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Conserved domains on  [gi|1371712025|gb|PST29112|]
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ABC transporter ATP-binding protein [Mesorhizobium loti]

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 ...
 20-381 0e+00

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 564.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNM 99
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 260 FDGKVTSAEDGYIRvetTGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAhapvNAAEGEIWDIGYLGDMTVFHIR 339
Cdd:COG3842   242 LPGTVLGDEGGGVR---TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPE----NGLPGTVEDVVFLGSHVRYRVR 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 340 LKDGKVVKASSLNAVRAvedPLGYDQQVWISFGDDAGVVLKD 381
Cdd:COG3842   315 LGDGQELVVRVPNRAAL---PLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-381 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 564.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNM 99
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 260 FDGKVTSAEDGYIRvetTGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAhapvNAAEGEIWDIGYLGDMTVFHIR 339
Cdd:COG3842   242 LPGTVLGDEGGGVR---TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPE----NGLPGTVEDVVFLGSHVRYRVR 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 340 LKDGKVVKASSLNAVRAvedPLGYDQQVWISFGDDAGVVLKD 381
Cdd:COG3842   315 LGDGQELVVRVPNRAAL---PLEPGDRVGLSWDPEDVVVLPA 353
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
19-379 1.58e-170

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 480.87  E-value: 1.58e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVN 98
Cdd:PRK11607   15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK11607   95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVN 258
Cdd:PRK11607  175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 259 IFDGKVTSAEDGYIRVETTGGI-PVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAHApVNAAEGEIWDIGYLGDMTVFH 337
Cdd:PRK11607  255 VFEGVLKERQEDGLVIDSPGLVhPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADG-CNFAVGEVIHIAYLGDLSIYH 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 338 IRLKDGKVVKASSLNAVRAVEDPLGYDQQVWISFGDDAGVVL 379
Cdd:PRK11607  334 VRLKSGQMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVL 375
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 24-255 1.90e-148

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: 418.95  E-value: 1.90e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIG 255
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 54-379 4.50e-141

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: 403.80  E-value: 4.50e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  54 LLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAER 133
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 134 VAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHD 213
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 214 QEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFDGKVTSAEDGYIRVETTGGIPVRMASPEKPGNG 293
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 294 AKAAVAIRPEKIRIGRQPPAHApVNAAEGEIWDIGYLGDMTVFHIRLKDGKVVKASSLNAVRAVEDPLGYDQQVWISFGD 373
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANS-SNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHP 319


                  ....*.
gi 1371712025 374 DAGVVL 379
Cdd:TIGR01187 320 GSEVVL 325
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
24-371 3.30e-96

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 290.44  E-value: 3.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTaVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFDGK 263
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 264 VTsaEDGYIRVETTGGIpvRMASPEKpgNGAKAAVAIRPEKIRIGRQPPAHAPVNAAEGEIWDIGYLGDMTVFHIRLkdG 343
Cdd:NF040840  241 AE--KGGEGTILDTGNI--KIELPEE--KKGKVRIGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKLTLDV--G 312

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1371712025 344 KVVKA----SSLnavraVEDPLGYDQQVWISF 371
Cdd:NF040840  313 IILVAfitrSSF-----LDLEINEGKEVYASF 339
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 39-180 3.68e-49

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 162.82  E-value: 3.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG--IPPYRRPVNMMFQSYALFPHMTVENNV 116
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 117 AFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-244 2.67e-39

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 149.12  E-value: 2.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  16 ADPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL-AGIPPYR 94
Cdd:NF033858  259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIATR 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:NF033858  339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 175 LLLDEPLGALDKKLREetQF-ELM-DLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:NF033858  419 LILDEPTSGVDPVARD--MFwRLLiELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
33-227 2.03e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 117.72  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  33 FGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNmmfqsyALFPhMTV 112
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 113 ENNVAFGLKQD----GMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1371712025 189 REETQfELMDLQQELGLTFVVVTHDQEEAMTmADRIAVM 227
Cdd:NF040873  155 RERII-ALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-243 3.17e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.55  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGiPPYRRPVN----M 99
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVCpriaY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYA--LFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:NF033858   81 MPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 178 DEPLGALDKKLREetQF-ELMD-LQQEL-GLTFVVVTHDQEEAMTMaDRIAVMSHGKVVQVATPAEIYE 243
Cdd:NF033858  161 DEPTTGVDPLSRR--QFwELIDrIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
GguA NF040905
sugar ABC transporter ATP-binding protein;
27-234 5.75e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 79.06  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  27 KNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPT---SGEIILDGQ--SLAGIP-PYRRPVNMM 100
Cdd:NF040905    5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEvcRFKDIRdSEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAE---RVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:NF040905   84 HQELALIPYLSIAENIFLGNERAKRGVIDWNEtnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 178 DEPLGALDkklrEETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:NF040905  164 DEPTAALN----EEDSAALLDLLLELkaqGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
24-233 1.51e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 70.92  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCG--KSTLLRMLAGfeqPTSGE-------IILDGQSLAGIPPYR 94
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*tWCANRRALRRTIG*H 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNM-MFQSYAlfphmTVENNVAFGLKQDgMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:NF000106   91 RPVR*gRRESFS-----GRENLYMIGR*LD-LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 174 VLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 48-226 1.58e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 64.70  E-value: 1.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   48 TREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGqslagippyrrpvnmmfqsyalfphmtvennvafglkqdgmpk 127
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  128 adiAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFE-----LMDLQQE 202
Cdd:smart00382  38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 1371712025  203 LGLTFVVVTHDQEEAMTMADRIAV 226
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
154-233 8.27e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.48  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRPKVLLLDEP-----LGAldkklreetQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIA 225
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIY 475


                  ....*...
gi 1371712025 226 VMSHGKVV 233
Cdd:NF040905  476 VMNEGRIT 483
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-381 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 564.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNM 99
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 260 FDGKVTSAEDGYIRvetTGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAhapvNAAEGEIWDIGYLGDMTVFHIR 339
Cdd:COG3842   242 LPGTVLGDEGGGVR---TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPE----NGLPGTVEDVVFLGSHVRYRVR 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 340 LKDGKVVKASSLNAVRAvedPLGYDQQVWISFGDDAGVVLKD 381
Cdd:COG3842   315 LGDGQELVVRVPNRAAL---PLEPGDRVGLSWDPEDVVVLPA 353
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
19-379 1.58e-170

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 480.87  E-value: 1.58e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVN 98
Cdd:PRK11607   15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK11607   95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVN 258
Cdd:PRK11607  175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 259 IFDGKVTSAEDGYIRVETTGGI-PVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAHApVNAAEGEIWDIGYLGDMTVFH 337
Cdd:PRK11607  255 VFEGVLKERQEDGLVIDSPGLVhPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADG-CNFAVGEVIHIAYLGDLSIYH 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 338 IRLKDGKVVKASSLNAVRAVEDPLGYDQQVWISFGDDAGVVL 379
Cdd:PRK11607  334 VRLKSGQMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVL 375
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 24-371 1.43e-153

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 436.43  E-value: 1.43e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:COG3839    84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGD--VNIFD 261
Cdd:COG3839   164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 262 GKVtsaEDGYIRVettGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPahapvNAAEGEIWDIGYLGDMTVFHIRLK 341
Cdd:COG3839   244 GTV---EGGGVRL---GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGD-----GGLEATVEVVEPLGSETLVHVRLG 312

                         330       340       350
                  ....*....|....*....|....*....|
gi 1371712025 342 DGKVVkasslnAVRAVEDPLGYDQQVWISF 371
Cdd:COG3839   313 GQELV------ARVPGDTRLRPGDTVRLAF 336
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
21-381 1.26e-148

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 425.13  E-value: 1.26e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMM 100
Cdd:PRK09452   12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:PRK09452   92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 181 LGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIF 260
Cdd:PRK09452  172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 261 DGKVTSA-EDGYIRVETTGGI-PVRMASPEKPGNGAKaaVAIRPEKIRIgRQPPAHAPVNAAEGEIWDIGYLGdMTV-FH 337
Cdd:PRK09452  252 DATVIERlDEQRVRANVEGREcNIYVNFAVEPGQKLH--VLLRPEDLRV-EEINDDEHAEGLIGYVRERNYKG-MTLdSV 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1371712025 338 IRLKDGKVVKASS-LNAvravEDP-LGY--DQQVWISFGDDAGVVLKD 381
Cdd:PRK09452  328 VELENGKMVMVSEfFNE----DDPdFDHslGQKVAVTWVEGWEVVLAD 371
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 24-255 1.90e-148

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: 418.95  E-value: 1.90e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIG 255
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 54-379 4.50e-141

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: 403.80  E-value: 4.50e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  54 LLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAER 133
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 134 VAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHD 213
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 214 QEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFDGKVTSAEDGYIRVETTGGIPVRMASPEKPGNG 293
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 294 AKAAVAIRPEKIRIGRQPPAHApVNAAEGEIWDIGYLGDMTVFHIRLKDGKVVKASSLNAVRAVEDPLGYDQQVWISFGD 373
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANS-SNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHP 319


                  ....*.
gi 1371712025 374 DAGVVL 379
Cdd:TIGR01187 320 GSEVVL 325
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 24-343 1.55e-139

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 400.68  E-value: 1.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL-AGIPPYRRPVNMMFQ 102
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFDG 262
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 263 KVtsaEDGYIRVettGGIPVRMASPEKPGngaKAAVAIRPEKIRIGRQPPAHapvNAAEGEIWDIGYLGDMTVFHIRLKD 342
Cdd:COG1118   243 RV---IGGQLEA---DGLTLPVAEPLPDG---PAVAGVRPHDIEVSREPEGE---NTFPATVARVSELGPEVRVELKLED 310


                  .
gi 1371712025 343 G 343
Cdd:COG1118   311 G 311
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 20-371 9.59e-131

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: 378.61  E-value: 9.59e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNM 99
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 260 FDGKVtsAEDGYIRVettgGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPPAHapvNAAEGEIWDIGYLGDMTVFHIR 339
Cdd:TIGR03265 241 LPGTR--GGGSRARV----GGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNAA---NLLLARVEDMEFLGAFYRLRLR 311

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1371712025 340 LK--DGKVVKAS-SLNAVRavEDPLGYDQQVWISF 371
Cdd:TIGR03265 312 LEglPGQALVADvSASEVE--RLGIRAGQPIWIEL 344
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 24-236 3.51e-120

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: 346.43  E-value: 3.51e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVA 236
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 24-256 2.09e-112

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: 327.76  E-value: 2.09e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLK----QDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03296    83 YALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGD 256
Cdd:cd03296   163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
24-346 3.80e-109

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 323.72  E-value: 3.80e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQ 102
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGD--VNIF 260
Cdd:PRK11650  164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 261 DGKVtsAEDGyIRVETTGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGR-QPPAHAPVNAAEgeiwdigYLGDMTVFHIR 339
Cdd:PRK11650  244 DGRV--SADG-AAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSaEGGVPLTVDTVE-------LLGADNLAHGR 313


                  ....*..
gi 1371712025 340 LKDGKVV 346
Cdd:PRK11650  314 WGGQPLV 320
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 18-243 2.46e-106

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 313.18  E-value: 2.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY 93
Cdd:COG1116     2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRpvnMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:COG1116    82 RG---VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 174 VLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGkvvqvatPAEIYE 243
Cdd:COG1116   159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR-------PGRIVE 221
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 24-259 3.55e-105

