03216    81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03216   110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 16-235 6.74e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 130.97  E-value: 6.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE----AANLPPYQRDVNTVFQ--DYALF- 88
Cdd:PRK13639   14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydKKSLLEVRKTVGIVFQnpDDQLFa 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PhmSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK13639   94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 169 LREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT--------PFVAEFV 235
Cdd:PRK13639  172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETirkanlrlPRVAHLI 245
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 1-221 1.03e-35

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 130.28  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRtfGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ----R 76
Cdd:PRK13548    1 AMLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DVntVFQDYAL-FPhMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV----- 150
Cdd:PRK13548   79 AV--LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 151 -NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:PRK13548  156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-213 4.40e-35

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: 128.28  E-value: 4.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFE-QLTSGSIRIHGQE--AANLppyqRD--- 77
Cdd:COG1119     3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERrgGEDV----WElrk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 ----VNTVFQDYaLFPHMSVLENVAYGLM-VKGVAKR---ERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:COG1119    79 riglVSPALQLR-FPRDETVLDVVLSGFFdSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG1119   158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 16-223 4.80e-35

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 127.66  E-value: 4.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFPhMSV 93
Cdd:cd03249    15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGL------MVKGVAKrerLARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03249    94 AENIRYGKpdatdeEVEEAAK---KANIHDFIMSLPDGYdtlVGERG-SQLSGGQKQRIAIARALLRNPKILLLDEATSA 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 165 LDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:cd03249   170 LDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
cbiO PRK13640
energy-coupling factor transporter ATPase;
4-226 5.74e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 128.76  E-value: 5.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVR--AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF---EQLTSGSIRIHGQE--AANLPPYQR 76
Cdd:PRK13640    5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITltAKTVWDIRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DVNTVFQDY-ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK13640   85 KVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEAlSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:PRK13640  165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 17-230 7.33e-35

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 129.70  E-value: 7.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ-----RDVNTVFQD-YA-LFP 89
Cdd:PRK11308   28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMVK-GVAKRERLARAQEALESVALgfvaerKPAH-------LSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK11308  108 RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGL------RPEHydryphmFSGGQRQRIAIARALMLDPDVVVADEP 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PRK11308  182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 9-235 1.02e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 127.34  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----TSGSIRIHGQEAANLP--PYQRDVNTV 81
Cdd:PRK14247    8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDviELRRRVQMV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVLENVAYGLMVKGVA--KRERLARAQEALESVAL-GFVAER--KPA-HLSGGQRQRVALARALVNRPRV 155
Cdd:PRK14247   88 FQIPNPIPNLSIFENVALGLKLNRLVksKKELQERVRWALEKAQLwDEVKDRldAPAgKLSGGQQQRLCIARALAFQPEV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRQLgiTFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFV 235
Cdd:PRK14247  168 LLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 15-214 2.40e-34

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: 125.72  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLppyqrDVNTVFQdyalfPHMSVL 94
Cdd:cd03220    33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  95 ENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQ 174
Cdd:cd03220   103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039033371 175 GELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIE 214
Cdd:cd03220   183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
5-213 4.35e-34

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 124.99  E-value: 4.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANL-----PPYQRDV 78
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:PRK10908   82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRqLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK10908  162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 9-228 4.53e-34

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: 125.46  E-value: 4.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDY 85
Cdd:TIGR04406   6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQEA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGL-MVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:TIGR04406  86 SIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 165 LDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT 228
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKV 228
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 5-223 6.95e-34

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: 124.65  E-value: 6.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN--LPPYQRDVNT 80
Cdd:cd03251     1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFpHMSVLENVAYGlmvKGVAKRE------RLARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVN 151
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAYG---RPGATREeveeaaRAANAHEFIMELPEGYdtvIGERG-VKLSGGQRQRIAIARALLK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:cd03251   156 DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 1-213 8.64e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 125.62  E-value: 8.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGD-VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRD 77
Cdd:PRK13647    1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnAENEKWVRSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDY--ALFPhMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK13647   81 VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK13647  160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 4-226 1.08e-33

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: 130.27  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTF--GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVN 79
Cdd:COG4987   333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIA 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFpHMSVLENVaygLMVKGVAKRERLAraqEALESVALGFVAERKP-----------AHLSGGQRQRVALARA 148
Cdd:COG4987   413 VVPQRPHLF-DTTLRENL---RLARPDATDEELW---AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSEALSMsDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:COG4987   486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 23-198 1.34e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 123.74  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR------DVNTVFQDYALFPHMSVLEN 96
Cdd:PRK10584   29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALEN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:PRK10584  109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188

                         170       180
                  ....*....|....*....|..
gi 1039033371 177 LKKLQRQLGITFIFVTHDQSEA 198
Cdd:PRK10584  189 LFSLNREHGTTLILVTHDLQLA 210
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 11-230 2.15e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 129.98  E-value: 2.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  11 SRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ-----RDVNTVFQD- 84
Cdd:PRK10261  331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDp 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YA-LFPHMSVLENVAYGLMVKGVAKRERLA-RAQEALESVALGFV-AERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK10261  411 YAsLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PRK10261  491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
cbiO PRK13642
energy-coupling factor transporter ATPase;
16-223 4.21e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 124.05  E-value: 4.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDY-ALFPHMS 92
Cdd:PRK13642   19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltAENVWNLRRKIGMVFQNPdNQFVGAT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13642   99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 173 MQGELKKLQRQLGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13642  179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-270 7.02e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 124.15  E-value: 7.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRD-VN 79
Cdd:PRK13537    4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK13537   84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPFVAEFVGTS- 238
Cdd:PRK13537  164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIYGPDp 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039033371 239 NVVRSELA-----QRLLGESRTFSIR---PEHIRLLEQGG 270
Cdd:PRK13537  243 VALRDELAplaerTEISGETLFCYVRdpePLHARLKGRAG 282
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 1-213 2.13e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 122.50  E-value: 2.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFG-----DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTclrLIAGFEQL---TSGSIRI-----HGQE 67
Cdd:PRK13651    1 MQIKVK--NIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNALllpDTGTIEWifkdeKNKK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  68 AANL-----------PPY----------QRDVNTVFQ--DYALFpHMSVLENVAYGLMVKGVAKRERLARAQEALESVAL 124
Cdd:PRK13651   76 KTKEkekvleklviqKTRfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 125 --GFVaERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMS 202
Cdd:PRK13651  155 deSYL-QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWT 232

                         250
                  ....*....|.
gi 1039033371 203 DRVAVFNNGRI 213
Cdd:PRK13651  233 KRTIFFKDGKI 243
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 1-235 3.18e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 120.72  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLT-----SGSIRIHGQ----EAANL 71
Cdd:PRK14267    1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniysPDVDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  72 PPYQRDVNTVFQDYALFPHMSVLENVAYGLMVKGVA--KRERLARAQEALESVAL-GFVAER---KPAHLSGGQRQRVAL 145
Cdd:PRK14267   81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVksKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 146 ARALVNRPRVLLLDEPLGALD---LKLREQMQGELKKlqrqlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK14267  161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235

                         250
                  ....*....|...
gi 1039033371 223 YMRPKTPFVAEFV 235
Cdd:PRK14267  236 FENPEHELTEKYV 248
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 5-223 3.57e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 121.01  E-value: 3.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF-GDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ--EAANLPPYQRDVNT 80
Cdd:PRK13648    8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaiTDDNFEKLRKHIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQD-YALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK13648   88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13648  168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
15-229 4.04e-32

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 120.71  E-value: 4.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEaanLPP--YQ---RDVNTVFQD--YAL 87
Cdd:COG4167    24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LEYgdYKyrcKHIRMIFQDpnTSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 FPHMSVlenvayGLMVKGVAK-------RERLARAQEALESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:COG4167   101 NPRLNI------GQILEEPLRlntdltaEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIAD 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:COG4167   175 EALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 20-213 4.07e-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: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFPHmSVLENV 97
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYLPQDDELFSG-SIAENI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 ayglmvkgvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKlREQMQGEL 177
Cdd:cd03246    97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQA 138

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039033371 178 KKLQRQLGITFIFVTHdQSEALSMSDRVAVFNNGRI 213
Cdd:cd03246   139 IAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 12-225 4.12e-32

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 125.59  E-value: 4.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  12 RTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTC----LRLIAgfeqlTSGSIRIHGQEAANLP-----PYQRDVNTVF 82
Cdd:PRK15134  294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVF 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QD--YALFPHMSVLENVAYGLMV--KGVAKRERLARAQEALESVALGFVA-ERKPAHLSGGQRQRVALARALVNRPRVLL 157
Cdd:PRK15134  369 QDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLII 448

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGR-IEQVD------TPRELYMR 225
Cdd:PRK15134  449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDcervfaAPQQEYTR 523
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 2-222 7.09e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.48  E-value: 7.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   2 TIAVQFIDVSRTFGDVR--AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRD 77
Cdd:PRK13632    5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITisKENLKEIRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQ--DYAlFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK13632   85 IGIIFQnpDNQ-FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALsMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK13632  164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 5-222 8.31e-32

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: 119.26  E-value: 8.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAV-DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN--LPPYQRDVNTV 81
Cdd:cd03253     1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFpHMSVLENVAYGLM------VKGVAKRerlARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVNR 152
Cdd:cd03253    81 PQDTVLF-NDTIGYNIRYGRPdatdeeVIEAAKA---AQIHDKIMRFPDGYdtiVGERG-LKLSGGEKQRVAIARAILKN 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 153 PRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03253   156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 8-213 1.13e-31

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: 118.13  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDV-RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlPPYQRDVNTVFQD-- 84
Cdd:cd03226     3 ENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDvd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHmSVLENVAYGLMVKGvakrERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03226    82 YQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039033371 165 LDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03226   157 LDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
cbiO PRK13641
energy-coupling factor transporter ATPase;
18-227 1.21e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 120.32  E-value: 1.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE------AANLPPYQRDVNTVFQ--DYALFP 89
Cdd:PRK13641   21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgNKNLKKLRKKVSLVFQfpEAQLFE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HmSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK13641  101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 169 LREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPK 227
Cdd:PRK13641  180 GRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 9-230 1.36e-31

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 120.98  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTF----GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF---EQLTSGSIRIHGQEAANLPPYQ------ 75
Cdd:PRK09473   17 DLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklra 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  76 RDVNTVFQD--YALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVALGFVAERK---PAHLSGGQRQRVALARAL 149
Cdd:PRK09473   97 EQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMAL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:PRK09473  177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHP 256


                  .
gi 1039033371 230 F 230
Cdd:PRK09473  257 Y 257
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 23-213 1.87e-31

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: 118.01  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDYALFPHMSVLENVAY 99
Cdd:TIGR03410  19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVEENLLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 100 GLMVKGVAKRERLARAQE---ALESVAlgfvaERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:TIGR03410  99 GLAALPRRSRKIPDEIYElfpVLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 177 LKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:TIGR03410 174 IRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
cbiO PRK13649
energy-coupling factor transporter ATPase;
1-223 4.59e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 118.31  E-value: 4.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFG-----DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN----- 70
Cdd:PRK13649    1 MGINLQ--NVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  71 -LPPYQRDVNTVFQdyalFPHM-----SVLENVAYGLMVKGVAKRERLARAQEALESVALG-FVAERKPAHLSGGQRQRV 143
Cdd:PRK13649   79 dIKQIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 144 ALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13649  155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 4-235 6.55e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 117.46  E-value: 6.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTF---GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ-----------EAA 69
Cdd:PRK14246    7 AEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqiDAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  70 NLppyQRDVNTVFQDYALFPHMSVLENVAYGLMVKGVA-KRERLARAQEALESVAL-GFVAER--KPA-HLSGGQRQRVA 144
Cdd:PRK14246   87 KL---RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRlnSPAsQLSGGQQQRLT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 145 LARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlgITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYM 224
Cdd:PRK14246  164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241

                         250
                  ....*....|.
gi 1039033371 225 RPKTPFVAEFV 235
Cdd:PRK14246  242 SPKNELTEKYV 252
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 25-222 1.17e-30

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 115.72  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  25 IDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeaANLPPYQRDVNTVFQ------DYALFPHMSVLENVA 98
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQrhefawDFPISVAHTVMSGRT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  99 yGLMvkGVAKRERLA---RAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQG 175
Cdd:TIGR03771  78 -GHI--GWLRRPCVAdfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039033371 176 ELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFnNGRIEQVDTPREL 222
Cdd:TIGR03771 155 LFIELA-GAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-223 1.39e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 117.11  E-value: 1.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG---QEAANLPPYQRDVNTVFQ--DYALFPHMsV 93
Cdd:PRK13633   25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQnpDNQIVATI-V 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGLMVKGVAKRERLARAQEALESVALgFVAERKPAH-LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13633  104 EEDVAFGPENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 173 MQGELKKLQRQLGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13633  183 VVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 9-228 2.25e-30