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 309.42  E-value: 3.55e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 24-236 4.28e-105

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: 308.41  E-value: 4.28e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVA 236
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 24-235 1.19e-103

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: 304.78  E-value: 1.19e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPyrrPVNM 99
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMS--HGKVVQV 235
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 24-255 7.22e-102

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 303.55  E-value: 7.22e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY--RRpvNMM 100
Cdd:COG1125     2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelRR--RIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 F--QSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL--EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLL 176
Cdd:COG1125    80 YviQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 177 LDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIG 255
Cdd:COG1125   160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
21-310 8.21e-101

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 302.41  E-value: 8.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMM 100
Cdd:PRK11432    4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:PRK11432   84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 181 LGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIF 260
Cdd:PRK11432  164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIF 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 261 DGKVtsaEDGYIRVettGG--IPVRMASPEKPGNGAkAAVAIRPEKIRIGRQ 310
Cdd:PRK11432  244 PATL---SGDYVDI---YGyrLPRPAAFAFNLPDGE-CTVGVRPEAITLSEQ 288
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
24-344 2.30e-100

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 301.95  E-value: 2.30e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:PRK11000    4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:PRK11000   84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGD--VNIFD 261
Cdd:PRK11000  164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkMNFLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 262 GKVTSAEDGYIRVETTGG----IPVRMASPEKpgnGAKAAVAIRPEKIrigrQPPAHAPVnAAEGEIWDIGYLGDMTVFH 337
Cdd:PRK11000  244 VKVTATAIEQVQVELPNRqqvwLPVEGRGVQV---GANMSLGIRPEHL----LPSDIADV-TLEGEVQVVEQLGNETQIH 315


                  ....*..
gi 1371712025 338 IRLKDGK 344
Cdd:PRK11000  316 IQIPAIR 322
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
24-371 3.30e-96

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 290.44  E-value: 3.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTaVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFDGK 263
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 264 VTsaEDGYIRVETTGGIpvRMASPEKpgNGAKAAVAIRPEKIRIGRQPPAHAPVNAAEGEIWDIGYLGDMTVFHIRLkdG 343
Cdd:NF040840  241 AE--KGGEGTILDTGNI--KIELPEE--KKGKVRIGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKLTLDV--G 312

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1371712025 344 KVVKA----SSLnavraVEDPLGYDQQVWISF 371
Cdd:NF040840  313 IILVAfitrSSF-----LDLEINEGKEVYASF 339
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
24-268 8.10e-95

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 287.37  E-value: 8.10e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQdgMPK------ADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK10851   83 YALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 178 DEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDV 257
Cdd:PRK10851  161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240

                         250
                  ....*....|.
gi 1371712025 258 NIFDGKVTSAE 268
Cdd:PRK10851  241 NRLQGTIRGGQ 251
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 24-255 5.22e-94

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: 281.11  E-value: 5.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMM 100
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPveLRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLE--KFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIG 255
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 24-347 7.60e-90

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: 274.95  E-value: 7.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP--TSGEIILDGQSLAGIPPYRRPVNMMF 101
Cdd:TIGR03258   6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 182 GALDKKLREETQFELMDLQQEL-GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIF 260
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 261 DGKVTSAEDGYIRVETTGGIPVRMASPEKPGNGAKAAVAIRPEKIRIGRQPpahAPVNAAEGEIWDIGYLGDMTVFHIRL 340
Cdd:TIGR03258 246 PAIALGITEAPGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLALTPRP---AGEGRFHATIASVEWHGAALHLLCDL 322


                  ....*..
gi 1371712025 341 KDGKVVK 347
Cdd:TIGR03258 323 DAACDEP 329
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 29-258 5.41e-86

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: 261.81  E-value: 5.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  29 VTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------YRRPVNMMFQ 102
Cdd:cd03294    30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMVFQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:cd03294   110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVN 258
Cdd:cd03294   190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 24-259 8.25e-86

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: 259.96  E-value: 8.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTaVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03299     1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNI 259
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 9-245 1.74e-84

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: 266.00  E-value: 1.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   9 RRSFAPWADPASKPFISVKNVTKKF-----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILD 83
Cdd:COG1123   246 ARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  84 GQSLAGIP-----PYRRPVNMMFQ--SYALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQL 154
Cdd:COG1123   326 GKDLTKLSrrslrELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLpPDLADRYPHEL 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 155 SGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:COG1123   406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485

                         250
                  ....*....|.
gi 1371712025 235 VATPAEIYEAP 245
Cdd:COG1123   486 DGPTEEVFANP 496
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 19-254 2.93e-84

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: 256.06  E-value: 2.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-----PY 93
Cdd:COG1127     1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQSYALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRP 172
Cdd:COG1127    81 RRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 173 KVLLLDEP--------LGALDKKLREetqfelmdLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:COG1127   161 EILLYDEPtagldpitSAVIDELIRE--------LRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232

                         250
                  ....*....|
gi 1371712025 245 PNSrFVADFI 254
Cdd:COG1127   233 DDP-WVRQFL 241
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
24-257 1.28e-80

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 250.38  E-value: 1.28e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YR 94
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKklrEETQ--FELM-DLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVA 251
Cdd:COG1135   162 LLCDEATSALDP---ETTRsiLDLLkDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238


                  ....*.
gi 1371712025 252 DFIGDV 257
Cdd:COG1135   239 RFLPTV 244
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
21-233 4.75e-80

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 244.95  E-value: 4.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP---- 92
Cdd:COG1136     2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErela 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 -YRR-PVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:COG1136    82 rLRRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETqFELM-DLQQELGLTFVVVTHDqEEAMTMADRIAVMSHGKVV 233
Cdd:COG1136   162 RPKLILADEPTGNLDSKTGEEV-LELLrELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
24-255 1.08e-79

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 244.28  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNiyTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:COG3840     2 LRLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLA-KRPkVLLLDEPLG 182
Cdd:COG3840    80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIG 255
Cdd:COG3840   159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 24-231 9.65e-79

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: 239.78  E-value: 9.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG----IPPYRRPVNM 99
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGlkqdgmpkadiaervaqmlklvklekfakrkphqLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 180 PLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 31-290 1.53e-78

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


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 245.92  E-value: 1.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  31 KKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------YRRPVNMMFQSY 104
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGAL 184
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 185 DKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFdgKV 264
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLS--QV 238

                         250       260
                  ....*....|....*....|....*.
gi 1371712025 265 TSAEDGYIRVETTggiPVRMASPEKP 290
Cdd:TIGR01186 239 FDAERIAQRMNTG---PITKTADKGP 261
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 24-257 4.19e-78

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 240.28  E-value: 4.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG----IPPYRRPVNM 99
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALDKKLREETqFELM-DLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDV 257
Cdd:COG1126   162 EPTSALDPELVGEV-LDVMrDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 24-232 1.37e-76

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 235.85  E-value: 1.37e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------Y 93
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:cd03255    81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 174 VLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMtMADRIAVMSHGKV 232
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
24-241 1.64e-76

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 236.11  E-value: 1.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQ 102
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAF--GLKqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:COG1131    81 EPALYPDLTVRENLRFfaRLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 181 LGALDKKLREetqfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG1131   159 TSGLDPEARR----ELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 24-245 1.72e-76

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: 235.69  E-value: 1.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPPYRRPVNMM 100
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQS--YALFpHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALDKKLREetqfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:COG1122   160 EPTAGLDPRGRR----ELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 24-245 3.07e-75

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: 232.86  E-value: 3.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YR 94
Cdd:cd03258     2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 24-262 8.71e-74

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: 229.69  E-value: 8.71e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG----DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPV 97
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSY--ALFPHMTVENNVAFGLKQDGMPkaDIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFI 254
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELL 239


                  ....*...
gi 1371712025 255 GDVNIFDG 262
Cdd:COG1124   240 AASLAFER 247
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
24-240 1.29e-73

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 228.40  E-value: 1.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA-----GIPPYRRPV 97
Cdd:COG2884     2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrrEIPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 178 DEPLGALDkklrEETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:COG2884   162 DEPTGNLD----PETSWEIMELLEEInrrGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 28-312 1.62e-73

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: 232.68  E-value: 1.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  28 NVTKKFGDFTAvdDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGI--PPYRRPVNMMF 101
Cdd:COG4148     6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIflPPHRRRIGYVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKQdgMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:COG4148    84 QEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 182 GALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDVNIFD 261
Cdd:COG4148   162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 262 GKVTS--AEDGYIRVETTGGiPVRMASPEKPgNGAKAAVAIRPEKIRIGRQPP 312
Cdd:COG4148   242 ATVAAhdPDYGLTRLALGGG-RLWVPRLDLP-PGTRVRVRIRARDVSLALEPP 292
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 24-253 2.92e-73

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: 227.77  E-value: 2.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY-----RRPVN 98
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFGLKQDG-MPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 178 DEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSrFVADF 253
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDP-LVRQF 235
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
38-251 1.02e-72

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 227.44  E-value: 1.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGiPPYRRPVnmMFQSYALFPHMTVENNVA 117
Cdd:COG4525    22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDNVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 118 FGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELM 197
Cdd:COG4525    99 FGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 198 DLQQELGLTFVVVTHDQEEAMTMADRIAVMSH--GKVVQVatpaeiYEAP-NSRFVA 251
Cdd:COG4525   179 DVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER------LELDfSRRFLA 229
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 24-233 1.05e-72

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 226.23  E-value: 1.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-----PYR 94
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSY--ALFPHMTVENNVAFGLK--QDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLA 169
Cdd:cd03257    82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 170 KRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 31-234 1.68e-72

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 225.25  E-value: 1.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  31 KKFGDFTAVDDLSLNiytREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL------AGIPPYRRPVNMMFQSY 104
Cdd:cd03297     8 KRLPDFTLKIDFDLN---EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQRKIGLVFQQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTVENNVAFGLKqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGAL 184
Cdd:cd03297    85 ALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371712025 185 DKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:cd03297   163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 18-245 6.55e-71

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 225.00  E-value: 6.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKF-----------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQS 86
Cdd:COG4608     2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  87 LAGIP-----PYRRPVNMMFQ-SYA-LFPHMTVENNVAFGLKQDGM-PKADIAERVAQMLKLVKLEK-FAKRKPHQLSGG 157
Cdd:COG4608    82 ITGLSgrelrPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 158 QRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQeeAMT--MADRIAVMSHGKVVQV 235
Cdd:COG4608   162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDL--SVVrhISDRVAVMYLGKIVEI 239

                         250
                  ....*....|
gi 1371712025 236 ATPAEIYEAP 245
Cdd:COG4608   240 APRDELYARP 249
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 24-232 9.17e-69

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: 215.47  E-value: 9.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG----IPPYRRPVNM 99
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:cd03262   161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 25-231 1.87e-68

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: 214.64  E-value: 1.87e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVNMM 100
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTklSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQsyalFP-HM----TVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVL 175
Cdd:cd03225    81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 176 LLDEPLGALDkklrEETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:cd03225   157 LLDEPTAGLD----PAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 21-245 8.75e-66

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 217.08  E-value: 8.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPT---SGEIILDGQSLAGIPPYRR 95
Cdd:COG1123     2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 P--VNMMFQS--YALFPhMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKR 171
Cdd:COG1123    82 GrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 172 PKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:COG1123   161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 24-245 2.96e-65

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: 210.29  E-value: 2.96e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP---TSGEIILDGQSLAGIPP---- 92
Cdd:COG0444     2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 -YR-RPVNMMFQ-SY-ALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKL---EKFAKRKPHQLSGGQRQRVAL 164
Cdd:COG0444    82 kIRgREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 165 ARSLAKRPKVLLLDEPLGALDK-------KLreetqfeLMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:COG0444   162 ARALALEPKLLIADEPTTALDVtiqaqilNL-------LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234


                  ....*...
gi 1371712025 238 PAEIYEAP 245
Cdd:COG0444   235 VEELFENP 242
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 24-242 4.40e-65

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: 208.46  E-value: 4.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-----DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG-----IPPY 93
Cdd:TIGR04521   1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQ--SYALFpHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:TIGR04521  81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 24-257 9.00e-65

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 209.66  E-value: 9.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YR 94
Cdd:PRK11153    2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK11153   82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKklrEETQ--FELM-DLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVA 251
Cdd:PRK11153  162 LLCDEATSALDP---ATTRsiLELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238


                  ....*.
gi 1371712025 252 DFIGDV 257
Cdd:PRK11153  239 EFIQST 244
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
24-257 9.55e-64

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 203.79  E-value: 9.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGIPPYRRPVNM 99
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFG-LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDV 257
Cdd:PRK09493  162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 24-242 1.16e-63

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: 204.20  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG---IPPYRRPVN 98
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSyalfPH-----MTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:TIGR04520  81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 174 VLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAmTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 39-248 1.23e-63

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: 203.08  E-value: 1.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVnmmFQSYALFPHMTVENNVAF 118
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---FQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 119 GLKQ--DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFEL 196
Cdd:TIGR01184  78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 197 MDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVatpAEIYEAPNSR 248
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANI---GQILEVPFPR 206
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 22-233 6.92e-63

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 201.82  E-value: 6.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YRR 95
Cdd:COG3638     1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTVENNV-------------AFGLkqdgMPKADIaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRV 162
Cdd:COG3638    81 RIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 163 ALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:COG3638   156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 24-241 1.28e-62

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 201.04  E-value: 1.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMF 101
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRreLARRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFG----LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:COG1120    82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 178 DEPLGALDkkLReeTQFELMDLQQEL----GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG1120   162 DEPTSHLD--LA--HQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 24-241 6.02e-62

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: 198.82  E-value: 6.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP---VNMM 100
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNV----------AFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:cd03219    81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 171 RPKVLLLDEPLGALDkklREETQfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03219   161 DPKLLLLDEPAAGLN---PEETE-ELAELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 24-241 2.09e-61

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


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 197.02  E-value: 2.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF-----EQPTSGEIILDGQSLAGIPP----YR 94
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVdvleLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPhMTVENNVAFGLKQDGM-PKADIAERVAQMLKLVKLEKFAKRKPH--QLSGGQRQRVALARSLAKR 171
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 172 PKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 24-243 2.30e-61

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: 197.39  E-value: 2.30e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQ 102
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:COG4555    82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 183 ALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:COG4555   162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 24-232 1.59e-60

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 196.05  E-value: 1.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIildgqsLAGIPPY---RRPVNMM 100
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLaeaREDTRLM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKAdiaervAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:PRK11247   87 FQDARLLPWKKVIDNVGLGLKGQWRDAA------LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 181 LGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK11247  161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
21-243 2.17e-60

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 196.39  E-value: 2.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPPYRRP 96
Cdd:PRK13635    3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDVRRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 VNMMFQSY-ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVL 175
Cdd:PRK13635   83 VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 176 LLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK13635  163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
24-232 7.72e-60

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 192.34  E-value: 7.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMF 101
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPhMTVENNVAFGLKQDGmpKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:COG4619    81 QEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 181 LGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:COG4619   158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 43-235 1.25e-58

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: 189.69  E-value: 1.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  43 SLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQ 122
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 123 DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQE 202
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371712025 203 LGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQV 235
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 41-233 4.75e-58

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: 188.09  E-value: 4.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNVAFGL 120
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 121 KQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQ 200
Cdd:cd03298    96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371712025 201 QELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03298   176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 24-231 1.32e-57

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 186.69  E-value: 1.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA-----GIPPYRRPV 97
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 178 DEPLGALDKKLREetqfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:TIGR02673 162 DEPTGNLDPDLSE----RILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
43-233 4.90e-57

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 185.94  E-value: 4.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  43 SLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQ 122
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 123 DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQE 202
Cdd:PRK10771   99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1371712025 203 LGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK10771  179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 24-244 5.08e-57

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: 186.23  E-value: 5.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YRRPV 97
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFG-LKQ--------DGMPKADIaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSL 168
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGrLGRrstwrslfGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 24-232 5.20e-57

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: 183.75  E-value: 5.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQ 102
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVafglkqdgmpkadiaervaqmlklvklekfakrkphQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371712025 183 ALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 24-241 5.68e-57

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: 185.40  E-value: 5.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD--FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY-RRPVNMM 100
Cdd:cd03263     1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAF--GLKqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03263    81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 179 EPLGALDKKLREetqfELMDLQQEL--GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03263   159 EPTSGLDPASRR----AIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
24-306 5.73e-57

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 191.01  E-value: 5.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------YRRPV 97
Cdd:PRK10070   29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK10070  109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 178 DEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVADFIGDV 257
Cdd:PRK10070  189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1371712025 258 NIfdGKVTSAEDgyIRVETTGGIPVRmaspeKPGNGAKAAVAIRPEKIR 306
Cdd:PRK10070  269 DI--SQVFSAKD--IARRTPNGLIRK-----TPGFGPRSALKLLQDEDR 308
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 18-240 1.14e-56

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 184.94  E-value: 1.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL------ 87
Cdd:COG4181     3 SSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalded 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 --AGIppYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKAdiAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALA 165
Cdd:COG4181    83 arARL--RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAmTMADRIAVMSHGKVVQVATPAE 240
Cdd:COG4181   159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
24-234 1.40e-56

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 185.67  E-value: 1.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGiPPYRRPVnmMFQS 103
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 184 LDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMS--HGKVVQ 234
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 26-224 3.25e-56

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: 182.82  E-value: 3.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  26 VKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------YRRPVNM 99
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371712025 180 PLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAmTMADRI 224
Cdd:TIGR03608 161 PTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHDPEVA-KQADRV 203
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 25-217 5.39e-56

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 182.68  E-value: 5.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP---TSGEIILDGQSLAGIPPYRRPVNMMF 101
Cdd:COG4136     3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKqDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:COG4136    83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371712025 182 GALDKKLREETQFELMDLQQELGLTFVVVTHDQEEA 217
Cdd:COG4136   162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 24-232 1.47e-55

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: 181.45  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG-----IPPYRRPV 97
Cdd:cd03292     1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 178 DEPLGALDKklreETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:cd03292   161 DEPTGNLDP----DTTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 16-245 1.90e-55

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: 190.28  E-value: 1.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  16 ADPASKPFISVKNVTKKF-----------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPTSGEIILDG 84
Cdd:COG4172   268 VPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDG 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  85 QSLAGIP-----PYRRPVNMMFQS-YA-LFPHMTVENNVAFGLK--QDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQL 154
Cdd:COG4172   347 QDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLdPAARHRYPHEF 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 155 SGGQRQRVALARSLAKRPKVLLLDEPLGALDKKlreeTQFE----LMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHG 230
Cdd:COG4172   427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVS----VQAQildlLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502

                         250
                  ....*....|....*
gi 1371712025 231 KVVQVATPAEIYEAP 245
Cdd:COG4172   503 KVVEQGPTEQVFDAP 517
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 19-244 2.84e-55

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 181.83  E-value: 2.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP------P 92
Cdd:COG1121     2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRPVNmmfqsyALFPhMTVENNVAFGLKQD----GMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSL 168
Cdd:COG1121    82 QRAEVD------WDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 169 AKRPKVLLLDEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMS-----HGKVVQVATPAE 240
Cdd:COG1121   155 AQDPDLLLLDEPFAGVDAA----TEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNrglvaHGPPEEVLTPEN 230


                  ....
gi 1371712025 241 IYEA 244
Cdd:COG1121   231 LSRA 234
cbiO PRK13637
energy-coupling factor transporter ATPase;
24-242 6.61e-54

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 179.86  E-value: 6.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-----AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG----IPPYR 94
Cdd:PRK13637    3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvkLSDIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQ--SYALFPHmTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL--EKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:PRK13637   83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13637  162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 16-254 6.82e-54

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 178.69  E-value: 6.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  16 ADPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRML-------AGFEqpTSGEIILDGQSL- 87
Cdd:COG1117     4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEDIy 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 -AGIPPY--RRPVNMMFQSYALFPhMTVENNVAFGLKQDGM-PKADIAERVAQMLKLV--------KLEKFAkrkpHQLS 155
Cdd:COG1117    82 dPDVDVVelRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAalwdevkdRLKKSA----LGLS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 156 GGQRQRVALARSLAKRPKVLLLDEPLGALD----KKLrEETqfeLMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:COG1117   157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-EEL---ILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGE 230

                         250       260
                  ....*....|....*....|...
gi 1371712025 232 VVQVATPAEIYEAPNSRFVADFI 254
Cdd:COG1117   231 LVEFGPTEQIFTNPKDKRTEDYI 253
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 24-244 1.86e-53

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: 188.12  E-value: 1.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNM 99
Cdd:COG2274   474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIGV 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFpHMTVENNVAFglkqdGMPKADIaERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSL 168
Cdd:COG2274   554 VLQDVFLF-SGTIRENITL-----GDPDATD-EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 169 AKRPKVLLLDEPLGALDkklrEETQFELMD-LQQEL-GLTFVVVTHDqEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:COG2274   627 LRNPRILILDEATSALD----AETEAIILEnLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
24-254 2.40e-53

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 176.74  E-value: 2.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--------AGIPPYRR 95
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpseKAIRLLRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTV-ENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVmENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQeLGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATpAEIYEAPNSRFVADFI 254
Cdd:COG4161   163 LLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 25-233 7.71e-53

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: 173.39  E-value: 7.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPyrrpvnmmfqsy 104
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 alfphmtvennvafglkqdgmpkADIAERVA---QMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:cd03214    69 -----------------------KELARKIAyvpQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 182 GALDKKlreeTQFELMD----LQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03214   126 SHLDIA----HQIELLEllrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 24-241 8.41e-53

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: 174.87  E-value: 8.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-PYRRPVNMMFQ 102
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:cd03265    81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03265   161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 28-312 1.82e-52

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: 178.00  E-value: 1.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  28 NVTKKFGDFTAvdDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGI--PPYRRPVNMMF 101
Cdd:TIGR02142   4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIflPPEKRRIGYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKqdgmpKADIAERV---AQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:TIGR02142  82 QEARLFPHLSVRGNLRYGMK-----RARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVAdFIGDVN 258
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGS 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 259 IFDGKVTSAEDGY--IRVETTGGipvRMASPEKPGN-GAKAAVAIRPEKIRIGRQPP 312
Cdd:TIGR02142 236 LIEGVVAEHDQHYglTALRLGGG---HLWVPENLGPtGARLRLRVPARDVSLALQKP 289
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 24-254 2.32e-51

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 171.74  E-value: 2.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--------AGIPPYRR 95
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsdKAIRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTV-ENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVqQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKklreETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATpAEIYEAPNSRFVA 251
Cdd:PRK11124  163 LLFDEPTAALDP----EITAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237