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 115.95  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYA 86
Cdd:COG4604     6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILRQENH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  87 LFPHMSVLENVAYGLM--VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:COG4604    86 INSRLTVRELVAFGRFpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELyMRPKT 228
Cdd:COG4604   166 LDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-ITPEV 228
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 21-222 2.81e-30

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 121.22  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  21 DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAA--NLPPYQRDVNTVFQDYALFPHmSVLENVA 98
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFENIA 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  99 YGLMVKgvakrerLARAQEALESVALGFVAERKP-----------AHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL 167
Cdd:TIGR03797 549 GGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEATSALDN 621

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 168 KLREQMQGELKKLQrqlgITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR03797 622 RTQAIVSESLERLK----VTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDEL 671
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-221 8.04e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.02  E-value: 8.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTF----------------------GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTS 58
Cdd:COG1134     1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  59 GSIRIHGQEAANLppyqrDVNTVFQdyalfPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGG 138
Cdd:COG1134    81 GRVEVNGRVSALL-----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 139 QRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDT 218
Cdd:COG1134   151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229


                  ...
gi 1039033371 219 PRE 221
Cdd:COG1134   230 PEE 232
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-255 1.19e-29

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 117.25  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQfiDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDV 78
Cdd:PRK09536    2 PMIDVS--DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHMSVLENVAYGLmvkgVAKRERLARA--------QEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:PRK09536   80 ASVPQDTSLSFEFDVRQVVEMGR----TPHRSRFDTWtetdraavERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 151 NRPRVLLLDEPLGALDLklreQMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRP- 226
Cdd:PRK09536  156 QATPVLLLDEPTASLDI----NHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADt 231

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039033371 227 -KTPFVAE-FVGTSNVVRSELAQRLLGESRT 255
Cdd:PRK09536  232 lRAAFDARtAVGTDPATGAPTVTPLPDPDRT 262
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 4-236 1.31e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 114.42  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRL-------IAGFEQltSGSIRIHGQEAAN---LPP 73
Cdd:PRK14271   21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSIFNyrdVLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  74 YQRDVNTVFQDYALFPhMSVLENVAYGLMV-KGVAKRERLARAQEALESVAL-GFVAER---KPAHLSGGQRQRVALARA 148
Cdd:PRK14271   99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLART 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLgiTFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT 228
Cdd:PRK14271  178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255


                  ....*...
gi 1039033371 229 PFVAEFVG 236
Cdd:PRK14271  256 AETARYVA 263
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-220 4.50e-29

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 112.80  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF----------EQLTSGSIRIHGQEAAN 70
Cdd:PRK09984    1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  71 LPPYQRDVNTVFQDYALFPHMSVLENVAYGLMvkGVA----------KRERLARAQEALESVALGFVAERKPAHLSGGQR 140
Cdd:PRK09984   81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 141 QRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVA------VFNNGRIE 214
Cdd:PRK09984  159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIValrqghVFYDGSSQ 238


                  ....*.
gi 1039033371 215 QVDTPR 220
Cdd:PRK09984  239 QFDNER 244
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 19-222 4.88e-29

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 111.81  E-value: 4.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFpHMSVLEN 96
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQENVLF-NRSIRDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAY---GLMVKGVAKRERLARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLR 170
Cdd:cd03252    96 IALadpGMSMERVIEAAKLAGAHDFISELPEGYdtiVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 171 EQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03252   175 HAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 5-222 8.13e-29

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: 111.16  E-value: 8.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTV 81
Cdd:cd03254     3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHmSVLENVAYG---LMVKGVAKRERLARAQEALESVALGFVAERKPA--HLSGGQRQRVALARALVNRPRVL 156
Cdd:cd03254    83 LQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENggNLSQGERQLLAIARAMLRDPKIL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:cd03254   162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDEL 224
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 5-222 1.43e-28

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: 115.97  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFG--DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN--LPPYQRDVNT 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHmSVLENVAYGLMVK-GVAKRERLARAQEALESV-----ALGFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQaDRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAP 489

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNEL 554
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
5-235 1.74e-28

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 111.40  E-value: 1.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQeaaNLPPYQRD------- 77
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPAMSRSrlytvrk 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 -VNTVFQDYALFPHMSVLENVAYGLmvkgvakRERLARAQE--------ALESVALGFVAERKPAHLSGGQRQRVALARA 148
Cdd:PRK11831   85 rMSMLFQSGALFTDMNVFDNVAYPL-------REHTQLPAPllhstvmmKLEAVGLRGAAKLMPSELSGGMARRAALARA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEP--------LGALdLKLreqmqgeLKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPR 220
Cdd:PRK11831  158 IALEPDLIMFDEPfvgqdpitMGVL-VKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229

                         250
                  ....*....|....*
gi 1039033371 221 ELYMRPKtPFVAEFV 235
Cdd:PRK11831  230 ALQANPD-PRVRQFL 243
cbiO PRK13643
energy-coupling factor transporter ATPase;
18-223 2.17e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 111.36  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI------HGQEAANLPPYQRDVNTVFQ--DYALFP 89
Cdd:PRK13643   20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKPVRKKVGVVFQfpESQLFE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HmSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK13643  100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 169 LREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13643  179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 15-226 2.32e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 111.05  E-value: 2.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQ--DYALFPh 90
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitKENIREVRKFVGLVFQnpDDQIFS- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLR 170
Cdd:PRK13652   94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 171 EQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:PRK13652  174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-212 4.12e-28

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 111.85  E-value: 4.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   2 TIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG-QEAANLPPYQRDVNT 80
Cdd:PRK13536   39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLEN-VAYGLMVkGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK13536  119 VPQFDNLDLEFTVRENlLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:PRK13536  198 EPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 19-227 5.13e-28

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: 109.00  E-value: 5.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKT-TCLRLI----AGFEQlTSGSIRIHGQEAANLPPYQRDVNTVFQD--YALFPHM 91
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSlTCLAILgllpPGLTQ-TSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAE---RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:TIGR02770  80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 169 LREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPK 227
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPK 218
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 9-194 6.23e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 113.62  E-value: 6.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIH-GQEAANLPpyqrdvntvfQDYAL 87
Cdd:COG0488     3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEPPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 FPHMSVLENV----------------AYGLMVKGVAKRERLARAQEALESV--------------ALGFVAE---RKPAH 134
Cdd:COG0488    73 DDDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsGLGFPEEdldRPVSE 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 135 LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQrqlgITFIFVTHD 194
Cdd:COG0488   153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 10-213 6.64e-28

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: 108.96  E-value: 6.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeaanLPPYQRDVNTVFQDYALFP 89
Cdd:cd03267    27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKFLRRIGVVFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 H-------MSVLENVA-----YGLmvKGVAKRERLARAQEALESVALGFVAERKpahLSGGQRQRVALARALVNRPRVLL 157
Cdd:cd03267   102 QktqlwwdLPVIDSFYllaaiYDL--PPARFKKRLDELSELLDLEELLDTPVRQ---LSLGQRMRAEIAAALLHEPEILF 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03267   177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 5-213 7.30e-28

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: 108.33  E-value: 7.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVS---RTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEaanLPPYQ-----R 76
Cdd:cd03248    12 VKFQNVTfayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEhkylhS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DVNTVFQDYALFPHmSVLENVAYGL------MVKGVAKRerlARAQEALESVALGFVAE--RKPAHLSGGQRQRVALARA 148
Cdd:cd03248    89 KVSLVGQEPVLFAR-SLQDNIAYGLqscsfeCVKEAAQK---AHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKK-LQRQlgiTFIFVTHDQSeALSMSDRVAVFNNGRI 213
Cdd:cd03248   165 LIRNPQVLILDEATSALDAESEQQVQQALYDwPERR---TVLVIAHRLS-TVERADQILVLDGGRI 226
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-251 7.35e-28

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 113.47  E-value: 7.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEaanlppyQRDVNT 80
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-------MRFAST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 ----------VFQDYALFPHMSVLENVAYGLMVK--GVAKRERL-ARAQEALESVALGFVAERKPAHLSGGQRQRVALAR 147
Cdd:PRK11288   74 taalaagvaiIYQELHLVPEMTVAENLYLGQLPHkgGIVNRRLLnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 148 ALVNRPRVLLLDEPLGALDLKLREQmqgeLKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRieqvdtprelym 224
Cdd:PRK11288  154 ALARNARVIAFDEPTSSLSAREIEQ----LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGR------------ 217

                         250       260
                  ....*....|....*....|....*..
gi 1039033371 225 rpktpFVAEFVGTSNVVRSELAQRLLG 251
Cdd:PRK11288  218 -----YVATFDDMAQVDRDQLVQAMVG 239
cbiO PRK13646
energy-coupling factor transporter ATPase;
3-223 1.01e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 109.48  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFG-----DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN------L 71
Cdd:PRK13646    1 MTIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  72 PPYQRDVNTVFQdyalFPHMSVLEN-----VAYGLMVKGVAKRERLARAQEALesVALGF---VAERKPAHLSGGQRQRV 143
Cdd:PRK13646   81 RPVRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLL--MDLGFsrdVMSQSPFQMSGGQMRKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 144 ALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13646  155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 3-194 1.32e-27

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 112.77  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVN 79
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHmSVLENVAYG------LMVKGVAKRERLARAQEALESvALGFVAERKPAHLSGGQRQRVALARALVNRP 153
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLArpdasdAEIREALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039033371 154 RVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHD 194
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 19-223 1.53e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 109.17  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ----EAANLPPYQRDVNTVFQ--DYALFPhMS 92
Cdd:PRK13636   21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidySRKGLMKLRESVGMVFQdpDNQLFS-AS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVKGVAKRERLARAQEALESVALGFVaERKPAH-LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:PRK13636  100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 172 QMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13636  179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 18-213 2.19e-27

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: 105.98  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVF------QDYALFPHM 91
Cdd:cd03215    14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYglmvkgvakrerlaraqealesvalgfvaerkPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:cd03215    94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033371 172 QMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03215   142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-227 4.42e-27

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 107.02  E-value: 4.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSrtFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQrdvnt 80
Cdd:PRK11231    1 MTLRTENLTVG--YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFP--HM-----SVLENVAYG----LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:PRK11231   74 LARRLALLPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLklreQMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELyMRP 226
Cdd:PRK11231  154 AQDTPVVLLDEPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-MTP 228


                  .
gi 1039033371 227 K 227
Cdd:PRK11231  229 G 229
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-212 5.32e-27

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: 105.98  E-value: 5.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTF-----GDVR--AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA----A 69
Cdd:COG4778     1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  70 NLPPYQ------RDVNTVFQdyalF----PHMSVLENVAYGLMVKGVAKRERLARAQEALEsvALGfVAER----KPAHL 135
Cdd:COG4778    81 QASPREilalrrRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLA--RLN-LPERlwdlPPATF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 136 SGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:COG4778   154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 23-221 5.55e-27

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: 111.38  E-value: 5.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQDYALFPHmSVLENVAyg 100
Cdd:COG4618   351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENIA-- 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMvkGVAKRE------RLARAQEALESVALGF---VAERkPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDlklre 171
Cdd:COG4618   428 RF--GDADPEkvvaaaKLAGVHEMILRLPDGYdtrIGEG-GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD----- 499

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 172 qMQGE------LKKLqRQLGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:COG4618   500 -DEGEaalaaaIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-235 1.03e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 106.27  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLtSGSIRIHG----------QEAANLPP 73
Cdd:PRK14258    7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqniyERRVNLNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  74 YQRDVNTVFQDYALFPhMSVLENVAYGLMVKG-VAKRERLARAQEALESVALGFVAERK----PAHLSGGQRQRVALARA 148
Cdd:PRK14258   86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVF--NNGRIEQV---DTPRELY 223
Cdd:PRK14258  165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKKIF 244

                         250
                  ....*....|..
gi 1039033371 224 MRPKTPFVAEFV 235
Cdd:PRK14258  245 NSPHDSRTREYV 256
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 7-213 1.26e-26

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: 104.17  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   7 FIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG--FEQLTSGSIRIHGQeaaNLPP--YQRDVNTVF 82
Cdd:cd03213    12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR---PLDKrsFRKIIGYVP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYGLMVKGvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:cd03213    89 QDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 163 GALDLKLREQMQGELKKLqRQLGITFIFVTHD-QSEALSMSDRVAVFNNGRI 213
Cdd:cd03213   140 SGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 9-223 1.37e-26

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 105.78  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA-----ANLPPYQR------D 77
Cdd:PRK11701   11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqlrdlYALSEAERrrllrtE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYA--LFPHMSVLENVAYGLMVKGVAKRERL-ARAQEALESVALGfvAER---KPAHLSGGQRQRVALARALVN 151
Cdd:PRK11701   91 WGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIrATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARNLVT 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI------EQV-DTPRELY 223
Cdd:PRK11701  169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesgltDQVlDDPQHPY 247
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 5-226 1.47e-26

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 110.58  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF---GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ--EAANLPPYQRDVN 79
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplVQYDHHYLHRQVA 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 TVFQDYALFPHmSVLENVAYGLmvKGVAKRERLARAQEALesvALGFVAE----------RKPAHLSGGQRQRVALARAL 149
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAAN---AHDFIMEfpngydtevgEKGSQLSGGQKQRIAIARAL 632