                  ...
gi 1371712025 252 DFI 254
Cdd:PRK11124  238 NYL 240
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 38-245 7.63e-51

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 172.84  E-value: 7.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YRRPVNMMFQS-YA-LFPHM 110
Cdd:PRK11308   30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsLNPRK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 111 TVENNVAFGLK-QDGMPKADIAERVAQMLKLVKLE-KFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:PRK11308  110 KVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 189 REETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK11308  190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 24-244 3.05e-50

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: 168.63  E-value: 3.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG-----IPPYRRPV 97
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNV-------------AFGLkqdgMPKADIaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVAL 164
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVlhgrlgykptwrsLLGR----FSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 165 ARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
cbiO PRK13650
energy-coupling factor transporter ATPase;
24-242 3.79e-50

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 169.91  E-value: 3.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG---DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVN 98
Cdd:PRK13650    5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSY-ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK13650   85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 178 DEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEaMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13650  165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
24-246 7.25e-50

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 168.37  E-value: 7.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY----RRPVnm 99
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRAV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYAL-FPhMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLA-------KR 171
Cdd:COG4559    80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 172 PKVLLLDEPLGALDkkLREetQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:COG4559   159 PRWLFLDEPTSALD--LAH--QHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 19-245 1.11e-49

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: 174.87  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKS----TLLRMLAGFEQPTSGEIILDGQSLAGI 90
Cdd:COG4172     2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  91 PPYR------RPVNMMFQ--SYALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKL---EKFAKRKPHQLSGGQ 158
Cdd:COG4172    82 SERElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALDKKLREETqFELM-DLQQELGLTFVVVTHDqeeaMT----MADRIAVMSHGKVV 233
Cdd:COG4172   162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQI-LDLLkDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIV 236

                         250
                  ....*....|..
gi 1371712025 234 QVATPAEIYEAP 245
Cdd:COG4172   237 EQGPTAELFAAP 248
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 39-180 3.68e-49

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 162.82  E-value: 3.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG--IPPYRRPVNMMFQSYALFPHMTVENNV 116
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 117 AFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 13-244 5.71e-49

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: 173.41  E-value: 5.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASkpfISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP 91
Cdd:COG4988   329 LPAAGPPS---IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 P--YRRPVNMMFQSYALFpHMTVENNVAFglkqdGMPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQ 158
Cdd:COG4988   406 PasWRRQIAWVPQNPYLF-AGTIRENLRL-----GRPDASDEE-LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQ 478

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALDkklrEETQFELMDLQQEL--GLTFVVVTHDqEEAMTMADRIAVMSHGKVVQVA 236
Cdd:COG4988   479 AQRLALARALLRDAPLLLLDEPTAHLD----AETEAEILQALRRLakGRTVILITHR-LALLAQADRILVLDDGRIVEQG 553


                  ....*...
gi 1371712025 237 TPAEIYEA 244
Cdd:COG4988   554 THEELLAK 561
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 24-233 9.26e-49

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: 164.06  E-value: 9.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF--GDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP--- 96
Cdd:TIGR02211   2 LKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 ---VNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:TIGR02211  82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 174 VLLLDEPLGALDKKlREETQFELM-DLQQELGLTFVVVTHDQEEAMTMaDRIAVMSHGKVV 233
Cdd:TIGR02211 162 LVLADEPTGNLDNN-NAKIIFDLMlELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 25-231 3.73e-48

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 160.49  E-value: 3.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMFQ 102
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 syalfphmtvennvafglkqdgmpkadiaervaqmlklvklekfakrkphqLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:cd00267    81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371712025 183 ALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 17-243 4.09e-48

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 164.01  E-value: 4.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  17 DPASKPFISVKNVTKKFGDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPP 92
Cdd:PRK13632    1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRPVNMMFQSY-ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKR 171
Cdd:PRK13632   81 IRKKIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 172 PKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAmTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK13632  161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 25-232 4.21e-48

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 162.32  E-value: 4.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIppyRRPVNMMFQSY 104
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 AL---FPhMTVENNVAFGLKQD----GMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:cd03235    78 SIdrdFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 178 DEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:cd03235   157 DEPFAGVDPK----TQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
22-248 4.36e-48

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 164.09  E-value: 4.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKF---------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----- 87
Cdd:PRK10419    2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 AGIPPYRRPVNMMFQSY--ALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVA 163
Cdd:PRK10419   82 AQRKAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV--QVATPAEI 241
Cdd:PRK10419  162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVetQPVGDKLT 241


                  ....*..
gi 1371712025 242 YEAPNSR 248
Cdd:PRK10419  242 FSSPAGR 248
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 22-217 4.89e-48

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: 161.88  E-value: 4.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMM 100
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADiaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:COG4133    81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371712025 181 LGALDKKLREETQfELMDLQQELGLTFVVVTHDQEEA 217
Cdd:COG4133   159 FTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL 194
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 24-241 2.48e-47

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: 160.68  E-value: 2.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP---VNMM 100
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKqdGMPKADIAERVAQMLKLV-KLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 180 PLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
18-254 5.47e-47

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 160.74  E-value: 5.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP---YR 94
Cdd:COG4598     3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVN------------MMFQSYALFPHMTVENNVAFG-LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQR 161
Cdd:COG4598    83 VPADrrqlqrirtrlgMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 162 VALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG4598   163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241

                         250
                  ....*....|...
gi 1371712025 242 YEAPNSRFVADFI 254
Cdd:COG4598   242 FGNPKSERLRQFL 254
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 38-246 9.38e-47

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 161.34  E-value: 9.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG------IPPYRRPVNMMFQsyalFP-HM 110
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLRKKVGIVFQ----FPeHQ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 111 ----TVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALD 185
Cdd:PRK13634   98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 186 KKLREetqfELMD----LQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK13634  178 PKGRK----EMMEmfykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 24-234 9.92e-47

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: 158.51  E-value: 9.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIyTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQ 102
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQkLRRRIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 183 ALDKKLREetqfELMDLQQELGLTFVVV--THDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:cd03264   160 GLDPEERI----RFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVF 209
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 19-245 1.25e-46

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 159.77  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY---RR 95
Cdd:PRK11300    1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiaRM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTV-EN-----------NVAFGL-KQDGMPKA--DIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQ 160
Cdd:PRK11300   81 GVVRTFQHVRLFREMTViENllvaqhqqlktGLFSGLlKTPAFRRAesEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 161 RVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:PRK11300  161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240


                  ....*
gi 1371712025 241 IYEAP 245
Cdd:PRK11300  241 IRNNP 245
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 24-233 1.60e-46

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: 157.76  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQS 103
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKadiaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03268    81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 184 LD----KKLREetqfELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03268   157 LDpdgiKELRE----LILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 24-231 1.65e-46

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 156.77  E-value: 1.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT--AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNM 99
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFpHMTVENNVafglkqdgmpkadiaervaqmlklvklekfakrkphqLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 180 PLGALDKklreETQFELMDLQQEL--GLTFVVVTHDqEEAMTMADRIAVMSHGK 231
Cdd:cd03228   123 ATSALDP----ETEALILEALRALakGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 22-240 2.30e-46

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 159.17  E-value: 2.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY----RRPV 97
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRRAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 nmMFQSYAL-FPhMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLA------K 170
Cdd:PRK13548   81 --LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 171 RPKVLLLDEPLGALDkkLREetQFELMDLQQEL----GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:PRK13548  158 PPRWLLLDEPTSALD--LAH--QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 24-234 1.02e-45

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: 157.66  E-value: 1.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF---------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-- 92
Cdd:TIGR02769   3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 ---YRRPVNMMFQ-SYALF-PHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLE-KFAKRKPHQLSGGQRQRVALA 165
Cdd:TIGR02769  83 rraFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 24-233 1.07e-45

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: 154.12  E-value: 1.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQslagippyrrPVNmmFQS 103
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----------EVS--FAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 yalfphmtvennvafglkqdgmPKADIAERVAqmlkLVklekfakrkpHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03216    69 ----------------------PRDARRAGIA----MV----------YQLSVGERQMVEIARALARNARLLILDEPTAA 112

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 184 LDKKlreETQ--FELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03216   113 LTPA---EVErlFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 24-245 1.86e-45

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: 164.17  E-value: 1.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNM 99
Cdd:COG4987   334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRRIAV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFpHMTVENNVAFGLkqdgmPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSL 168
Cdd:COG4987   414 VPQRPHLF-DTTLRENLRLAR-----PDATDEE-LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 169 AKRPKVLLLDEPLGALDkklrEETQFELM-DLQQEL-GLTFVVVTHDqEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:COG4987   487 LRDAPILLLDEPTEGLD----AATEQALLaDLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 19-244 9.37e-45

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 160.96  E-value: 9.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----------A 88
Cdd:COG3845     1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprdaiaL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  89 GIppyrrpvNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLvkLEKF-----AKRKPHQLSGGQRQRVA 163
Cdd:COG3845    81 GI-------GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIREL--SERYgldvdPDAKVEDLSVGEQQRVE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDkklREETQfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:COG3845   152 ILKALYRGARILILDEPTAVLT---PQEAD-ELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227


                  ....
gi 1371712025 241 IYEA 244
Cdd:COG3845   228 TSEE 231
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
24-242 1.19e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 155.25  E-value: 1.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD------FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDG---QSLAGIPPYR 94
Cdd:PRK13633    5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSyalfPH-----MTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLA 169
Cdd:PRK13633   85 NKAGMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 170 KRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 24-279 1.45e-44

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 155.65  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYR-------Rp 96
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 vnmmfqsyALFPHMTVENNVAF--GLKqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:COG4152    81 --------GLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALD----KKLREetqfELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA-PNSRF 249
Cdd:COG4152   151 LILDEPFSGLDpvnvELLKD----VIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTL 225

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1371712025 250 VADFIGDV----NIFDGKVTSAEDGYIRVETTGG 279
Cdd:COG4152   226 RLEADGDAgwlrALPGVTVVEEDGDGAELKLEDG 259
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 24-233 6.90e-44

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: 151.28  E-value: 6.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAgiPPYRRPVNMMFQS 103
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTV-ENNVAFG-LKqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:cd03269    79 RGLYPKMKViDQLVYLAqLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 182 GALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03269   157 SGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 21-243 7.60e-44

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: 159.20  E-value: 7.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKF-----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIL------------- 82
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpg 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  83 -DGQSLAgippyRRPVNMMFQSYALFPHMTVENNV--AFGLKqdgMPKADIAERVAQMLKLVKL-EKFAK----RKPHQL 154
Cdd:TIGR03269 357 pDGRGRA-----KRYIGILHQEYDLYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFdEEKAEeildKYPDEL 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 155 SGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508


                  ....*....
gi 1371712025 235 VATPAEIYE 243
Cdd:TIGR03269 509 IGDPEEIVE 517
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 24-256 7.84e-44

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 152.21  E-value: 7.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSG-----EIILD-----GQSLAGIPPY 93
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDtarslSQQKGLIRQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQSYALFPHMTVENNVAFG-LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRP 172
Cdd:PRK11264   84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 173 KVLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNS----R 248
Cdd:PRK11264  164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtrQ 242


                  ....*...
gi 1371712025 249 FVADFIGD 256
Cdd:PRK11264  243 FLEKFLLQ 250
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 22-241 2.32e-43

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: 150.52  E-value: 2.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRR------ 95
Cdd:COG0410     2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgig 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 --PvnmmfQSYALFPHMTVENNVAFGLKQdGMPKADIAERVAQMLKLV-KLEKFAKRKPHQLSGGQRQRVALARSLAKRP 172
Cdd:COG0410    82 yvP-----EGRRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 173 KVLLLDEP-LGaLDKKLREETqFE-LMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG0410   156 KLLLLDEPsLG-LAPLIVEEI-FEiIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 24-248 4.24e-43

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 149.62  E-value: 4.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP---VNMM 100
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 181 LGALDKKLREETQFELMDLqQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSR 248
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-241 1.01e-42

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 155.56  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP---YRRP 96
Cdd:COG1129     1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 VNMMFQSYALFPHMTVENNVAFG--LKQDG-MPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:COG1129    81 IAIIHQELNLVPNLSVAENIFLGrePRRGGlIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 174 VLLLDEPLGALDkklREETQ--FELM-DLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG1129   161 VLILDEPTASLT---EREVErlFRIIrRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 24-248 1.53e-42

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 148.64  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRR-------- 95
Cdd:COG1137     4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigyl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PvnmmfQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVL 175
Cdd:COG1137    84 P-----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 176 LLDEPLGALDKKLREETQFELMDLQQE-LGltfVVVT-HDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSR 248
Cdd:COG1137   159 LLDEPFAGVDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 38-245 1.64e-42

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 151.40  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-----YRRPVNMMFQS--YALFPHM 110
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewraVRSDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 111 TVENNVAFGLK--QDGMPKADIAERV-AQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:PRK15079  116 TIGEIIAEPLRtyHPKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 188 LREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK15079  196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
24-240 1.69e-42

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 156.09  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTkkF---GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVN 98
Cdd:COG1132   340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIG 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFpHMTVENNVAFGLkqdgmPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARS 167
Cdd:COG1132   418 VVPQDTFLF-SGTIRENIRYGR-----PDATDEE-VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 168 LAKRPKVLLLDEPLGALD--------KKLREETQfelmdlqqelGLTFVVVTH------DqeeamtmADRIAVMSHGKVV 233
Cdd:COG1132   491 LLKDPPILILDEATSALDtetealiqEALERLMK----------GRTTIVIAHrlstirN-------ADRILVLDDGRIV 553


                  ....*..
gi 1371712025 234 QVATPAE 240
Cdd:COG1132   554 EQGTHEE 560
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
20-237 7.43e-42

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 146.50  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGD---FTAV-DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--- 92
Cdd:PRK11629    2 NKILLQCDNLCKRYQEgsvQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaak 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 ---YRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLA 169
Cdd:PRK11629   82 aelRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 170 KRPKVLLLDEPLGALDKKlREETQFELM-DLQQELGLTFVVVTHDQEEAMTMaDRIAVMSHGKVVQVAT 237
Cdd:PRK11629  162 NNPRLVLADEPTGNLDAR-NADSIFQLLgELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 24-246 8.49e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 147.92  E-value: 8.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGIPPYRRPVN 98
Cdd:PRK13639    2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSY--ALFPHmTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLL 176
Cdd:PRK13639   82 IVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 177 LDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK13639  161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 24-241 2.07e-41

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 146.00  E-value: 2.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMF 101
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGL----KqdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:COG4604    82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 178 DEPLGALD--------KKLReetqfelmDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG4604   160 DEPLNNLDmkhsvqmmKLLR--------RLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 24-242 1.47e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 144.61  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQ----SLAGIPPYRRPVN 98
Cdd:PRK13636    6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidySRKGLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQS--YALFPhMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLL 176
Cdd:PRK13636   86 MVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 177 LDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13636  165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
24-241 3.16e-40

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 142.85  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPyrrpvNMMFQS 103
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFP--HMT-----VENNVAFG----LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRP 172
Cdd:PRK11231   78 LALLPqhHLTpegitVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 173 KVLLLDEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:PRK11231  158 PVVLLDEPTTYLDIN----HQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
17-244 7.89e-40

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 143.41  E-value: 7.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  17 DPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY-RR 95
Cdd:PRK13537    1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHaRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTV-ENNVAFGlKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK13537   81 RVGVVPQFDNLDPDFTVrENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 24-233 2.24e-39

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 139.81  E-value: 2.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-PYRRPVN 98
Cdd:cd03266     2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 179 EPLGALDkKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03266   162 EPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 25-251 2.66e-39

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: 139.58  E-value: 2.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRR--------P 96
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragiayvP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 vnmmfQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLvkLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLL 176
Cdd:TIGR03410  82 -----QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 177 LDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVA 251
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-244 2.67e-39

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 149.12  E-value: 2.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  16 ADPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL-AGIPPYR 94
Cdd:NF033858  259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIATR 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:NF033858  339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 175 LLLDEPLGALDKKLREetQF-ELM-DLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:NF033858  419 LILDEPTSGVDPVARD--MFwRLLiELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 25-233 2.70e-39

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 138.93  E-value: 2.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRpVNMMFQS 103
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 --YALFPHmTVENNVAFGLKqdgmPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:cd03226    80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 182 GALDKKLREETQfELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03226   155 SGLDYKNMERVG-ELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 20-243 5.18e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 140.27  E-value: 5.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKF-GD--FTaVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEII-----LDGQSLAGIp 91
Cdd:PRK13648    4 KNSIIVFKNVSFQYqSDasFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 pyRRPVNMMFQS-YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:PRK13648   82 --RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 171 RPKVLLLDEPLGALDKKLREetqfELMDL----QQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK13648  160 NPSVIILDEATSMLDPDARQ----NLLDLvrkvKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 24-245 6.94e-39

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 139.59  E-value: 6.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF-----EQPTSGEIILDGQSLAG--IPP--YR 94
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPieVR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFGLKQDGM--PKADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRVALARSL 168
Cdd:PRK14267   85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 169 AKRPKVLLLDEPLGALD----KKLrEETQFELMDlqqelGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:PRK14267  165 AMKPKILLMDEPTANIDpvgtAKI-EELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238


                  .
gi 1371712025 245 P 245
Cdd:PRK14267  239 P 239
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
24-264 1.39e-38

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 139.13  E-value: 1.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQ-----SLAGIPPYRRPVN 98
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamSRSRLYTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK11831   88 MLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 178 DEP--------LGALDKKLREetqfelmdLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRf 249
Cdd:PRK11831  168 DEPfvgqdpitMGVLVKLISE--------LNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR- 238

                         250
                  ....*....|....*
gi 1371712025 250 VADFIGdvNIFDGKV 264
Cdd:PRK11831  239 VRQFLD--GIADGPV 251
cbiO PRK13645
energy-coupling factor transporter ATPase;
35-242 1.53e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 139.76  E-value: 1.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  35 DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIL-DGQSLAGIPP------YRRPVNMMFQ--SYA 105
Cdd:PRK13645   23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKikevkrLRKEIGLVFQfpEYQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 106 LFPHmTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGAL 184
Cdd:PRK13645  103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 185 DKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13645  182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 24-233 1.92e-38

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 138.68  E-value: 1.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-----DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVN 98
Cdd:COG1101     2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 M--MFQSYAL--FPHMTVENNVA--------FGLKQdGMPKADIA---ERVAQmLKLvKLEKFAKRKPHQLSGGQRQRVA 163
Cdd:COG1101    82 IgrVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRRElfrELLAT-LGL-GLENRLDTKVGLLSGGQRQALS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKlreeTQFELMDLQQEL----GLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:COG1101   159 LLMATLTKPKLLLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 23-233 5.26e-38

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: 144.62  E-value: 5.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  23 FISVKNVTKKF-GDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY--RRPVN 98
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIG 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFpHMTVENNVAFGlkqdgMPKADiAERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARS 167
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG-----APYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 168 LAKRPKVLLLDEPLGALDKklREETQFeLMDLQQEL-GLTFVVVTHDQeEAMTMADRIAVMSHGKVV 233
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDN--RSEERF-KDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIV 678
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
28-233 8.47e-38

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 139.24  E-value: 8.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  28 NVTKKFGDFTAVDDLSLNiyTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGI--PPYRRPVNMMF 101
Cdd:PRK11144    5 NFKQQLGDLCLTVNLTLP--AQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGIclPPEKRRIGYVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKqdgmpkadiAERVAQMLKLVKL---EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK11144   83 QDARLFPHYKVRGNLRYGMA---------KSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 179 EPLGALD---KKlreetqfELMD----LQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK11144  154 EPLASLDlprKR-------ELLPylerLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 24-233 1.07e-37

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 135.41  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD--FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY--RRPVNM 99
Cdd:cd03245     3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFpHMTVENNVAFglkqdGMPKADiAERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSL 168
Cdd:cd03245    83 VPQDVTLF-YGTLRDNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 169 AKRPKVLLLDEPLGALDkklrEETQFELMD-LQQEL-GLTFVVVTHDQeEAMTMADRIAVMSHGKVV 233
Cdd:cd03245   156 LNDPPILLLDEPTSAMD----MNSEERLKErLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
cbiO PRK13642
energy-coupling factor transporter ATPase;
24-242 1.17e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 136.76  E-value: 1.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF---GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG--IPPYRRPVN 98
Cdd:PRK13642    5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSY-ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK13642   85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 178 DEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13642  165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 34-246 1.27e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 136.86  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  34 GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPPYRRPVNMMFQSY--ALFPh 109
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFVGLVFQNPddQIFS- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 110 MTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLR 189
Cdd:PRK13652   94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 190 EETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK13652  174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
cbiO PRK13649
energy-coupling factor transporter ATPase;
24-243 2.96e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 136.03  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-----AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG------IPP 92
Cdd:PRK13649    3 INLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRPVNMMFQsyalFPHM-----TVENNVAFGLKQDGMPKADiAERVA-QMLKLVKL-EKFAKRKPHQLSGGQRQRVALA 165
Cdd:PRK13649   83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEE-AEALArEKLALVGIsESLFEKNPFELSGGQMRRVAIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKLREetqfELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13649  158 GILAMEPKILVLDEPTAGLDPKGRK----ELMTLFKKLhqsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233


                  .
gi 1371712025 243 E 243
Cdd:PRK13649  234 Q 234
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 24-254 4.05e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 134.66  E-value: 4.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF-----EQPTSGEIILDGQSLAGIP--PYRRP 96
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDviELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 VNMMFQSYALFPHMTVENNVAFGLKQDGM--PKADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRVALARSLAK 170
Cdd:PRK14247   84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFV 250
Cdd:PRK14247  164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241


                  ....
gi 1371712025 251 ADFI 254
Cdd:PRK14247  242 EKYV 245
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 40-243 5.92e-37

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: 133.82  E-value: 5.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  40 DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMFQSYALFPhMTVENNVA 117
Cdd:cd03249    20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTIAENIR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 118 FGLkqdgmPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLLDEPLGALDK 186
Cdd:cd03249    99 YGK-----PDATDEE-VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 187 KLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:cd03249   173 ESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 20-254 7.36e-37

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 134.13  E-value: 7.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF-----EQPTSGEIILDGQSLAGipP-- 92
Cdd:PRK14239    2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS--Prt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 ----YRRPVNMMFQSYALFPhMTVENNVAFGLKQDGMP-KADIAERVAQMLKLVKLEKFAKRKPHQ----LSGGQRQRVA 163
Cdd:PRK14239   80 dtvdLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALD----KKLrEETQFELMDlqqelGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPA 239
Cdd:PRK14239  159 IARVLATSPKIILLDEPTSALDpisaGKI-EETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232