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLrEQMQGELKKLQrqlGITFIFVTHDQSEAlSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAEC-EQLLQESRSRA---SRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 9-235 1.83e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 105.63  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlTSGSIRIHGQE--AANLPPYQ--RD 77
Cdd:PRK14243   15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNlyAPDVDPVEvrRR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHmSVLENVAYGLMVKGVaKRERLARAQEALESVALGFVAERK----PAHLSGGQRQRVALARALVNRP 153
Cdd:PRK14243   93 IGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKlkqsGLSLSGGQQQRLCIARAIAVQP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 154 RVLLLDEPLGALD----LKLREQMqgelKKLQRQLgiTFIFVTHDQSEALSMSDRVAVFN---------NGRIEQVDTPR 220
Cdd:PRK14243  171 EVILMDEPCSALDpistLRIEELM----HELKEQY--TIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTE 244

                         250
                  ....*....|....*
gi 1039033371 221 ELYMRPKTPFVAEFV 235
Cdd:PRK14243  245 KIFNSPQQQATRDYV 259
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 10-233 2.58e-26

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 106.32  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG-----QEAANLppyqRDVNTVF-Q 83
Cdd:COG4586    28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEFA----RRIGVVFgQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENVA-----YGlmVKGVAKRERLARAQEALEsvalgfVAE--RKPA-HLSGGQRQRVALARALVNRPRV 155
Cdd:COG4586   104 RSQLWWDLPAIDSFRllkaiYR--IPDAEYKKRLDELVELLD------LGEllDTPVrQLSLGQRMRCELAAALLHRPKI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 156 LLLDEP-LGaLDLKLREQMQGELKKLQRQLGITFIFVTHDQS--EALsmSDRVAVFNNGRI----------EQVDTPREL 222
Cdd:COG4586   176 LFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIiydgsleelkERFGPYKTI 252

                         250
                  ....*....|.
gi 1039033371 223 YMRPKTPFVAE 233
Cdd:COG4586   253 VLELAEPVPPL 263
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 20-222 2.75e-26

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 109.83  E-value: 2.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFPHmSVLENV 97
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPawLRRQMGVVLQENVLFSR-SIRDNI 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AY---GLMVKGVAKRERLARAQEALESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:TIGR01846 552 ALcnpGAPFEHVIHAAKLAGAHDFISELPQGYNTEvgEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEAL 631

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039033371 173 MQGELKKLQRqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR01846 632 IMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEEL 678
cbiO PRK13645
energy-coupling factor transporter ATPase;
5-223 2.78e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 105.86  E-value: 2.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF-----EQLTSGSIRIHG--QEAANLPPYQRD 77
Cdd:PRK13645   12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPAnlKKIKEVKRLRKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQ--DYALFPHmSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:PRK13645   92 IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGN 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PRK13645  171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 15-197 5.77e-26

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 103.26  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFPHmS 92
Cdd:PRK10247   18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQTPTLFGD-T 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVKGvaKRERLARAQEALESVALGFVAERKP-AHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:PRK10247   97 VYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174

                         170       180
                  ....*....|....*....|....*.
gi 1039033371 172 QMQGELKKLQRQLGITFIFVTHDQSE 197
Cdd:PRK10247  175 NVNEIIHRYVREQNIAVLWVTHDKDE 200
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 3-222 1.03e-25

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: 107.90  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGDvRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNT 80
Cdd:TIGR01193 474 IVINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINY 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHmSVLENVAYG----LMVKGVAKRERLARAQEALESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPR 154
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGakenVSQDEIWAACEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSK 631

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQlgiTFIFVTHDQSEAlSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-205 1.40e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 101.16  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNtvfqdyALFPhMSV 93
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGLMVK----GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039033371 170 REQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRV 205
Cdd:NF040873  155 RERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-218 3.21e-25

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 101.49  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ---RD 77
Cdd:PRK11614    2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHMSVLENVAY-GLMVKGVAKRERLARAQEALESvalgfVAERK---PAHLSGGQRQRVALARALVNRP 153
Cdd:PRK11614   82 VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPR-----LHERRiqrAGTMSGGEQQMLAIGRALMSQP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 154 RVLLLDEPLGALDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDT 218
Cdd:PRK11614  157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 23-213 3.71e-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: 3.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQDYALFPHmSVLENVAY- 99
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENIARf 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 100 --GLMVKGVAKRERLARAQEALESVALGFVAERKP--AHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQG 175
Cdd:TIGR01842 416 geNADPEKIIEAAKLAGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN 495

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039033371 176 ELKKLQRQlGITFIFVTHDQSeALSMSDRVAVFNNGRI 213
Cdd:TIGR01842 496 AIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRI 531
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
4-213 5.22e-25

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 105.81  E-value: 5.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAA--NLPPYQRDVNT 80
Cdd:PRK13657  334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFpHMSVLENVAYGlmvKGVAKRERLARAQEALEsvALGFVaERKPA-----------HLSGGQRQRVALARAL 149
Cdd:PRK13657  414 VFQDAGLF-NRSIEDNIRVG---RPDATDEEMRAAAERAQ--AHDFI-ERKPDgydtvvgergrQLSGGERQRLAIARAL 486

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLqRQLGITFIfVTHDQSeALSMSDRVAVFNNGRI 213
Cdd:PRK13657  487 LKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAHRLS-TVRNADRILVFDNGRV 547
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 23-166 7.07e-25

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 99.95  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqEAANLPPYQRDVNTVFQDYALFPHMSVLENVAYGLM 102
Cdd:PRK13539   21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-GDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAA 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 103 VKGvakrERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV-NRPrVLLLDEPLGALD 166
Cdd:PRK13539  100 FLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALD 159
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 10-230 7.47e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 102.51  E-value: 7.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDV----RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGF----EQLTSGSIRIHGQEAANLPPYQR----- 76
Cdd:PRK11022    9 LSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvg 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 -DVNTVFQD--YALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVALGFVAER---KPAHLSGGQRQRVALARAL 149
Cdd:PRK11022   89 aEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:PRK11022  169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHP 248


                  .
gi 1039033371 230 F 230
Cdd:PRK11022  249 Y 249
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 16-213 8.29e-25

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: 100.04  E-value: 8.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LTSGSIRIHGQEaanLPPY--QRDVNTVFQDYALFPH 90
Cdd:cd03234    19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP---RKPDqfQKCVAYVRQDDILLPG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYGLMVKG---VAKRERLAR-AQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD 166
Cdd:cd03234    96 LTVRETLTYTAILRLprkSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039033371 167 LKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:cd03234   176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 11-226 8.52e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 102.24  E-value: 8.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  11 SRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI--------HGQEAANLPPYQRD----- 77
Cdd:PRK13631   33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNPYSKKiknfk 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 -----VNTVFQ--DYALFPHmSVLENVAYGLMVKGVAKRERLARAQEALESVALGF-VAERKPAHLSGGQRQRVALARAL 149
Cdd:PRK13631  113 elrrrVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGIL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 150 VNRPRVLLLDEPLGALDLKlREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:PRK13631  192 AIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-211 1.10e-24

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 104.48  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP---YQRD 77
Cdd:PRK09700    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFPHMSVLENVAYG-LMVKGVAK------RERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:PRK09700   82 IGIIYQELSVIDELTVLENLYIGrHLTKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNG 211
Cdd:PRK09700  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 10-212 1.44e-24

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 103.86  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG------FEqltsGSIRIHGQE--AANLPPYQRD-VNT 80
Cdd:PRK13549   11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYE----GEIIFEGEElqASNIRDTERAgIAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAYG--LMVKGVAKRERL-ARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLL 157
Cdd:PRK13549   87 IHQELALVKELSVLENIFLGneITPGGIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 158 LDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:PRK13549  167 LDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
3-222 2.07e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 104.44  E-value: 2.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRdVNT 80
Cdd:NF033858  265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRRR-VGY 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVLENVAygLMVK--GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:NF033858  344 MSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQRQLGITfIFV-THDQSEALSmSDRVAVFNNGRIEQVDTPREL 222
Cdd:NF033858  422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 10-223 2.80e-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: 99.52  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ-----------RDV 78
Cdd:TIGR02323   9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQlseaerrrlmrTEW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYA--LFPHMSVLENVAYGLMVKGVAKRERL-ARAQEALESVALGFV-AERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:TIGR02323  89 GFVHQNPRdgLRMRVSAGANIGERLMAIGARHYGNIrATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIARNLVTRPR 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI------EQV-DTPRELY 223
Cdd:TIGR02323 169 LVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltDQVlDDPQHPY 244
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
21-193 3.24e-24

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 97.95  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  21 DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-AANLPPYQRDVntvfqdyaLF--------PHM 91
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPiRRQRDEYHQDL--------LYlghqpgikTEL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYGLMVKGVAKRERLAraqEALESVAL-GFvaERKPAH-LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:PRK13538   90 TALENLRFYQRLHGPGDDEALW---EALAQVGLaGF--EDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164

                         170       180
                  ....*....|....*....|....
gi 1039033371 170 REQMQGELKKLQRQLGITfIFVTH 193
Cdd:PRK13538  165 VARLEALLAQHAEQGGMV-ILTTH 187
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 9-222 3.32e-24

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: 102.96  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQL--TSGSI-----------RIHGQEAANLP--- 72
Cdd:TIGR03269   5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgYVERPSKVGEPcpv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  73 -----------------PYQRDVN----TVFQ-DYALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAER 130
Cdd:TIGR03269  85 cggtlepeevdfwnlsdKLRRRIRkriaIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 131 KPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNN 210
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244

                         250
                  ....*....|..
gi 1039033371 211 GRIEQVDTPREL 222
Cdd:TIGR03269 245 GEIKEEGTPDEV 256
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 9-213 5.26e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 102.44  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP---YQRDVNTVFQDY 85
Cdd:PRK15439   16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGLmvkgVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:PRK15439   96 LLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039033371 166 DLKLREQMQGELKKLQrQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK15439  172 TPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 23-215 6.59e-24

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 102.23  E-value: 6.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTsGSIRIHGQEAANLPP--YQRDVNTVFQDYALFpHMSVLENVayg 100
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNV--- 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMVKGVAKRERL------ARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:PRK11174  444 LLGNPDASDEQLqqalenAWVSEFLPLLPQGLdtpIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 172 QMQGELKKLQRQLgiTFIFVTHdQSEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK11174  523 LVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
cbiO PRK13644
energy-coupling factor transporter ATPase;
9-249 1.07e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 98.52  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGD-VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN---LPPYQRDVNTVFQD 84
Cdd:PRK13644    6 NVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 -YALFPHMSVLENVAYG---LMVKGVAKRERLARAqeaLESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:PRK13644   86 pETQFVGRTVEEDLAFGpenLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 161 PLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEaLSMSDRVAVFNNGRIEQVDTPRELYMRPKTpfvaEFVGTSNV 240
Cdd:PRK13644  163 VTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL----QTLGLTPP 236


                  ....*....
gi 1039033371 241 VRSELAQRL 249
Cdd:PRK13644  237 SLIELAENL 245
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 20-193 1.11e-23

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 101.81  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEffSML--GPSGSGKTTCLRLIAGFEQLTSGSIRI-HGQEAANLP--PYqrdvntvfqdyalFPHMSVL 94
Cdd:COG4178   379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrPY-------------LPLGTLR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  95 ENVAYGLMVKGVAkrerLARAQEALESVALGFVAER--KPAH----LSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:COG4178   444 EALLYPATAEAFS----DAELREALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519

                         170       180
                  ....*....|....*....|....*.
gi 1039033371 169 LREQMqgeLKKLQRQL-GITFIFVTH 193
Cdd:COG4178   520 NEAAL---YQLLREELpGTTVISVGH 542
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 15-194 1.79e-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: 100.90  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP--PYQRDVNTVFQDYALFpHMS 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGlmvKGVAKRERLARAqeaLESVALGFVAERKP-----------AHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:TIGR02868 425 VRENLRLA---RPDATDEELWAA---LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039033371 162 LGALDLKLREQMQGELkkLQRQLGITFIFVTHD 194
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHH 529
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 9-222 1.88e-23

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 96.89  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQDY 85
Cdd:PRK10895    8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQEA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:PRK10895   88 SIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 165 LDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK10895  168 VDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 18-230 4.19e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 99.78  E-value: 4.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKT----TCLRLIAGFEQL-TSGSIRIHGQEAANLP-PYQRDVN-----TVFQD-- 84
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASeQTLRGVRgnkiaMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPhMSVLENVAYGLMVKGVAKRERLARAQ--EALESVALGFVAER---KPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK15134  103 VSLNP-LHTLEKQLYEVLSLHRGMRREAARGEilNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIAD 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PRK15134  182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
18-213 4.81e-23