                         250
                  ....*....|....*
gi 1371712025 240 EIYEAPNSRFVADFI 254
Cdd:PRK14239  233 QMFMNPKHKETEDYI 247
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
24-254 7.86e-37

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 134.33  E-value: 7.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP----------- 92
Cdd:PRK10619    6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 ----YRRPVNMMFQSYALFPHMTVENNVAFGLKQD-GMPKADIAERVAQMLKLVKLEKFAKRK-PHQLSGGQRQRVALAR 166
Cdd:PRK10619   86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIAR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 167 SLAKRPKVLLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK10619  166 ALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244


                  ....*...
gi 1371712025 247 SRFVADFI 254
Cdd:PRK10619  245 SPRLQQFL 252
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 19-261 8.46e-37

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 140.76  E-value: 8.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKF----GDFT-------AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL 87
Cdd:PRK10261  309 DGEPILQVRNLVTRFplrsGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 AGIPPY-----RRPVNMMFQS-YA-LFPHMTVENNVAFGLKQDGMPKADIA-ERVAQMLKLVKLE-KFAKRKPHQLSGGQ 158
Cdd:PRK10261  389 DTLSPGklqalRRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLLpEHAWRYPHEFSGGQ 468

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATP 238
Cdd:PRK10261  469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548

                         250       260
                  ....*....|....*....|...
gi 1371712025 239 AEIYEAPNSRFVADFIGDVNIFD 261
Cdd:PRK10261  549 RAVFENPQHPYTRKLMAAVPVAD 571
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
24-256 9.77e-37

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 134.15  E-value: 9.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDF-----TAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA-GIPPY 93
Cdd:PRK15112    5 LEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 R-RPVNMMFQ--SYALFPHMTVENNVAFGLKQD-GMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSL 168
Cdd:PRK15112   85 RsQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVThdQEEAMT--MADRIAVMSHGKVVQVATPAEIYEAP- 245
Cdd:PRK15112  165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLASPl 242

                         250
                  ....*....|....
gi 1371712025 246 ---NSRFVADFIGD 256
Cdd:PRK15112  243 helTKRLIAGHFGE 256
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 24-244 1.07e-36

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 133.28  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----------------------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEII 81
Cdd:COG1134     5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  82 LDGQ--SLAGippyrrpVNMMFQsyalfPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQR 159
Cdd:COG1134    85 VNGRvsALLE-------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 160 QRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPA 239
Cdd:COG1134   153 ARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231


                  ....*
gi 1371712025 240 EIYEA 244
Cdd:COG1134   232 EVIAA 236
cbiO PRK13640
energy-coupling factor transporter ATPase;
24-245 1.67e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 133.77  E-value: 1.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDF--TAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGE---IILDGQSLAG--IPPYRRP 96
Cdd:PRK13640    6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAktVWDIREK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 VNMMFQSY-ALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVL 175
Cdd:PRK13640   86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 176 LLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAmTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK13640  166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 24-244 1.78e-36

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 132.35  E-value: 1.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD--FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYRRPVNM 99
Cdd:cd03251     1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFpHMTVENNVAFGLkqdgmPKADiAERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSL 168
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAYGR-----PGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:cd03251   154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 22-233 5.35e-36

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 131.75  E-value: 5.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSG-EIILDGQSLAG--IPPYRRpvN 98
Cdd:COG1119     2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGedVWELRK--R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALF----PHMTVENNVA------FGLKQDgmPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSL 168
Cdd:COG1119    80 IGLVSPALQlrfpRDETVLDVVLsgffdsIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREetQF-ELMD-LQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:COG1119   158 VKDPELLILDEPTAGLDLGARE--LLlALLDkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 24-233 7.54e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 132.17  E-value: 7.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPPYRRPVNMM 100
Cdd:PRK13647    5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaENEKWVRSKVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSY--ALFPhMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK13647   85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 179 EPLGALDKKlREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK13647  164 EPMAYLDPR-GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 24-243 9.64e-36

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: 136.86  E-value: 9.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQ--PTSGEII-----------LDGQSLAGI 90
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyVERPSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  91 P--------------------PYRRPVN----MMFQ-SYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEK 145
Cdd:TIGR03269  81 PcpvcggtlepeevdfwnlsdKLRRRIRkriaIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 146 FAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIA 225
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250
                  ....*....|....*...
gi 1371712025 226 VMSHGKVVQVATPAEIYE 243
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 38-247 9.87e-36

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: 130.57  E-value: 9.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP----TSGEIILDGQSLAGIPPYRRPVNMMFQS--YALFPHMT 111
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 112 VENNVAFGLKQDGMPKADIAERVAQMLKLVKL---EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 189 REETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNS 247
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 13-227 5.34e-35

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: 134.72  E-value: 5.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASkpfISVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP 91
Cdd:TIGR02857 314 VTAAPASS---LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 P--YRRPVNMMFQSYALFPHmTVENNVAFGLkqdgmPKADIAErVAQMLKLVKLEKFAKRKP-----------HQLSGGQ 158
Cdd:TIGR02857 391 AdsWRDQIAWVPQHPFLFAG-TIAENIRLAR-----PDASDAE-IREALERAGLDEFVAALPqgldtpigeggAGLSGGQ 463

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALDkklrEETQFELMDLQQEL--GLTFVVVTHDqEEAMTMADRIAVM 227
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
cbiO PRK13644
energy-coupling factor transporter ATPase;
24-250 6.31e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 129.72  E-value: 6.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFT-AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEII---LDGQSLAGIPPYRRPVNM 99
Cdd:PRK13644    2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQS-YALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK13644   82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 179 EPLGALDKKlREETQFELMDLQQELGLTFVVVTHDQEEaMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFV 250
Cdd:PRK13644  162 EVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 22-254 9.72e-35

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 128.62  E-value: 9.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF-----EQPTSGEIILDGQSL----AGIPP 92
Cdd:PRK14258    6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyerrVNLNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRPVNMMFQSYALFPhMTVENNVAFGLKQDGM-PKADIAERVAQMLKLVKLEKFAKRKPHQ----LSGGQRQRVALARS 167
Cdd:PRK14258   86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 168 LAKRPKVLLLDEPLGALD--KKLREETQFELMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSH-----GKVVQVATPAE 240
Cdd:PRK14258  165 LAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSE--LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242

                         250
                  ....*....|....
gi 1371712025 241 IYEAPNSRFVADFI 254
Cdd:PRK14258  243 IFNSPHDSRTREYV 256
cbiO PRK13641
energy-coupling factor transporter ATPase;
39-246 1.01e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 129.18  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA------GIPPYRRPVNMMFQsyalFPHM-- 110
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 111 ---TVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDK 186
Cdd:PRK13641   99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 187 KLREEtQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK13641  179 EGRKE-MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 24-254 1.36e-34

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 128.36  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLR-------MLAGFEqpTSGEIILDGQSL--AGIPP-- 92
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPDVDPve 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRPVNMMFQSYALFPHmTVENNVAFGLKQDGMpKADIAERVAQMLKLVKLEKFAKRKPHQ----LSGGQRQRVALARSL 168
Cdd:PRK14243   89 VRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 169 AKRPKVLLLDEPLGALD--KKLREEtqfELMdlqQELG--LTFVVVTHDQEEAMTMADRIAVMS---------HGKVVQV 235
Cdd:PRK14243  167 AVQPEVILMDEPCSALDpiSTLRIE---ELM---HELKeqYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEF 240

                         250
                  ....*....|....*....
gi 1371712025 236 ATPAEIYEAPNSRFVADFI 254
Cdd:PRK14243  241 DRTEKIFNSPQQQATRDYV 259
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 20-237 3.34e-34

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 126.37  E-value: 3.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPV 97
Cdd:PRK10247    4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHmTVENNVAFGL---KQDGMPKADIAERVAQMLKLVKLEKfakrKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK10247   84 SYCAQTPTLFGD-TVYDNLIFPWqirNQQPDPAIFLDDLERFALPDTILTK----NIAELSGGEKQRISLIRNLQFMPKV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:PRK10247  159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEAR 221
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 24-269 4.97e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 127.89  E-value: 4.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-----DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIL---------------- 82
Cdd:PRK13651    3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekek 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  83 ----------DGQSLAGIPPYRRPVNMMFQ--SYALFpHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKR 149
Cdd:PRK13651   83 vleklviqktRFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 150 KPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSH 229
Cdd:PRK13651  162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 230 GKVVQVATPAEIYEapNSRFVAD----------FIG---DVNIFDGKVTSAED 269
Cdd:PRK13651  241 GKIIKDGDTYDILS--DNKFLIEnnmeppkllnFVNkleKKGIDVPKVTSIEE 291
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 24-245 7.38e-34

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: 132.77  E-value: 7.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAV--DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG--IPPYRRPVNM 99
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLilDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRRQLGV 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHmTVENNVAfGLKQDGMpkaDIAERVAQMlklVKLEKFAKRKP---H--------QLSGGQRQRVALARSL 168
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIA-GGAPLTL---DEAWEAARM---AGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARAL 603

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 169 AKRPKVLLLDEPLGALDKklreETQFELMDLQQELGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:TIGR03797 604 VRKPRILLFDEATSALDN----RTQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 24-217 1.10e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 124.89  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-------FTAVDdlsLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP 96
Cdd:PRK10584    7 VEVHHLKKSVGQgehelsiLTGVE---LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 ------VNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:PRK10584   84 klrakhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEA 217
Cdd:PRK10584  164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 24-233 1.49e-33

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


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 124.18  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----------------------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEII 81
Cdd:cd03220     1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  82 LDGqslagippyrRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQR 161
Cdd:cd03220    81 VRG----------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 162 VALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03220   151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
40-233 2.03e-33

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 131.38  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  40 DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------YRRPVNMMFQSYALFPHMTVE 113
Cdd:PRK10535   25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLTAA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 114 NNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQ 193
Cdd:PRK10535  105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1371712025 194 FELMDLQQElGLTFVVVTHDQEEAmTMADRIAVMSHGKVV 233
Cdd:PRK10535  185 AILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
24-233 2.37e-33

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 123.83  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA-----GIPPYRRPV 97
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK10908   82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 178 DEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK10908  162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 24-242 2.91e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 126.12  E-value: 2.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-----FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEI----ILDGQSLAGIPPY- 93
Cdd:PRK13631   22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELIt 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 -------------RRPVNMMFQ--SYALFPHmTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGG 157
Cdd:PRK13631  102 npyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 158 QRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:PRK13631  181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259


                  ....*
gi 1371712025 238 PAEIY 242
Cdd:PRK13631  260 PYEIF 264
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 24-232 5.63e-33

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 121.17  E-value: 5.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTA--VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNM 99
Cdd:cd03246     1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPhmtvennvafglkqdgmpkADIAERVaqmlklvklekfakrkphqLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:cd03246    81 LPQDDELFS-------------------GSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 180 PLGALDkklrEETQFELMDLQQEL---GLTFVVVTHdQEEAMTMADRIAVMSHGKV 232
Cdd:cd03246   123 PNSHLD----VEGERALNQAIAALkaaGATRIVIAH-RPETLASADRILVLEDGRV 173
cbiO PRK13643
energy-coupling factor transporter ATPase;
38-243 8.55e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 124.08  E-value: 8.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEI------ILDGQSLAGIPPYRRPVNMMFQsyalFPHM- 110
Cdd:PRK13643   21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIKPVRKKVGVVFQ----FPESq 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 111 ----TVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEK-FAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALD 185
Cdd:PRK13643   97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 186 KKLREEtQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK13643  177 PKARIE-MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 24-244 2.00e-32