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 99.32  E-value: 4.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ------------RdvntvfQDY 85
Cdd:COG1129   266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedR------KGE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYGLMVK----GV--AKRERlARAQEALESVALgfvaerKPAH-------LSGGQRQRVALARALVNR 152
Cdd:COG1129   340 GLVLDLSIRENITLASLDRlsrgGLldRRRER-ALAEEYIKRLRI------KTPSpeqpvgnLSGGNQQKVVLAKWLATD 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 153 PRVLLLDEP-----LGAldlklreqmQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG1129   413 PKVLILDEPtrgidVGA---------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 23-212 4.99e-23

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: 94.84  E-value: 4.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAanlppYqrdvntVFQdYALFPHMSVLENVAYGLm 102
Cdd:cd03250    24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA-----Y------VSQ-EPWIQNGTIRENILFGK- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 vkgVAKRERLARAQEA------LESVALG---FVAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQM 173
Cdd:cd03250    91 ---PFDEERYEKVIKAcalepdLEILPDGdltEIGEKG-INLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHI 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 174 -----QGELKKlqrqlGITFIFVTHdQSEALSMSDRVAVFNNGR 212
Cdd:cd03250   167 fenciLGLLLN-----NKTRILVTH-QLQLLPHADQIVVLDNGR 204
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-219 5.81e-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: 100.47  E-value: 5.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-AANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   98 AYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGEL 177
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039033371  178 kkLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTP 219
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 15-193 9.99e-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: 93.96  E-value: 9.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQDYALFPHMSV 93
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGLMVKGVAKRErlarAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQM 173
Cdd:TIGR01189  91 LENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166

                         170       180
                  ....*....|....*....|.
gi 1039033371 174 QGELKK-LQRQlGITfIFVTH 193
Cdd:TIGR01189 167 AGLLRAhLARG-GIV-LLTTH 185
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 10-212 1.31e-22

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 98.36  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTS--GSIRIHGQE--AANLPPYQRD-VNTVFQD 84
Cdd:TIGR02633   7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkASNIRDTERAgIVIIHQE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYG--LMVKG--VAKRERLARAQEALESVALGFVAERKP-AHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:TIGR02633  87 LTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 17-230 1.81e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 98.39  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKT-TCLRLIAGFEQ----LTSGS----------IRIHGQEAANLPPYQ-RDVNT 80
Cdd:PRK10261   29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQagglVQCDKmllrrrsrqvIELSEQSAAQMRHVRgADMAM 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQD--YALFPHMSVLENVAYGLMV-KGVAKRERLARAQEALESVAL---GFVAERKPAHLSGGQRQRVALARALVNRPR 154
Cdd:PRK10261  109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 155 VLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PRK10261  189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 9-214 3.35e-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: 3.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI-HGQEAANLPpyqrdvntvfQDYAL 87
Cdd:COG0488   320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFD----------QHQEE 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 F-PHMSVLENVAYGlmvkGVAKRERLARAQeaLEsvALGFVAER--KPAH-LSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:COG0488   390 LdPDKTVLDELRDG----APGGTEQEVRGY--LG--RFLFSGDDafKPVGvLSGGEKARLALAKLLLSPPNVLLLDEPTN 461

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 164 ALDLKLREQMQGELKKLQrqlGiTFIFVTHDQsEAL-SMSDRVAVFNNGRIE 214
Cdd:COG0488   462 HLDIETLEALEEALDDFP---G-TVLLVSHDR-YFLdRVATRILEFEDGGVR 508
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
17-213 1.15e-21

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 92.55  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI--HGQEAANLPPYQRDVNTVFQD--YALFPHMS 92
Cdd:PRK15112   26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddHPLHFGDYSYRSQRIRMIFQDpsTSLNPRQR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVK-GVAKRERLARAQEALESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLR 170
Cdd:PRK15112  106 ISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039033371 171 EQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK15112  186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-234 1.66e-21

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 91.71  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRihgqeaanlPPYQRDVNT 80
Cdd:PRK09544    1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHMSVleNVAYGLMVK-GVAKRERLAraqeALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK09544   72 VPQKLYLDTTLPL--TVNRFLRLRpGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFnNGRIEQVDTPRELYMRPKtpFVAEF 234
Cdd:PRK09544  146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 20-226 2.44e-21

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 95.01  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDVNTVFQDYALFpHMSVLENV 97
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPRevLANSVAMVDQDIFLF-EGTVRDNL 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AyglMVKGVAKRERLARA------QEALESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDlkl 169
Cdd:TIGR03796 574 T---LWDPTIPDADLVRAckdaaiHDVITSRPGGYDAElaEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD--- 647

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371 170 reqMQGELKKLQ--RQLGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:TIGR03796 648 ---PETEKIIDDnlRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWAVG 702
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 4-215 6.29e-21

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: 93.73  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSrtFG---DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP--YQRDV 78
Cdd:COG5265   357 EVRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAI 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFpHMSVLENVAYGlmvKGVAKRERLARAQEA------LESVALGF---VAER--KpahLSGGQRQRVALAR 147
Cdd:COG5265   435 GIVPQDTVLF-NDTIAYNIAYG---RPDASEEEVEAAARAaqihdfIESLPDGYdtrVGERglK---LSGGEKQRVAIAR 507

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 148 ALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHdqseALSM---SDRVAVFNNGRI-EQ 215
Cdd:COG5265   508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH----RLSTivdADEILVLEAGRIvER 573
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 5-214 4.18e-20

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: 86.21  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFG--DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVF 82
Cdd:cd03247     1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAyglmvkgvakrerlaraqealesvalgfvaerkpAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:cd03247    81 NQRPYLFDTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 163 GALD----LKLREQMQGELKklqrqlGITFIFVTHDQSeALSMSDRVAVFNNGRIE 214
Cdd:cd03247   127 VGLDpiteRQLLSLIFEVLK------DKTLIWITHHLT-GIEHMDKILFLENGKII 175
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
30-228 6.46e-20

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 87.92  E-value: 6.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  30 GEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ--EAANLPPYQRDVNTVFQDYALFPHMSVLENVAYG------- 100
Cdd:PRK10575   37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGrypwhga 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMVKGVAKRERLaraQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKL 180
Cdd:PRK10575  117 LGRFGAADREKV---EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039033371 181 QRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELyMRPKT 228
Cdd:PRK10575  194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-MRGET 240
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
16-221 7.63e-20

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 90.23  E-value: 7.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR------DVNTVFQDYALFP 89
Cdd:PRK09700  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmaYITESRRDNGFFP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMVK--------GV---AKRERLARAQEALESVALGFVaERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:PRK09700  355 NFSIAQNMAISRSLKdggykgamGLfheVDEQRTAENQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIF 433

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 159 DEPLGALDLKLReqmqGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:PRK09700  434 DEPTRGIDVGAK----AEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 5-195 8.35e-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: 84.42  E-value: 8.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHgqeaanlppyqrdvntvfqd 84
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 yalfphmsvlenvayglmvkgvakrerlaraqealESVALGFVAerkpaHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03221    61 -----------------------------------STVKIGYFE-----QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039033371 165 LDLKLREQMQGELKKLQRqlgiTFIFVTHDQ 195
Cdd:cd03221   101 LDLESIEALEEALKEYPG----TVILVSHDR 127
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 22-234 1.18e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 89.72  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  22 RVSIDIQDGEFFSMLGPSGSGKTTCLRLIAgFEQLT----SGSIRIHGqEAANLPPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:TIGR00955  43 NVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG-MPIDAKEMRAISAYVQQDDLFIPTLTVREHL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AYGLMVK---GVAKRERLARAQEALESVALgfvaeRKPAH-----------LSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:TIGR00955 121 MFQAHLRmprRVTKKEKRERVDEVLQALGL-----RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 164 ALDLKLREQMQGELKKLQrQLGITFIFVTHD-QSEALSMSDRVAVFNNGRIEQVDTPRELymrpkTPFVAEF 234
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA-----VPFFSDL 261
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 16-193 1.36e-19

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 85.24  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  16 DVRAV-DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQDYALFPHMSV 93
Cdd:cd03231    11 DGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGHAPGIKTTLSV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGLMVKGVAKRErlaraqEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL----KL 169
Cdd:cd03231    91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagvaRF 164

                         170       180
                  ....*....|....*....|....
gi 1039033371 170 REQMQGELkklqrQLGITFIFVTH 193
Cdd:cd03231   165 AEAMAGHC-----ARGGMVVLTTH 183
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-222 1.38e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 89.69  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTF--GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQeaaNLPPYQ-----RD 77
Cdd:PRK11176  342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTlaslrNQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VNTVFQDYALFpHMSVLENVAYGlmVKGVAKRERLARAQEAleSVALGFVAERKP----------AHLSGGQRQRVALAR 147
Cdd:PRK11176  419 VALVSQNVHLF-NDTIANNIAYA--RTEQYSREQIEEAARM--AYAMDFINKMDNgldtvigengVLLSGGQRQRIAIAR 493

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 148 ALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLgiTFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK11176  494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAEL 565
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 17-213 2.12e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 88.93  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR---DVNTVFQD---YALFPH 90
Cdd:COG3845   271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIPEDrlgRGLVPD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYG-LMVKGVAKRERLARAqeALESVALGFVAE---RKP------AHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:COG3845   351 MSVAENLILGrYRRPPFSRGGFLDRK--AIRAFAEELIEEfdvRTPgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQ 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 161 PLGALDLKLREQMQGELKKLqRQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:COG3845   429 PTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 20-229 2.14e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 85.91  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKT-TCLRLI----AGFEQlTSGSIRIHGQEAANLPPYQRDVNTVFQD--YALFPHMS 92
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAYGLMVKGVAKRErlARAQEALESVALG---FVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:PRK10418   98 MHTHARETCLALGKPADD--ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 170 REQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:PRK10418  176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 20-196 3.40e-19

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: 83.36  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA-ANLP--PYqrdvntvfqdyalFPHMSVLEN 96
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDlLFLPqrPY-------------LPLGTLREQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAYglmvkgvakrerlaraqeALESValgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEPLGALDlklrEQMQGE 176
Cdd:cd03223    84 LIY------------------PWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129

                         170       180
                  ....*....|....*....|
gi 1039033371 177 LKKLQRQLGITFIFVTHDQS 196
Cdd:cd03223   130 LYQLLKELGITVISVGHRPS 149
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 15-213 6.88e-19

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: 83.35  E-value: 6.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFE--QLTSGSIRIHGQEAANLPPYQRDVNTVFqdyalfphMS 92
Cdd:cd03217    11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIF--------LA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLENVAyglmVKGVakrerlaRAQEALESVALGFvaerkpahlSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:cd03217    83 FQYPPE----IPGV-------KNADFLRYVNEGF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033371 173 MQGELKKLqRQLGITFIFVTHDQSEALSM-SDRVAVFNNGRI 213
Cdd:cd03217   143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
14-228 1.01e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 84.67  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ----EAANLPPYQRDVNTVFQD--YAL 87
Cdd:PRK13638   11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldySKRGLLALRQQVATVFQDpeQQI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  88 FpHMSVLENVAYGLMVKGVAKRERLARAQEALESV-ALGFvaERKPAH-LSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:PRK13638   91 F-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVdAQHF--RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 166 DLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKT 228
Cdd:PRK13638  168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-222 1.96e-18

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 86.61  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlppyqrDVNTVFQDYALFPHMSVLENVA 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLL 2027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   99 YG-------LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:TIGR01257 2028 TGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371  172 QMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-226 2.56e-18

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 84.79  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTtclrliagfeqltSGSIRIH--GQEAANLP-------PY 74
Cdd:NF000106   13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALPAHv*GPDAGRRPwrf*twcAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  75 QRDVNTVFQDY-----ALFPHMSVLENVAYGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:NF000106   80 RRALRRTIG*Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEA------LSMSDRVAVFNNGRIEQVDTP---R 220
Cdd:NF000106  160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238


                  ....*.
gi 1039033371 221 ELYMRP 226
Cdd:NF000106  239 TLQIRP 244
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 9-195 6.37e-18

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 81.16  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFG---DV---RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIhgqeaanlppyqrdvntVF 82
Cdd:COG2401    29 IVLEAFGvelRVverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYGLMVKgvAKRERLARAqeALESVALGFvaeRKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:COG2401    92 PDNQFGREASLIDAIGRKGDFK--DAVELLNAV--GLSDAVLWL---RRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039033371 163 GALDLKLREQMQGELKKLQRQLGITFIFVTHDQ 195
Cdd:COG2401   165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
15-230 8.19e-18

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 83.03  E-value: 8.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFE----QLTSGSIRIHGQEAANLPPYQR------DVNTVFQD 84
Cdd:COG4170    18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 --YALFPHMSV---LENVAYGLMVKGV---AKRERLARAQEALESVAL---GFVAERKPAHLSGGQRQRVALARALVNRP 153
Cdd:COG4170    98 psSCLDPSAKIgdqLIEAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQP 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 154 RVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:COG4170   178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPY 254
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 23-219 9.12e-18

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: 80.62  E-value: 9.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTC----LRLIagfeQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQDYALFPHmSVLEN 96
Cdd:cd03244    23 ISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 vaygLMVKGVAKRERLaraQEALESVALGFVAERKP-----------AHLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:cd03244    98 ----LDPFGEYSDEEL---WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 166 DLKLREQMQgelKKLQRQL-GITFIFVTHdQSEALSMSDRVAVFNNGRIEQVDTP 219
Cdd:cd03244   171 DPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
15-230 3.36e-17

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 81.00  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQ----LTSGSIRIHGQEAANLPPYQR------DVNTVFQD 84
Cdd:PRK15093   18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 --YALFPHMSV---LENVAYGLMVKG-----VAKRERlaRAQEALESValGFVAERK-----PAHLSGGQRQRVALARAL 149
Cdd:PRK15093   98 pqSCLDPSERVgrqLMQNIPGWTYKGrwwqrFGWRKR--RAIELLHRV--GIKDHKDamrsfPYELTEGECQKVMIAIAL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTP 229
Cdd:PRK15093  174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHP 253


                  .
gi 1039033371 230 F 230
Cdd:PRK15093  254 Y 254
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
14-222 4.28e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 80.03  E-value: 4.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQ--RDVNTVFQDYALFPHM 91
Cdd:PRK10253   17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 SVLENVAYG------LMVKGvaKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:PRK10253   97 TVQELVARGryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 166 DLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PRK10253  175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 14-205 5.57e-17

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 81.92  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ-EAANL---PPyqRDVN-TVFqDYalf 88
Cdd:PRK11147   13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLqqdPP--RNVEgTVY-DF--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 phmsVLENVA--------YGLMVKGVAKR------ERLARAQEALES--------------VALGFVAERKPAHLSGGQR 140
Cdd:PRK11147   87 ----VAEGIEeqaeylkrYHDISHLVETDpseknlNELAKLQEQLDHhnlwqlenrinevlAQLGLDPDAALSSLSGGWL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 141 QRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlgiTFIFVTHDQSEALSMSDRV 205
Cdd:PRK11147  163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 4-213 6.65e-17

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 81.41  E-value: 6.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGD--VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlppyqrdvntv 81
Cdd:PRK11160  338 SLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD----------- 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPHMSVL------------ENVaygLMVKGVAKRERLAraqEALESVALGFVAERKPA----------HLSGGQ 139
Cdd:PRK11160  407 YSEAALRQAISVVsqrvhlfsatlrDNL---LLAAPNASDEALI---EVLQQVGLEKLLEDDKGlnawlgeggrQLSGGE 480

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 140 RQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHDQSEALSMsDRVAVFNNGRI 213
Cdd:PRK11160  481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQI 551
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-161 1.26e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.94  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlppyQRDVNTVFQ 83
Cdd:NF033858    1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYA---------LFPHMSVLENVA-----YGLmvkgvAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL 149
Cdd:NF033858   77 RIAympqglgknLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                         170
                  ....*....|..
gi 1039033371 150 VNRPRVLLLDEP 161
Cdd:NF033858  152 IHDPDLLILDEP 163
PLN03211 PLN03211
ABC transporter G-25; Provisional
 9-212 2.08e-16

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 80.31  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTS--GSIRIHGQEAANlpPYQRDVNTVFQDYA 86
Cdd:PLN03211   73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDI 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  87 LFPHMSVLENVAYGLMV---KGVAKRERLARAQEALESVALG-----FVAERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:PLN03211  151 LYPHLTVRETLVFCSLLrlpKSLTKQEKILVAESVISELGLTkcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 159 DEPLGALDLKLREQMQGELKKLQrQLGITFIFVTHD-QSEALSMSDRVAVFNNGR 212
Cdd:PLN03211  231 DEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 7-213 3.08e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 79.63  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   7 FIDVSRTFGDVR-AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQ 83
Cdd:PRK10522  325 LRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvtAEQPEDYRKLFSAVFT 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMsvlenvaygLMVKGVAKRERLARA-------QEALEsVALGFVAERKpahLSGGQRQRVALARALVNRPRVL 156
Cdd:PRK10522  405 DFHLFDQL---------LGPEGKPANPALVEKwlerlkmAHKLE-LEDGRISNLK---LSKGQKKRLALLLALAEERDIL 471

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSeALSMSDRVAVFNNGRI 213
Cdd:PRK10522  472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQL 527
hmuV PRK13547
heme ABC transporter ATP-binding protein;
5-226 4.32e-16

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 77.17  E-value: 4.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGdvRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG--FEQLTSGSIRIHGQEAANLPPYQR-DVNTV 81
Cdd:PRK13547    4 ADHLHVARRHR--AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 FQDYALFPH-------MSVLENVAYG----LMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:PRK13547   82 ARLRAVLPQaaqpafaFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 151 N---------RPRVLLLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRE 221
Cdd:PRK13547  162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241


                  ....*
gi 1039033371 222 LyMRP 226
Cdd:PRK13547  242 V-LTP 245
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 6-213 6.04e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 78.51  E-value: 6.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   6 QFIDVSRTFGDVR---------AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR 76
Cdd:PRK10762  245 QYPRLDKAPGEVRlkvdnlsgpGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDG 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  77 DVNTVF---QDY---ALFPHMSVLENV---AYGLMVKGvAKRERLARAQEALESVALGF-----VAERKPAHLSGGQRQR 142
Cdd:PRK10762  325 LANGIVyisEDRkrdGLVLGMSVKENMsltALRYFSRA-GGSLKHADEQQAVSDFIRLFniktpSMEQAIGLLSGGNQQK 403

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 143 VALARALVNRPRVLLLDEPLGALDLKLRE---QMQGELKklqrQLGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK10762  404 VAIARGLMTRPKVLILDEPTRGVDVGAKKeiyQLINQFK----AEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
GguA NF040905
sugar ABC transporter ATP-binding protein;
9-217 6.49e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 78.29  E-value: 6.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG------FEqltsGSIRIHGQEAANlppyqRDVN--- 79
Cdd:NF040905    6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEVCRF-----KDIRdse 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  80 -----TVFQDYALFPHMSVLENVAYGlmvKGVAKR------ERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARA 148
Cdd:NF040905   77 algivIIHQELALIPYLSIAENIFLG---NERAKRgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR-IEQVD 217
Cdd:NF040905  154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRtIETLD 222
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 8-203 1.91e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 73.83  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE-AANLPPYQRDVNTVFQDYA 86
Cdd:PRK13540    5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSiKKDLCTYQKQLCFVGHRSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  87 LFPHMSVLENVAYGLMVKGVAkrerlARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD 166
Cdd:PRK13540   85 INPYLTLRENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 167 LKLREQMQGELKKLQRQLGItfIFVTHDQSEALSMSD 203
Cdd:PRK13540  160 ELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-166 4.98e-15

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: 75.74  E-value: 4.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIhgQEAANLpPY---QRDvntv 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GETVKL-AYvdqSRD---- 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  82 fqdyALFPHMSVLENVAYGLMVKGVAKRERLARAQEAlesvALGFVA---ERKPAHLSGGQRQRVALARALVNRPRVLLL 158
Cdd:TIGR03719 396 ----ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVG----RFNFKGsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467


                  ....*...
gi 1039033371 159 DEPLGALD 166
Cdd:TIGR03719 468 DEPTNDLD 475
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
19-226 7.11e-15

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 75.52  E-value: 7.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQeaaNLPPYQRD-----VNTVFQDYALFPHmSV 93
Cdd:PRK10789  330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDswrsrLAVVSQTPFLFSD-TV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVAYGlmvKGVAKRE------RLARAQEALESVALGF---VAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:PRK10789  406 ANNIALG---RPDATQQeiehvaRLASVHDDILRLPQGYdteVGERG-VMLSGGQKQRISIARALLLNAEILILDDALSA 481

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 165 LDLKLREQMQGELKKLQRQLgiTFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRELYMRP 226
Cdd:PRK10789  482 VDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 17-213 8.93e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 74.97  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG-FEQLTSGSIRIHGQEAANLPPYQ---RDVNTVFQD---YALFP 89
Cdd:PRK13549  275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMvKGVAKRERLARAQE---ALESVALGFVAERKP----AHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:PRK13549  355 VMGVGKNITLAAL-DRFTGGSRIDDAAElktILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPT 433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 163 GALDLKLREqmqgELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK13549  434 RGIDVGAKY----EIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 24-210 1.12e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.45  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   24 SIDIQDGEFFSMLGPSGSGKTTCLrliagFEQltSGSIRIHGQEAA--NLPPYQRDVNTVFQDYALFpHMSVLENVAYGl 101
Cdd:PTZ00265  1249 NVGMKNVNEFSLTKEGGSGEDSTV-----FKN--SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG- 1319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  102 mvKGVAKRERLARA------QEALESVALGFVAERKP--AHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQM 173
Cdd:PTZ00265  1320 --KEDATREDVKRAckfaaiDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039033371  174 QGELKKLQRQLGITFIFVTHdQSEALSMSDRVAVFNN 210
Cdd:PTZ00265  1398 EKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 17-214 1.16e-14

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 74.48  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG-FEQLTSGSIRIHGQEAANLPPYQ---RDVNTVFQD---YALFP 89
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVP 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  90 HMSVLENVAYGLMvKGVAKRERLARAQEA---LESVALGFVAERKP----AHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:TIGR02633 353 ILGVGKNITLSVL-KSFCFKMRIDAAAELqiiGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 163 GALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIE 214
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 23-222 1.64e-14

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 74.06  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ--EAANLPPYQRDVNTVFQDYALFPHmsvlenvayg 100
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpvTADNREAYRQLFSAVFSDFHLFDR---------- 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMvkGVAKRERLARAQEALESVALgfvaERKPA---------HLSGGQRQRVALARALV-NRPrVLLLDE------PLga 164
Cdd:COG4615   421 LL--GLDGEADPARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLeDRP-ILVFDEwaadqdPE-- 491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 165 ldlkLR----EQMQGELKklqrQLGITFIFVTHDQ---SEAlsmsDRVAVFNNGRIEQVDTPREL 222
Cdd:COG4615   492 ----FRrvfyTELLPELK----ARGKTVIAISHDDryfDLA----DRVLKMDYGKLVELTGPAAL 544
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-194 1.67e-14

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 72.61  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEA-----ANLPPYQRDVNTVfqDYAlFPhmSV 93
Cdd:PRK15056   22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqalqKNLVAYVPQSEEV--DWS-FP--VL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  94 LENVA----YGLM-VKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:PRK15056   97 VEDVVmmgrYGHMgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176

                         170       180
                  ....*....|....*....|....*.
gi 1039033371 169 LREQMQGELKKLqRQLGITFIFVTHD 194
Cdd:PRK15056  177 TEARIISLLREL-RDEGKTMLVSTHN 201
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-208 3.15e-14

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 71.29  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  26 DIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPY-QRDVNTVFQDYAlfphMSVLENVAYGLMVK 104
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDLL----SSITKDFYTHPYFK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 105 gvakrerlaraQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQL 184
Cdd:cd03237    97 -----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165

                         170       180
                  ....*....|....*....|....
gi 1039033371 185 GITFIFVTHDQSEALSMSDRVAVF 208
Cdd:cd03237   166 EKTAFVVEHDIIMIDYLADRLIVF 189
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 23-213 4.28e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 72.78  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQR-DVNTVF-----QDYALFPHMSVLEN 96
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VA------YGLMVKGVAKRERLARAQEALesvALGFVAERKPAH-LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:PRK15439  362 VCalthnrRGFWIKPARENAVLERYRRAL---NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 170 REQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK15439  439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 35-194 4.57e-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: 73.05  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  35 MLGPSGSGKTTCLRLIAGFEQLTSGsirihgqEAANLPPYQrdVNTVFQDYALFPHMSVLENVAYGLM-VKGVAKR---- 109
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIK--VGYLPQEPQLDPTKTVRENVEEGVAeIKDALDRfnei 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 110 ---------------ERLARAQEALES---------VALGFVAERKP------AHLSGGQRQRVALARALVNRPRVLLLD 159
Cdd:TIGR03719 107 sakyaepdadfdklaAEQAELQEIIDAadawdldsqLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLD 186

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039033371 160 EPLGALDLKLREQMQGELKKLQrqlGiTFIFVTHD 194
Cdd:TIGR03719 187 EPTNHLDAESVAWLERHLQEYP---G-TVVAVTHD 217
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
27-167 3.03e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 67.95  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANlPPYQRDVNTVFQDYALFPHMSVLENVAYglmVKGV 106
Cdd:PRK13543   34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLKADLSTLENLHF---LCGL 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 107 AKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDL 167
Cdd:PRK13543  110 HGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 5-166 3.09e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 70.53  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIhGQeaanlppyqrdvnTVFQD 84
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-------------TVKLA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 Y------ALFPHMSVLENVAYGLMVKGVAKRERLARAQEAlesvALGFVA---ERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK11819  391 YvdqsrdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVG----RFNFKGgdqQKKVGVLSGGERNRLHLAKTLKQGGNV 466