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: 127.91  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG--DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYRRPVNM 99
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYtlASLRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHmTVENNVAFGlKQDGMPKADIaERVAQMlklVKLEKFAKRKP---HQ--------LSGGQRQRVALARSL 168
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEI-ERALAA---AYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARAL 484

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
24-243 4.26e-32

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 123.40  E-value: 4.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEI-ILDGQSLAGIPPYRRPVNMMFQ 102
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTV-ENNVAFGlKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:PRK13536  122 FDNLDLEFTVrENLLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 182 GALDKKLREETQFELMDLQQeLGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK13536  201 TGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
cbiO PRK13646
energy-coupling factor transporter ATPase;
35-242 4.76e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 122.20  E-value: 4.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  35 DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG------IPPYRRPVNMMFQsyalFP 108
Cdd:PRK13646   19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 109 HM-----TVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEK-FAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:PRK13646   95 ESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13646  175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 19-257 5.79e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 121.74  E-value: 5.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSG-----EIILDGQSLAG---I 90
Cdd:PRK14271   17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNyrdV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  91 PPYRRPVNMMFQSYALFPhMTVENNVAFGLKQDGM-PKADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRVALA 165
Cdd:PRK14271   97 LEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK14271  176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253

                         250
                  ....*....|....*.
gi 1371712025 246 ----NSRFVADFIGDV 257
Cdd:PRK14271  254 khaeTARYVAGLSGDV 269
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 38-241 7.07e-32

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: 120.28  E-value: 7.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMFQSYALFpHMTVENN 115
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQENVLF-NRSIRDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 116 VAfgLKQDGMPKadiaERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLLDEPLGAL 184
Cdd:cd03252    96 IA--LADPGMSM----ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 185 DKKLREETQFELMDLQQelGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEI 241
Cdd:cd03252   170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 18-234 1.58e-31

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 120.03  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQS-----LAGIPP 92
Cdd:PRK11701    1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 YRRpvNMMFQSYALFphmtVENNVAFGLKQDGMPKADIAERV---------------AQMLKLVKLEkfAKR---KPHQL 154
Cdd:PRK11701   81 AER--RRLLRTEWGF----VHQHPRDGLRMQVSAGGNIGERLmavgarhygdirataGDWLERVEID--AARiddLPTTF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 155 SGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLreetQFELMD----LQQELGLTFVVVTHDQEEAMTMADRIAVMSHG 230
Cdd:PRK11701  153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV----QARLLDllrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228


                  ....
gi 1371712025 231 KVVQ 234
Cdd:PRK11701  229 RVVE 232
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 19-254 1.71e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 119.77  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKF---GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL-------- 87
Cdd:PRK14246    3 AGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 AGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMP-KADIAERVAQMLKLVKLEKFAKRK----PHQLSGGQRQRV 162
Cdd:PRK14246   83 IDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 163 ALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK14246  163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240

                         250
                  ....*....|..
gi 1371712025 243 EAPNSRFVADFI 254
Cdd:PRK14246  241 TSPKNELTEKYV 252
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
33-227 2.03e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 117.72  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  33 FGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNmmfqsyALFPhMTV 112
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 113 ENNVAFGLKQD----GMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1371712025 189 REETQfELMDLQQELGLTFVVVTHDQEEAMTmADRIAVM 227
Cdd:NF040873  155 RERII-ALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 24-249 2.57e-31

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: 118.87  E-value: 2.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYRRPVNMM 100
Cdd:cd03253     1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFpHMTVENNVAFglkqdGMPKADiAERVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARSLA 169
Cdd:cd03253    81 PQDTVLF-NDTIGYNIRY-----GRPDAT-DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 170 KRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYeAPNSRF 249
Cdd:cd03253   154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL-AKGGLY 229
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
32-242 7.69e-31

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 118.57  E-value: 7.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  32 KFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----AGIPPYRRPVNMMFQ--SYA 105
Cdd:PRK13638   10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRQQVATVFQdpEQQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 106 LFpHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALD 185
Cdd:PRK13638   90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 186 KKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIY 242
Cdd:PRK13638  169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 29-233 8.56e-31

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: 117.43  E-value: 8.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  29 VTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIildgqSLAGIPPYRRPVN-------MMF 101
Cdd:cd03267    27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRRKKflrrigvVFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:cd03267   102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 182 GALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03267   182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 21-232 9.26e-31

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: 115.61  E-value: 9.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKfgdfTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMM 100
Cdd:cd03215     2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 F------QSYALFPHMTVENNVAFglkqdgmpkadiaervaqmlklvklekfakrkPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:cd03215    78 AyvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRV 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:cd03215   126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 14-249 9.82e-31

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 122.89  E-value: 9.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  14 PWADPASkPFISVKNVTKKF-----------GDFTAVDDLSLNIYTREFFALLGASGCGKST----LLRMLAgfeqpTSG 78
Cdd:PRK15134  267 PLPEPAS-PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQG 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  79 EIILDGQSLAGIP-----PYRRPVNMMFQ--SYALFPHMTVENNVAFGLK--QDGMPKADIAERVAQMLKLVKLEKFAK- 148
Cdd:PRK15134  341 EIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRh 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 149 RKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMS 228
Cdd:PRK15134  421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500

                         250       260
                  ....*....|....*....|.
gi 1371712025 229 HGKVVQVATPAEIYEAPNSRF 249
Cdd:PRK15134  501 QGEVVEQGDCERVFAAPQQEY 521
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 19-245 1.27e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 122.51  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKS-TLLRMLAGFEQP----TSGEIILDGQSL-- 87
Cdd:PRK15134    1 MTQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 AGIPPYRR----PVNMMFQS--YALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKLEKFAKR---KPHQLSGG 157
Cdd:PRK15134   81 ASEQTLRGvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 158 QRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:PRK15134  161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240


                  ....*...
gi 1371712025 238 PAEIYEAP 245
Cdd:PRK15134  241 AATLFSAP 248
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 22-303 1.82e-30

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 120.33  E-value: 1.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYR--RPVNM 99
Cdd:PRK09536    2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVENNVAFGL-----KQDGMPKADIAErVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK09536   82 VPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 175 LLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRFVAD-- 252
Cdd:PRK09536  161 LLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDar 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 253 -FIGD--------VNIFDGKVTSAEDGYIRVETTG-GIPVRMASPEKPGNGAKAAVAIRPE 303
Cdd:PRK09536  240 tAVGTdpatgaptVTPLPDPDRTEAAADTRVHVVGgGQPAARAVSRLVAAGASVSVGPVPE 300
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 50-244 2.21e-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: 116.10  E-value: 2.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  50 EFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAgipPYRRPVNMMFQSYAL---FPhMTVENNVAFGlkQDGM- 125
Cdd:TIGR03771   7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFP-ISVAHTVMSG--RTGHi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 126 -----PKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKlreeTQFELMDLQ 200
Cdd:TIGR03771  81 gwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP----TQELLTELF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1371712025 201 QEL---GLTFVVVTHDQEEAMTMADRIaVMSHGKVVQVATPAEIYEA 244
Cdd:TIGR03771 157 IELagaGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDP 202
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 23-240 4.23e-30

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: 115.40  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  23 FISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP--PYRRPVNM 99
Cdd:cd03254     2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHmTVENNVAFglkqdGMPKADiAERVAQMLKLVKLEKFAKRKP-----------HQLSGGQRQRVALARSL 168
Cdd:cd03254    82 VLQDTFLFSG-TIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAM 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:cd03254   155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
21-233 5.23e-30

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 120.66  E-value: 5.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP---YRRPV 97
Cdd:PRK09700    3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGL----KQDGMPKADIAE---RVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK 170
Cdd:PRK09700   83 GIIYQELSVIDELTVLENLYIGRhltkKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 171 RPKVLLLDEPLGALDKKlREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK09700  163 DAKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 24-282 9.18e-30

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 116.73  E-value: 9.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----------GDF-----------TAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIil 82
Cdd:COG4586     2 IEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  83 dgqSLAGIPPYRRPVN-------MMFQSYALFPHMTVENNvaFGLKQD--GMPKADIAERVAQMLKLVKLEKFAKRKPHQ 153
Cdd:COG4586    80 ---RVLGYVPFKRRKEfarrigvVFGQRSQLWWDLPAIDS--FRLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRPKVLLLDEP-LGaLD----KKLREetqFeLMDLQQELGLTFVVVTHDQEEAMTMADRIAVMS 228
Cdd:COG4586   155 LSLGQRMRCELAAALLHRPKILFLDEPtIG-LDvvskEAIRE---F-LKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 229 HGKVV---QVATPAEIYeAPNSRFVADFIGDVNIFD----GKVTSAEDGYIRVETTGGIPV 282
Cdd:COG4586   230 HGRIIydgSLEELKERF-GPYKTIVLELAEPVPPLElprgGEVIEREGNRVRLEVDPRESL 289
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 13-245 2.22e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 115.98  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASKPFISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKS----TLLRMLAGfEQPTSGEIILDG 84
Cdd:PRK09473    2 VPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  85 QSLAGIPPYR------RPVNMMFQS--YALFPHMTVENNVAFGLKQ-DGMPKADIAERVAQMLKLVKLEKFAKRK---PH 152
Cdd:PRK09473   81 REILNLPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 153 QLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK09473  161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240

                         250
                  ....*....|...
gi 1371712025 233 VQVATPAEIYEAP 245
Cdd:PRK09473  241 MEYGNARDVFYQP 253
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 39-245 4.22e-29

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: 118.89  E-value: 4.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYR--RPVNMMFQSYALFpHMTVENNV 116
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAMVDQDIFLF-EGTVRDNL 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 117 AfgLKQDGMPKADI--AERVAQMLKLVKLEKFAKRKP-----HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKklr 189
Cdd:TIGR03796 574 T--LWDPTIPDADLvrACKDAAIHDVITSRPGGYDAElaeggANLSGGQRQRLEIARALVRNPSILILDEATSALDP--- 648

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 190 eETQFELMDLQQELGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:TIGR03796 649 -ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
17-245 6.46e-29

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 112.96  E-value: 6.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  17 DPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYR 94
Cdd:PRK10575    5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFPHMTVENNVAFG-------LKQDGmpkADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARS 167
Cdd:PRK10575   85 RKVAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFG---AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 168 LAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK10575  162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
24-232 2.26e-28

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 111.64  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF---EQPTSGEIILDGQS------LAG-IPPY 93
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTvqregrLARdIRKS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQSYALFPHMTVENNVAFG-LKQDGMPKADIA-------ERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALA 165
Cdd:PRK09984   85 RANTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTCFSwftreqkQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK09984  165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-233 2.52e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 115.93  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   6 GSIRRSFAPwADPASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILdGQ 85
Cdd:COG0488   299 KTVEIRFPP-PERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  86 SLAgippyrrpvnmmfQSY------ALFPHMTVENNVafglkQDGMPKADIAErVAQMlklvkLEKF------AKRKPHQ 153
Cdd:COG0488   377 TVK-------------IGYfdqhqeELDPDKTVLDEL-----RDGAPGGTEQE-VRGY-----LGRFlfsgddAFKPVGV 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREetqfELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:COG0488   433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE----ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 21-245 5.66e-28