                         170
                  ....*....|.
gi 1039033371 156 LLLDEPLGALD 166
Cdd:PRK11819  467 LLLDEPTNDLD 477
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-205 3.85e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 69.92  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRihGQEAANLPPYQRDVNTVF- 82
Cdd:PRK15064  319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--WSENANIGYYAQDHAYDFe 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  83 QDYALFPHMSVLENVAYG-LMVKGVAKReRLARAQEALESVALgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK15064  397 NDLTLFDWMSQWRQEGDDeQAVRGTLGR-LLFSQDDIKKSVKV----------LSGGEKGRMLFGKLMMQKPNVLVMDEP 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 162 LGALDLKLREQMQGELKKLQrqlGiTFIFVTHDQSEALSMSDRV 205
Cdd:PRK15064  466 TNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRI 505
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 9-194 5.05e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.98  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   9 DVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ-EAAnlppYqrdvntvFQDY-- 85
Cdd:PRK11147  324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA----Y-------FDQHra 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  86 ALFPHMSVLENVAYG---LMVKGVaKRERLARAQEALesvalgFVAER--KPAH-LSGGQRQRVALARALVNRPRVLLLD 159
Cdd:PRK11147  393 ELDPEKTVMDNLAEGkqeVMVNGR-PRHVLGYLQDFL------FHPKRamTPVKaLSGGERNRLLLARLFLKPSNLLILD 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033371 160 EPLGALD---LKLREQM----QGelkklqrqlgiTFIFVTHD 194
Cdd:PRK11147  466 EPTNDLDvetLELLEELldsyQG-----------TVLLVSHD 496
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
4-215 6.75e-13

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 69.36  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   4 AVQFIDVSRTFGDVRAV-DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP--PYQRDVNT 80
Cdd:PRK10790  340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAM 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  81 VFQDYALFPHmSVLENVAYGlmvkgvakRE-RLARAQEALESVALGFVAERKPA-----------HLSGGQRQRVALARA 148
Cdd:PRK10790  420 VQQDPVVLAD-TFLANVTLG--------RDiSEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARV 490

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlgITFIFVTHDQSEALSmSDRVAVFNNGR-IEQ 215
Cdd:PRK10790  491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQaVEQ 555
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 1-211 2.52e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 67.34  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   1 MTIAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyqRD--- 77
Cdd:PRK10762    1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP--KSsqe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 --VNTVFQDYALFPHMSVLENVAYGLMVK----GVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVN 151
Cdd:PRK10762   79 agIGIIHQELNLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 152 RPRVLLLDEPLGALDLKLREQMQGELKKLQRQ-LGITFIfvTHDQSEALSMSDRVAVFNNG 211
Cdd:PRK10762  159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYI--SHRLKEIFEICDDVTVFRDG 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 8-212 3.61e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 67.06  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   8 IDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE---AANLPPYQRDVNTVFQD 84
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 YALFPHMSVLENVAYGLM-VKGV-AKRERLARAQEAL-ESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK10982   82 LNLVLQRSVMDNMWLGRYpTKGMfVDQDKMYRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGR 212
Cdd:PRK10982  162 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-324 4.14e-12

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: 67.28  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQeAANLPPYQRDVNTVFQDYALFPHMsvLENVAYGLM 102
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQV 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  103 VKGVAkrerLARAQEALESVALGFVAErKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQM-------QG 175
Cdd:TIGR00957  734 LEACA----LLPDLEILPSGDRTEIGE-KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEG 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  176 ELKklqrqlGITFIFVTHDQSeALSMSDRVAVFNNGRIEQVDTPRELYMRPKTpfVAEFVGTSNVVRSELAqrlLGESRT 255
Cdd:TIGR00957  809 VLK------NKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQRDGA--FAEFLRTYAPDEQQGH---LEDSWT 876

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371  256 FSIRPE--HIRLLEQGGAAQDEIQVQGTLQ---EIHYQGAATRYeiaLNGGEKLLVSQANPQ-W-IAEGLQRQIGQ 324
Cdd:TIGR00957  877 ALVSGEgkEAKLIENGMLVTDVVGKQLQRQlsaSSSDSGDQSRH---HGSSAELQKAEAKEEtWkLMEADKAQTGQ 949
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
11-213 5.91e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 66.47  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  11 SRTFGDVR-AVDR---------VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQ--------EAAN-- 70
Cdd:PRK11288  250 PRPLGEVRlRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprDAIRag 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  71 --LPPYQRDvntvfQDyALFPHMSVLENVA---------YGLMVKGvaKRERlARAQEALESVALGF-VAERKPAHLSGG 138
Cdd:PRK11288  330 imLCPEDRK-----AE-GIIPVHSVADNINisarrhhlrAGCLINN--RWEA-ENADRFIRSLNIKTpSREQLIMNLSGG 400

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 139 QRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK11288  401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 18-219 9.48e-12

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: 63.59  E-value: 9.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  18 RAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP--PYQRDVNTVFQDYALFphMSVLE 95
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTIIPQDPTLF--SGTIR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  96 NvayGLMVKGVAKRERLARAQEALESvalgfvaerkPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQG 175
Cdd:cd03369   100 S---NLDPFDEYSDEEIYGALRVSEG----------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 176 ELKKLQRqlGITFIFVTHDQSEALSMsDRVAVFNNGRIEQVDTP 219
Cdd:cd03369   167 TIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 35-194 1.19e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.53  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  35 MLGPSGSGKTTCLRLIAGFEQLTSGSIRIhgQEAAN---LPpyqrdvntvfQDYALFPHMSVLENVAYGLM-VKGVAKR- 109
Cdd:PRK11819   38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKvgyLP----------QEPQLDPEKTVRENVEEGVAeVKAALDRf 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 110 ------------------ERLARAQEALESV--------------ALgfvaeRKP------AHLSGGQRQRVALARALVN 151
Cdd:PRK11819  106 neiyaayaepdadfdalaAEQGELQEIIDAAdawdldsqleiamdAL-----RCPpwdakvTKLSGGERRRVALCRLLLE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039033371 152 RPRVLLLDEPLGALD------LklrEQMqgelkkLQRQLGiTFIFVTHD 194
Cdd:PRK11819  181 KPDMLLLDEPTNHLDaesvawL---EQF------LHDYPG-TVVAVTHD 219
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 23-222 1.70e-11

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 63.32  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQlTSGSIRIHGQEAANLPP--------Y--QRDVNT----VFQDYALF 88
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaelarhraYlsQQQSPPfampVFQYLALH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSVLENVAYGLMvkgvakrERLAraqEALEsvaLGFVAERKPAHLSGGQRQRVALARAL------VN-RPRVLLLDEP 161
Cdd:COG4138    94 QPAGASSEAVEQLL-------AQLA---EALG---LEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 162 LGALDLklreQMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRI------EQVDTPREL 222
Cdd:COG4138   161 MNSLDV----AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLvasgetAEVMTPENL 226
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 27-213 2.69e-11

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: 61.89  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTCLRLIAGfeqLTSGSIRIHG---------QEAANlpPYQRDVNTVFQDYALFPHMSVLENV 97
Cdd:cd03233    30 VKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGdihyngipyKEFAE--KYPGEIIYVSEEDVHFPTLTVRETL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  98 AYGL------MVKGVakrerlaraqealesvalgfvaerkpahlSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:cd03233   105 DFALrckgneFVRGI-----------------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 172 QMQGELKKLQRQLGITfIFVTHDQS--EALSMSDRVAVFNNGRI 213
Cdd:cd03233   156 EILKCIRTMADVLKTT-TFVSLYQAsdEIYDLFDKVLVLYEGRQ 198
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-223 5.27e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 63.84  E-value: 5.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAG-FEQLTSGSIRIHGQeAANLPPYQRDVNTVFQDYALFPhmSVLENVAYGL 101
Cdd:PLN03232   636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-VAYVPQVSWIFNATVRENILFG--SDFESERYWR 712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  102 MVKGVAKRERLaraqEALESVALGFVAERKpAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQ 181
Cdd:PLN03232   713 AIDVTALQHDL----DLLPGRDLTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE 787

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039033371  182 RQlGITFIFVThDQSEALSMSDRVAVFNNGRIEQVDTPRELY 223
Cdd:PLN03232   788 LK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 5-208 5.86e-11

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: 60.66  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRAVDRVSiDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYqrdvntvfqd 84
Cdd:cd03222     1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY---------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 yalfphmsvlenvayglmvkgvakrerlaraqealesvalgfvaerkpAHLSGGQRQRVALARALVNRPRVLLLDEPLGA 164
Cdd:cd03222    70 ------------------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAY 101

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 165 LDLKLREQMQGELKKLQRQLGITFIFVTHDQSEALSMSDRVAVF 208
Cdd:cd03222   102 LDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
PLN03130 PLN03130
ABC transporter C family member; Provisional
 23-222 6.53e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 63.60  E-value: 6.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAG-FEQLTSGSIRIHGQEAanlppYQRDVNTVFqdyalfpHMSVLENVAYGL 101
Cdd:PLN03130   636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVA-----YVPQVSWIF-------NATVRDNILFGS 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  102 MVKgvakRERLARA------QEALESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ- 172
Cdd:PLN03130   704 PFD----PERYERAidvtalQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQv 779

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039033371  173 ----MQGELKKLQRqlgitfIFVThDQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:PLN03130   780 fdkcIKDELRGKTR------VLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 5-193 8.53e-11

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: 60.81  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFG-DVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRDVNTVFQ 83
Cdd:cd03290     1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 -DYA----LFPHMSVLENVAYGlmvkGVAKRERLARAQEA------LESVALGFVAE--RKPAHLSGGQRQRVALARALV 150
Cdd:cd03290    81 vAYAaqkpWLLNATVEENITFG----SPFNKQRYKAVTDAcslqpdIDLLPFGDQTEigERGINLSGGQRQRICVARALY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQ-MQGELKKLQRQLGITFIFVTH 193
Cdd:cd03290   157 QNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
PTZ00243 PTZ00243
ABC transporter; Provisional
 23-214 1.01e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 63.26  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHgQEAANLPPYQRDVNTVFQDYALFphmsvlenvayglm 102
Cdd:PTZ00243   679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAWIMNATVRGNILF-------------- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  103 vkgvAKRERLARAQEA---------LESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:PTZ00243   744 ----FDEEDAARLADAvrvsqleadLAQLGGGLETEigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1039033371  172 QMQGELkKLQRQLGITFIFVTHdQSEALSMSDRVAVFNNGRIE 214
Cdd:PTZ00243   820 RVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 23-213 1.87e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPYQRdVNTVF-------QDYALFPHM---- 91
Cdd:PRK10982  267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFalvteerRSTGIYAYLdigf 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  92 -SVLENVAYGLMVKGVAKRERLAR-AQEALESVALgfvaeRKPAH------LSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:PRK10982  346 nSLISNIRNYKNKVGLLDNSRMKSdTQWVIDSMRV-----KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033371 164 ALDLKLR---EQMQGELKKlqRQLGItfIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PRK10982  421 GIDVGAKfeiYQLIAELAK--KDKGI--IIISSEMPELLGITDRILVMSNGLV 469
PTZ00243 PTZ00243
ABC transporter; Provisional
 23-230 1.91e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 62.10  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQE--AANLPPYQRDVNTVFQDYALFPHmSVLENVAYG 100
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYGLRELRRQFSMIPQDPVLFDG-TVRQNVDPF 1407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  101 L---------MVKGVAKRERLARAQEALESVALgfvaeRKPAHLSGGQRQRVALARALVNRPR-VLLLDEPLGALDLKLR 170
Cdd:PTZ00243  1408 LeassaevwaALELVGLRERVASESEGIDSRVL-----EGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALD 1482

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  171 EQMQGELkkLQRQLGITFIFVTHdQSEALSMSDRVAVFNNGRIEQVDTPRELYMRPKTPF 230
Cdd:PTZ00243  1483 RQIQATV--MSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-204 2.05e-10

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: 58.54  E-value: 2.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   30 GEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeaanlppyqrdvntvfqdyalfphmsvlenvayglmvkgvakr 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  110 erLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD-----LKLREQMQGELKKLQRQL 184
Cdd:smart00382  38 --GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLLLKSEK 115

                          170       180
                   ....*....|....*....|
gi 1039033371  185 GITFIFVTHDQSEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 15-196 2.32e-10

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: 61.69  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  15 GDVrAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLPPyQRDVNTV--FQDYALFPhMS 92
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVP-QRPYMTLgtLRDQIIYP-DS 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  93 VLEnvaygLMVKGVAKRErlarAQEALESVALGFVAERKPA---------HLSGGQRQRVALARALVNRPRVLLLDEPLG 163
Cdd:TIGR00954 541 SED-----MKRRGLSDKD----LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039033371 164 ALDLklreQMQGELKKLQRQLGITFIFVTHDQS 196
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGITLFSVSHRKS 640
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 257-338 2.56e-10

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: 55.70  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 257 SIRPEHIRLLEQGGAaqdeiqVQGTLQEIHYQGAATRYEIALNGGEKLLVSQANPQwiaeGLQRQIGQPIVACWPRAAMV 336
Cdd:pfam08402   2 AIRPEKIRLAAAANG------LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAH----ARPPAPGDRVGLGWDPEDAH 71


                  ..
gi 1039033371 337 PL 338
Cdd:pfam08402  72 VL 73
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 23-211 2.56e-10

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: 60.26  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG------QEAANLPPYQRDvNTVFQ-DYALFPHMSVle 95
Cdd:cd03291    56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrisfssQFSWIMPGTIKE-NIIFGvSYDEYRYKSV-- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  96 nvayglmVKGVAKRERLARAQEAlESVALGfvaeRKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQM-Q 174
Cdd:cd03291   133 -------VKACQLEEDITKFPEK-DNTVLG----EGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfE 200

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 175 GELKKLQRQLgiTFIFVThDQSEALSMSDRVAVFNNG 211
Cdd:cd03291   201 SCVCKLMANK--TRILVT-SKMEHLKKADKILILHEG 234
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 23-222 3.55e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 59.56  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGfeqLT--SGSIRIHGQ-----EAANL------------PPYQRDvntVFQ 83
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG---LLpgSGSIQFAGQpleawSAAELarhraylsqqqtPPFAMP---VFQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALfpHMSVlenvayglmvkGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARAL-----VNRP--RVL 156
Cdd:PRK03695   89 YLTL--HQPD-----------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 157 LLDEPLGALDLKlreqMQGELKKLQRQL---GITFIFVTHDQSEALSMSDRVAVFNNGRI------EQVDTPREL 222
Cdd:PRK03695  156 LLDEPMNSLDVA----QQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLlasgrrDEVLTPENL 226
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-215 7.74e-10

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 58.67  E-value: 7.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeaanlppyqrDVNTVFQDYALFPHMSVLENVA 98
Cdd:PRK13546   39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  99 YGLMVKGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELK 178
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039033371 179 KLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK13546  188 EFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-254 8.40e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 60.37  E-value: 8.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN--LPPYQRDVNTVFQDYALFPHmSVLENVAYG 100
Cdd:PLN03232  1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  101 LMVKGVAKRERLARA--QEALESVALGFVAE--RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:PLN03232  1334 SEHNDADLWEALERAhiKDVIDRNPFGLDAEvsEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371  177 LKKLQRQlgITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELYMRPKTPFvAEFVGTSNVVRSELAQRLLGESR 254
Cdd:PLN03232  1414 IREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF-FRMVHSTGPANAQYLSNLVFERR 1487
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 5-196 8.83e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 60.04  E-value: 8.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371    5 VQFIDVS---RTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRI---HGQEAANLPPYQRDV 78
Cdd:PTZ00265   383 IQFKNVRfhyDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKI 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   79 NTVFQDYALFPHmSVLENVAYGL----------------------------------------MVKGVAKRE--RLARAQ 116
Cdd:PTZ00265   463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNEliEMRKNY 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  117 EALESVALGFVAERKPAH--------------------LSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGE 176
Cdd:PTZ00265   542 QTIKDSEVVDVSKKVLIHdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621

                          250       260
                   ....*....|....*....|
gi 1039033371  177 LKKLQRQLGITFIFVTHDQS 196
Cdd:PTZ00265   622 INNLKGNENRITIIIAHRLS 641
PLN03073 PLN03073
ABC transporter F family; Provisional
 34-213 4.99e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 57.56  E-value: 4.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  34 SMLGPSGSGKTTCLRLIAGFEQLTSGsirihgqeaanlppyqrdvnTVFQD----YALFPHMSV----LENVAYGLMVK- 104
Cdd:PLN03073  539 AMVGPNGIGKSTILKLISGELQPSSG--------------------TVFRSakvrMAVFSQHHVdgldLSSNPLLYMMRc 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 105 --GVAkrERLARAQeaLESVAL-GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQ 181
Cdd:PLN03073  599 fpGVP--EQKLRAH--LGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039033371 182 RqlGItfIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:PLN03073  675 G--GV--LMVSHDEHLISGSVDELWVVSEGKV 702
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 24-210 6.46e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.95  E-value: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  24 SIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP--PYQRDVNTVFQDY---ALFPHMSVLENVA 98
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeQLQKLVSDEWQRNntdMLSPGEDDTGRTT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  99 YGLMVKGVAKRERLARAQEALESVALgfvAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELK 178
Cdd:PRK10938  103 AEIIQDEVKDPARCEQLAQQFGITAL---LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039033371 179 KLQRQlGITFIFVTHDQSEALSMSDRVAVFNN 210
Cdd:PRK10938  180 SLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 23-211 8.86e-09

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: 57.23  E-value: 8.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHG------QEAANLPPYQRDvNTVFQ-DYALFPHMSVle 95
Cdd:TIGR01271  445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfspQTSWIMPGTIKD-NIIFGlSYDEYRYTSV-- 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   96 nvayglmVKGVAKRERLARAQEAlESVALGfvaeRKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD-LKLREQMQ 174
Cdd:TIGR01271  522 -------IKACQLEEDIALFPEK-DKTVLG----EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKEIFE 589

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039033371  175 GELKKLqrQLGITFIFVThDQSEALSMSDRVAVFNNG 211
Cdd:TIGR01271  590 SCLCKL--MSNKTRILVT-SKLEHLKKADKILLLHEG 623
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 28-194 1.30e-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: 55.07  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  28 QDGEFFSMLGPSGSGKTTCLRLIAGfeqltsgsirihgQEAANL-----PPYQRDVNTVF-----QDY---ALFPHMSVL 94
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAG-------------KLKPNLgkfddPPDWDEILDEFrgselQNYftkLLEGDVKVI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  95 ENVAY------------GLMVKGVAKRERLARAQEALEsvaLGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPL 162
Cdd:cd03236    91 VKPQYvdlipkavkgkvGELLKKKDERGKLDELVDQLE---LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039033371 163 GALDLKLREQMQGELKKLQRQlGITFIFVTHD 194
Cdd:cd03236   168 SYLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-222 1.46e-08

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 56.49  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAAN--LPPYQRDVNTVFQDYALF---------PHM 91
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFsgslrmnldPFS 1384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   92 SVLENVAYglMVKGVAKRERLARAQEAlesvALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:TIGR00957 1385 QYSDEEVW--WALELAHLKTFVSALPD----KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371  172 QMQGELKKlqrQL-GITFIFVTHDQSEALSMSdRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR00957 1459 LIQSTIRT---QFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 27-211 2.57e-08

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 53.02  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTCLRLIAGFEQ--LTSGSIRIHGQEaaNLPPYQRDVNTVFQDYALFPHMSVLENVAYGLMVK 104
Cdd:cd03232    30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRP--LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 105 GvakrerlaraqealesvalgfvaerkpahLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQl 184
Cdd:cd03232   108 G-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS- 157

                         170       180
                  ....*....|....*....|....*...
gi 1039033371 185 GITFIFVTHDQSEAL-SMSDRVAVFNNG 211
Cdd:cd03232   158 GQAILCTIHQPSASIfEKFDRLLLLKRG 185
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 5-208 4.66e-08

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 54.41  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   5 VQFIDVSRTFGDVRavdrVSID---IQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIrihgQEAANL---PPY-QRD 77
Cdd:COG1245   342 VEYPDLTKSYGGFS----LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----DEDLKIsykPQYiSPD 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  78 VN-TVfqdyalfphMSVLENVAYGLMVKGVAKrerlaraQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVL 156
Cdd:COG1245   414 YDgTV---------EEFLRSANTDDFGSSYYK-------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039033371 157 LLDEPLGALDLKLREQMQGELKKLQRQLGITFIFVTHDqseaLSM----SDRVAVF 208
Cdd:COG1245   478 LLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVF 529
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 27-237 4.74e-08

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: 53.37  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTC----LRLIAGFEqltsGSIRIHGQEAANLPPY--QRDVNTVFQDYALFPHmsvleNVAYG 100
Cdd:cd03288    44 IKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILFSG-----SIRFN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMVKGVAKRERLaraQEALESVALGFVAERKPAHL-----------SGGQRQRVALARALVNRPRVLLLDEPLGALDLKL 169
Cdd:cd03288   115 LDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371 170 REQMQGELkkLQRQLGITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELYMRPKTPFvAEFVGT 237
Cdd:cd03288   192 ENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLVRT 255
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 10-225 5.40e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.41  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  10 VSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIH-----GQEAANLPPYQRDVNTVFQd 84
Cdd:PRK10636  318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQLEFLRADESPLQ- 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  85 yalfpHMSVLenvayglmvkgvAKRERLARAQEALESvaLGFVAER---KPAHLSGGQRQRVALARALVNRPRVLLLDEP 161
Cdd:PRK10636  397 -----HLARL------------APQELEQKLRDYLGG--FGFQGDKvteETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371 162 LGALDLKLREQMQGELKKLQRQLgitfIFVTHDQSEALSMSDRVAVFNNGRIEQVDTPRELYMR 225
Cdd:PRK10636  458 TNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
PLN03140 PLN03140
ABC transporter G family member; Provisional
 30-166 5.88e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 54.47  E-value: 5.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   30 GEFFSMLGPSGSGKTTCLRLIAGFEQ--LTSGSIRIHG----QEA-ANLPPY--QRDVNTvfqdyalfPHMSVLENVAYG 100
Cdd:PLN03140   906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkQETfARISGYceQNDIHS--------PQVTVRESLIYS 977

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039033371  101 LMV---KGVAKRERLARAQEALESVAL-----GFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALD 166
Cdd:PLN03140   978 AFLrlpKEVSKEEKMMFVDEVMELVELdnlkdAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 23-213 6.26e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 52.87  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFE--QLTSGSIRIHGQEAANLPPYQRDVNTVFQdyaLFPHMSVLENVAYG 100
Cdd:PRK09580   20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFM---AFQYPVEIPGVSNQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LMVKGVAKRERLARAQEALESVALGFVAERK------PAHL---------SGGQRQRVALARALVNRPRVLLLDEPLGAL 165
Cdd:PRK09580   97 FFLQTALNAVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039033371 166 D---LKLREQMQGELKKLQRqlgiTFIFVTHDQSEALSMS-DRVAVFNNGRI 213
Cdd:PRK09580  177 DidaLKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRI 224
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 35-194 6.42e-08

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 54.02  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  35 MLGPSGSGKTTCLRLIAGfeqltsgsirihgQEAANLPPYQRDVN--TVFQDYA---LFPHMSVLEN----VAY------ 99
Cdd:COG1245   104 ILGPNGIGKSTALKILSG-------------ELKPNLGDYDEEPSwdEVLKRFRgteLQDYFKKLANgeikVAHkpqyvd 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 100 --GLMVKGVAkRERLARAQE--ALESVA----LGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLRE 171
Cdd:COG1245   171 liPKVFKGTV-RELLEKVDErgKLDELAeklgLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249

                         170       180
                  ....*....|....*....|...
gi 1039033371 172 QMQGELKKLQRQlGITFIFVTHD 194
Cdd:COG1245   250 NVARLIRELAEE-GKYVLVVEHD 271
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 27-213 6.76e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 54.34  E-value: 6.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   27 IQDGEFFSMLGPSGSGKTTCLRLIA----GFEQLTSGSIRIHGQEAANLPP-YQRDVNTVFQDYALFPHMSVLENVAYGL 101
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKhYRGDVVYNAETDVHFPHLTVGETLDFAA 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  102 MVKGVAKRERLARAQEALESVALGFVAERKPAH-------------LSGGQRQRVALARALVNRPRVLLLDEPLGALDLK 168
Cdd:TIGR00956  164 RCKTPQNRPDGVSREEYAKHIADVYMATYGLSHtrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039033371  169 LREQMQGELKKLQRQLGIT-FIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:TIGR00956  244 TALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQ 289
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 14-198 7.09e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.87  E-value: 7.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  14 FGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGfeqltsgsirIHGQEAAN---LPPYQR-------DV----- 78
Cdd:PRK10938  270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----------DHPQGYSNdltLFGRRRgsgetiwDIkkhig 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 ---NTVFQDYALfpHMSVLENVAYGL-----MVKGVAKRERLaRAQEALESVALGFVAERKPAH-LSGGQrQRVAL-ARA 148
Cdd:PRK10938  340 yvsSSLHLDYRV--STSVRNVILSGFfdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQ-QRLALiVRA 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 149 LVNRPRVLLLDEPLGALD-----LKLR--EQMQGElkkLQRQLgitfIFVTHDQSEA 198
Cdd:PRK10938  416 LVKHPTLLILDEPLQGLDplnrqLVRRfvDVLISE---GETQL----LFVSHHAEDA 465
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-208 8.84e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 53.66  E-value: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSI----RIhgqeaANLPPYQRDvntvfqDYalfpHMSVlenvayglm 102
Cdd:PRK13409  362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKI-----SYKPQYIKP------DY----DGTV--------- 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 vkgvakRERLARAQEALES----------VALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13409  418 ------EDLLRSITDDLGSsyykseiikpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039033371 173 MQGELKKLQRQLGITFIFVTHDqseaLSM----SDRVAVF 208
Cdd:PRK13409  492 VAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVF 527
PLN03130 PLN03130
ABC transporter C family member; Provisional
 110-243 1.25e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 53.59  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  110 ERLARA--QEALESVALGFVAERKPA--HLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlg 185
Cdd:PLN03130  1346 ESLERAhlKDVIRRNSLGLDAEVSEAgeNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS-- 1423

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039033371  186 ITFIFVTHDQSEALSmSDRVAVFNNGRIEQVDTPRELYMRPKTPFvaefvgtSNVVRS 243
Cdd:PLN03130  1424 CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAF-------SKMVQS 1473
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 17-205 3.11e-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: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  17 VRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRliAGFEqlTSGSIRIhgqeAANLPPYQRDvNTVFQDyalfphmsvlen 96
Cdd:cd03238     8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARL----ISFLPKFSRN-KLIFID------------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 vAYGLMVKgvakrerlaraqealesVALGFVA-ERKPAHLSGGQRQRVALARALVNRPR--VLLLDEPLGALDLKLREQM 173
Cdd:cd03238    67 -QLQFLID-----------------VGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039033371 174 QGELKKLqRQLGITFIFVTHDQsEALSMSDRV 205
Cdd:cd03238   129 LEVIKGL-IDLGNTVILIEHNL-DVLSSADWI 158
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-194 3.41e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 51.73  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  27 IQDGEFFSMLGPSGSGKTTCLRLIAGfeQLTSgsirihgqeaaNLPPYQRDVN----------TVFQDYalfphmsvLEN 96
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILSG--ELIP-----------NLGDYEEEPSwdevlkrfrgTELQNY--------FKK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  97 VAYGLM---------------VKGVAkRERLARAQEA------LESVALGFVAERKPAHLSGGQRQRVALARALVNRPRV 155
Cdd:PRK13409  155 LYNGEIkvvhkpqyvdlipkvFKGKV-RELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039033371 156 LLLDEPLGALDLKLREQMQGELKKLQRqlGITFIFVTHD 194
Cdd:PRK13409  234 YFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
PLN03073 PLN03073
ABC transporter F family; Provisional
 113-193 3.47e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.78  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 113 ARAQEALesVALGFVAE---RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlgiTFI 189
Cdd:PLN03073  322 ARAASIL--AGLSFTPEmqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFI 395


                  ....
gi 1039033371 190 FVTH 193
Cdd:PLN03073  396 VVSH 399
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 19-200 4.03e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 51.43  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  19 AVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIRIHGqeAANLPPYQRDVNTvfqdyalfpHMSVLENVA 98
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--SAALIAISSGLNG---------QLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  99 Y-GLMVkGVAKRERLARAQEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGEL 177
Cdd:PRK13545  108 LkGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186

                         170       180
                  ....*....|....*....|...
gi 1039033371 178 KKLQRQlGITFIFVTHDQSEALS 200
Cdd:PRK13545  187 NEFKEQ-GKTIFFISHSLSQVKS 208
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 37-160 4.50e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 49.48  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  37 GPSGSGKTTCLRLIAGFEQLTSGSIRIHGQEAANLP-PYqrdVNTVFQDYALFPHMSVLENVAYGLMVKGVAkrerlARA 115
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFENLKFWSEIYNSA-----ETL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039033371 116 QEALESVALGFVAERKPAHLSGGQRQRVALARALVNRPRVLLLDE 160
Cdd:PRK13541  105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-213 8.03e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.56  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAG--FEQLTSGSIRIHGQEAanlppyqrDVNTVFQ-------------- 83
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEV--------DVSTVSDaidaglayvtedrk 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  84 DYALFPHMSVLENV-AYGLmvKGVAKRERLARAQEALesvalgfVAER--------------KPAHLSGGQRQRVALARA 148
Cdd:NF040905  348 GYGLNLIDDIKRNItLANL--GKVSRRGVIDENEEIK-------VAEEyrkkmniktpsvfqKVGNLSGGNQQKVVLSKW 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 149 LVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQSEALSMSDRVAVFNNGRI 213
Cdd:NF040905  419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 3-277 8.23e-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: 49.85  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   3 IAVQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTclrLIAGFEQL--TSGSIRIHG--QEAANLPPYQRDV 78
Cdd:cd03289     3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRLlnTEGDIQIDGvsWNSVPLQKWRKAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  79 NTVFQDYALFPHmSVLENvaygLMVKGVAKRERLARAQE--ALESV------ALGFVAERKPAHLSGGQRQRVALARALV 150
Cdd:cd03289    80 GVIPQKVFIFSG-TFRKN----LDPYGKWSDEEIWKVAEevGLKSVieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 151 NRPRVLLLDEPLGALDLKLREQMQGELKklQRQLGITFIFVTHdQSEALSMSDRVAVFNNGRIEQVDTPRELYmrPKTPF 230
Cdd:cd03289   155 SKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQYDSIQKLL--NEKSH 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039033371 231 VAEFVGTSNvvRSELAQRLLGESRTFSIRPEHIRLLEQggaAQDEIQ 277
Cdd:cd03289   230 FKQAISPSD--RLKLFPRRNSSKSKRKPRPQIQALQEE---TEEEVQ 271
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 13-213 1.42e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 48.87  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  13 TFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFE--QLTSGSIRIHGQEAANLPPYQRdvntvfqdyalfPH 90
Cdd:CHL00131   16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER------------AH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  91 MSVLENVAYGLMVKGVAKRE--RLA-----RAQEALESVALGF---------VAERKPAHL--------SGGQRQRVA-L 145
Cdd:CHL00131   84 LGIFLAFQYPIEIPGVSNADflRLAynskrKFQGLPELDPLEFleiineklkLVGMDPSFLsrnvnegfSGGEKKRNEiL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 146 ARALVNrPRVLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQS--EALSmSDRVAVFNNGRI 213
Cdd:CHL00131  164 QMALLD-SELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRllDYIK-PDYVHVMQNGKI 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 5-222 5.92e-06

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: 48.37  E-value: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371    5 VQFIDVSRTFGDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTclrLIAGFEQL--TSGSIRIHG--QEAANLPPYQRDVNT 80
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLlsTEGEIQIDGvsWNSVTLQTWRKAFGV 1296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   81 VFQDYALFPhmsvlenvayGLMVKGVAKRERLARAQ--EALESVALGFVAERKPAHL-----------SGGQRQRVALAR 147
Cdd:TIGR01271 1297 IPQKVFIFS----------GTFRKNLDPYEQWSDEEiwKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLAR 1366

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371  148 ALVNRPRVLLLDEPLGALDLKLREQMQGELKklQRQLGITFIFVTHdQSEALSMSDRVAVFNNGRIEQVDTPREL 222
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEH-RVEALLECQQFLVIEGSSVKQYDSIQKL 1438
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 21-206 6.26e-06

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: 45.81  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  21 DRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAgfeqltsgsirihgqeaanlppyqrdvntvfqdYALFPHMSVLENVAYG 100
Cdd:cd03227    12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 101 LmvkgvakrerlARAQEALESVALGFVAERkpahLSGGQRQRVALARALVNR---PRVL-LLDEPLGALDLKlREQMQGE 176
Cdd:cd03227    59 K-----------AGCIVAAVSAELIFTRLQ----LSGGEKELSALALILALAslkPRPLyILDEIDRGLDPR-DGQALAE 122

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039033371 177 LKKLQRQLGITFIFVTHDqSEALSMSDRVA 206
Cdd:cd03227   123 AILEHLVKGAQVIVITHL-PELAELADKLI 151
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 20-194 1.10e-05

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: 45.68  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  20 VDRVSI-------DIQDGEFFSML----GPSGSGKTTCLrliagfeqltsgsirihgqEAANlppyqrdvntvfqdYALF 88
Cdd:cd03240     1 IDKLSIrnirsfhERSEIEFFSPLtlivGQNGAGKTTII-------------------EALK--------------YALT 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  89 PHMSvlenvaygLMVKGVAKRERLARAQEALESVALGF--------VAERKPA----------------------HLSGG 138
Cdd:cd03240    48 GELP--------PNSKGGAHDPKLIREGEVRAQVKLAFenangkkyTITRSLAilenvifchqgesnwplldmrgRCSGG 119

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039033371 139 QRQ------RVALARALVNRPRVLLLDEPLGALD-----LKLREQMQGELKKLQRQLGItfifVTHD 194
Cdd:cd03240   120 EKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIV----ITHD 182
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 60-222 1.38e-05

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: 46.93  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  60 SIRIHG---QEAANLPpyQRDVNTVFQDYALFPHmsvlENVAYGLMVKGVakRERLaraqEALESVALGFVA-ERKPAHL 135
Cdd:TIGR00630 422 AVTVGGksiADVSELS--IREAHEFFNQLTLTPE----EKKIAEEVLKEI--RERL----GFLIDVGLDYLSlSRAAGTL 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 136 SGGQRQRVALAR----ALVNrprVL-LLDEPLGALDLKLREQMQGELKKLqRQLGITFIFVTHDqSEALSMSDRV----- 205
Cdd:TIGR00630 490 SGGEAQRIRLATqigsGLTG---VLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVidigp 564

                         170
                  ....*....|....*...
gi 1039033371 206 -AVFNNGRIEQVDTPREL 222
Cdd:TIGR00630 565 gAGEHGGEVVASGTPEEI 582
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 23-194 2.43e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 46.04  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371  23 VSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQLTSGSIrihgqeaaNLPPYQRdVNTVFQDYALFPHMSVLENVAYGLM 102
Cdd:PRK15064   20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNER-LGKLRQDQFAFEEFTVLDTVIMGHT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 103 VKGVAKRER-----LARAQEA-------LESVAL---GFVAERKPAHL------------------SGGQRQRVALARAL 149
Cdd:PRK15064   91 ELWEVKQERdriyaLPEMSEEdgmkvadLEVKFAemdGYTAEARAGELllgvgipeeqhyglmsevAPGWKLRVLLAQAL 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039033371 150 VNRPRVLLLDEPLGALDLKLREQMQGELKklQRQlgITFIFVTHD 194
Cdd:PRK15064  171 FSNPDILLLDEPTNNLDINTIRWLEDVLN--ERN--STMIIISHD 211
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 15-166 8.82e-05

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 44.33  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   15 GDVRAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAgfEQLTSGSIRiHGQEAANLPP----YQRDVNTVFQDYALFPH 90
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPldssFQRSIGYVQQQDLHLPT 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371   91 MSVLENV---AYGLMVKGVAKRERLARAQEA-----LESVALGFVAErkPAH-LSGGQRQRVALARALVNRPRVLL-LDE 160
Cdd:TIGR00956  851 STVRESLrfsAYLRQPKSVSKSEKMEYVEEViklleMESYADAVVGV--PGEgLNVEQRKRLTIGVELVAKPKLLLfLDE 928


                   ....*.
gi 1039033371  161 PLGALD 166
Cdd:TIGR00956  929 PTSGLD 934
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 129-205 1.12e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.05  E-value: 1.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039033371  129 ERKPAHLSGGQRQRVALARALVNRPR--VLLLDEPLGALDLKLREQMQGELKKLQRQlGITFIFVTHDQsEALSMSDRV 205
Cdd:PRK00635   471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRI 547
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 113-195 1.75e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 43.23  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 113 ARAQEALEsvALGFVAE---RKPAHLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKLQRqlgiTFI 189
Cdd:PRK10636  127 SRAASLLH--GLGFSNEqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLI 200


                  ....*.
gi 1039033371 190 FVTHDQ 195
Cdd:PRK10636  201 LISHDR 206
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 109-205 5.35e-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: 40.70  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033371 109 RERLaraqEALESVALGFVA-ERKPAHLSGGQRQRVALARALVNRPRVLL--LDEPLGALDLKLREQMQGELKKLqRQLG 185
Cdd:cd03270   115 RERL----GFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLG 189

                          90       100
                  ....*....|....*....|
gi 1039033371 186 ITFIFVTHDQsEALSMSDRV 205
Cdd:cd03270   190 NTVLVVEHDE-DTIRAADHV 208
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 111-161 6.97e-04

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 40.68  E-value: 6.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 111 RLARAQEALESVALGFVAERKPAH-LSGGQRQRVALARALVNRPR---VLLLDEP 161
Cdd:cd03271   145 KIARKLQTLCDVGLGYIKLGQPATtLSGGEAQRIKLAKELSKRSTgktLYILDEP 199
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 111-161 3.03e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.61  E-value: 3.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039033371 111 RLARAQEALESVALGFVAERKPAH-LSGGQRQRVALARALVNR---PRVLLLDEP 161
Cdd:TIGR00630 805 SISRKLQTLCDVGLGYIRLGQPATtLSGGEAQRIKLAKELSKRstgRTLYILDEP 859
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 27-59 3.69e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.91  E-value: 3.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1039033371  27 IQDGEFFSML--GPSGSGKTTCLRLIAG-----FEQL---TSG 59
Cdd:PRK13342   31 IEAGRLSSMIlwGPPGTGKTTLARIIAGatdapFEALsavTSG 73
 
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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