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: 110.31  E-value: 5.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPV--- 97
Cdd:TIGR02323   1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEaer 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 -NMMFQSYALfphmtVENNVAFGLKQDGMPKADIAERV-------------AQMLKLVKLEKFAKR---KPHQLSGGQRQ 160
Cdd:TIGR02323  81 rRLMRTEWGF-----VHQNPRDGLRMRVSAGANIGERLmaigarhygniraTAQDWLEEVEIDPTRiddLPRAFSGGMQQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 161 RVALARSLAKRPKVLLLDEPLGALDKKLreetQFELMDLQQ----ELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVA 236
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSV----QARLLDLLRglvrDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231


                  ....*....
gi 1371712025 237 TPAEIYEAP 245
Cdd:TIGR02323 232 LTDQVLDDP 240
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 18-233 6.18e-28

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 114.92  E-value: 6.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTkkFG----DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-- 91
Cdd:PRK11160  333 AADQVSLTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSea 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 PYRRPVNMMFQSYALFPHmTVENNVAFGLkqdgmPKADiAERVAQMLKLVKLEKFAKRKP----------HQLSGGQRQR 161
Cdd:PRK11160  411 ALRQAISVVSQRVHLFSA-TLRDNLLLAA-----PNAS-DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRR 483

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 162 VALARSLAKRPKVLLLDEPLGALDKklreETQFELMDLQQEL--GLTFVVVTHdQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK11160  484 LGIARALLHDAPLLLLDEPTEGLDA----ETERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQII 552
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 41-245 8.09e-28

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 115.20  E-value: 8.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMFQSYALFPHmTVENNVAF 118
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhyLHRQVALVGQEPVLFSG-SVRENIAY 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 119 GLKQDGMpkadiaERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:TIGR00958 578 GLTDTPD------EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 188 LrEETQFELMDLQqelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:TIGR00958 652 C-EQLLQESRSRA---SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
27-244 8.69e-28

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 110.08  E-value: 8.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  27 KNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDG---QSLAGIPPYRRpVNMMFQS 103
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASKEVARR-IGLLAQN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGlKQDGMP-----KADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:PRK10253   90 ATTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 179 EPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:PRK10253  169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 24-230 1.33e-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: 108.68  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-----GD--FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQS----LAGIPP 92
Cdd:COG4778     5 LEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 Y-----RRPVnMMFQSYAL--FPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQLSGGQRQRVAL 164
Cdd:COG4778    85 ReilalRRRT-IGYVSQFLrvIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 165 ARSLAKRPKVLLLDEPLGALDKKLREetqfELMDLQQEL---GLTFVVVTHDqEEAM-TMADRIAVMSHG 230
Cdd:COG4778   164 ARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEAkarGTAIIGIFHD-EEVReAVADRVVDVTPF 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 26-232 1.87e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 113.24  E-value: 1.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  26 VKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILD-GQSLAGIPpyrrpvnmmfQSY 104
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTVENNVAFGLK--------------QDGMPKADIAE------------------RVAQMLKLVKL-EKFAKRKP 151
Cdd:COG0488    71 PLDDDLTVLDTVLDGDAelraleaeleeleaKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFpEEDLDRPV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 152 HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDkklreetqfelMD----LQQEL----GlTFVVVTHDQE--EAmtMA 221
Cdd:COG0488   151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-----------LEsiewLEEFLknypG-TVLVVSHDRYflDR--VA 216

                         250
                  ....*....|.
gi 1371712025 222 DRIAVMSHGKV 232
Cdd:COG0488   217 TRILELDRGKL 227
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
21-233 2.00e-27

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 108.43  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP---YRRPV 97
Cdd:PRK11614    3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYALFPHMTVENNVAFGlkqdGM--PKADIAERVAQMLKLV-KLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK11614   83 AIVPEGRRVFSRMTVEENLAMG----GFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 175 LLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK11614  159 LLLDEPSLGLAPIIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-241 2.07e-27

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 112.80  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   1 MMksLG-SIRRSFAPWADPASKPFISVKNVTKKfgdfTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGE 79
Cdd:COG1129   235 LM--VGrELEDLFPKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  80 IILDGQSL----------AGI---PPYRRpvnmmfqSYALFPHMTVENNVA---------FGLkqdgMPKADIAERVAQM 137
Cdd:COG1129   309 IRLDGKPVrirsprdairAGIayvPEDRK-------GEGLVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEY 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 138 LKLVKLekfakrKPH-------QLSGGQRQRVALARSLAKRPKVLLLDEP-----LGAldKklreetqFELMDLQQEL-- 203
Cdd:COG1129   378 IKRLRI------KTPspeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPtrgidVGA--K-------AEIYRLIRELaa 442

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1371712025 204 -GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:COG1129   443 eGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 24-245 4.90e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 109.45  E-value: 4.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD----FTAVDDLSLNIYTREFFALLGASGCGKS--TLLRM-LAGFEQPTSGE-IILDGQSLAGIPPYRR 95
Cdd:PRK11022    4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSLAIMgLIDYPGRVMAEkLEFNGQDLQRISEKER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 ------PVNMMFQS--YALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKLEKFAKR---KPHQLSGGQRQRVA 163
Cdd:PRK11022   84 rnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK11022  164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243


                  ..
gi 1371712025 244 AP 245
Cdd:PRK11022  244 AP 245
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 16-241 7.77e-27

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: 112.14  E-value: 7.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  16 ADPASKPFISVKNVTKKFGDFTAV--DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP- 92
Cdd:TIGR01846 448 ALPELRGAITFENIRFRYAPDSPEvlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPa 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 -YRRPVNMMFQSYALFPHmTVENNVAfgLKQDGMPKadiaERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQ 160
Cdd:TIGR01846 528 wLRRQMGVVLQENVLFSR-SIRDNIA--LCNPGAPF----EHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQ 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 161 RVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:TIGR01846 601 RIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEE 677


                  .
gi 1371712025 241 I 241
Cdd:TIGR01846 678 L 678
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 18-244 2.70e-26

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: 110.22  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRR 95
Cdd:COG4618   325 PRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 -------PvnmmfQSYALFPHmTVENNVAfglkqdGMPKADiAERVAQMLKLVKLEKFAKRKP-----------HQLSGG 157
Cdd:COG4618   405 grhigylP-----QDVELFDG-TIAENIA------RFGDAD-PEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGG 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 158 QRQRVALARSLAKRPKVLLLDEPLGALD----KKLREetqfELMDLQQElGLTFVVVTHDQeEAMTMADRIAVMSHGKVV 233
Cdd:COG4618   472 QRQRIGLARALYGDPRLVVLDEPNSNLDdegeAALAA----AIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQ 545

                         250
                  ....*....|.
gi 1371712025 234 QVATPAEIYEA 244
Cdd:COG4618   546 AFGPRDEVLAR 556
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 24-233 3.72e-26

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: 103.16  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG--DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRP-VNMM 100
Cdd:cd03247     1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFpHMTVENNVAfglkqdgmpkadiaervaqmlklvklekfakrkpHQLSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:cd03247    81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 181 LGALDKKlreeTQFELMDL--QQELGLTFVVVTHdQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03247   126 TVGLDPI----TERQLLSLifEVLKDKTLIWITH-HLTGIEHMDKILFLENGKII 175
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 8-238 5.49e-26

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 110.10  E-value: 5.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025    8 IRRSFAPWADPASKPFISVKNVTKKFGDF--TAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQ 85
Cdd:TIGR01257  913 INDSFFERELPGLVPGVCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK 992

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   86 SL-AGIPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVAL 164
Cdd:TIGR01257  993 DIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025  165 ARSLAKRPKVLLLDEPLGALDKKLREETqFELMdLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATP 238
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSI-WDLL-LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 42-246 6.86e-26

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 109.16  E-value: 6.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  42 LSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPTSGEIILDGQSLAGIPP--YRRPVNMMFQSYALFpHMTVENNVAFG 119
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNVLLG 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 120 lkqdgmpKADIA-ERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKk 187
Cdd:PRK11174  447 -------NPDASdEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA- 518

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 188 lREEtQFELMDLQQE-LGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK11174  519 -HSE-QLVMQALNAAsRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 13-213 7.44e-26

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 108.60  E-value: 7.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASKPFISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP 91
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 --PYRRPVNMMFQSYALFpHMTVENNVAFglkqdGMPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQ 158
Cdd:TIGR02868 404 qdEVRRRVSVCAQDAHLF-DTTVRENLRL-----ARPDATDEE-LWAALERVGLADWLRALPDgldtvlgeggaRLSGGE 476

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALDKKLREETqfeLMDLQQEL-GLTFVVVTHD 213
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 40-233 9.73e-26

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: 108.75  E-value: 9.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  40 DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNMMFQSYALFpHMTVENNVA 117
Cdd:COG5265   375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAIGIVPQDTVLF-NDTIAYNIA 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 118 FGlkqdgMPKADIAErVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKVLLLDEPLGALDK 186
Cdd:COG5265   454 YG-----RPDASEEE-VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 187 KLREETQFELMDLQQelGLTFVVVTH------DqeeamtmADRIAVMSHGKVV 233
Cdd:COG5265   528 RTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIV 571
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 41-232 1.06e-25

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 103.32  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSlagIPPY-----RRPVNMMFQSYALFPHmTVENN 115
Cdd:cd03248    32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYehkylHSKVSLVGQEPVLFAR-SLQDN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 116 VAFGLKQDGMPKADIAERVAQMLKLV-KLEKF----AKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLRE 190
Cdd:cd03248   108 IAYGLQSCSFECVKEAAQKAHAHSFIsELASGydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1371712025 191 ETQFELMDLQQElgLTFVVVTHdQEEAMTMADRIAVMSHGKV 232
Cdd:cd03248   188 QVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 24-231 1.36e-25

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: 100.60  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgqslagippyrrpvnmmfqS 103
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------S 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMtvennvafglkqdgmpkadiaervaqmlklvklekfakrkpHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:cd03221    62 TVKIGYF-----------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371712025 184 LDkklrEETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:cd03221   101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 24-241 2.08e-25

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 103.05  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY---RRPVNMM 100
Cdd:PRK10895    4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDE 179
Cdd:PRK10895   84 PQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 180 PLGALD-------KKLREETqfelmdlqQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:PRK10895  164 PFAGVDpisvidiKRIIEHL--------RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 24-212 2.63e-25

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 107.20  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTA-VDDLSLNIYTREffALL--GASGCGKSTLLRMLAGFEQPTSGEIILdgqslagiPPYRRpvnMM 100
Cdd:COG4178   363 LALEDLTLRTPDGRPlLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VL 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 F---QSYalFPHMTVENNVAFGLKQDGMPKADIAErvaqMLKLVKLEKFAKR------KPHQLSGGQRQRVALARSLAKR 171
Cdd:COG4178   430 FlpqRPY--LPLGTLREALLYPATAEAFSDAELRE----ALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHK 503

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1371712025 172 PKVLLLDEPLGALDkklrEETQFELMD-LQQEL-GLTFVVVTH 212
Cdd:COG4178   504 PDWLFLDEATSALD----EENEAALYQlLREELpGTTVISVGH 542
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 24-233 3.42e-25

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: 101.09  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKK------FGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAG--FEQPTSGEIILDGQSLaGIPPYRR 95
Cdd:cd03213     4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL-DKRSFRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTVENNVAFGLKqdgmpkadiaervaqmLKlvklekfakrkphQLSGGQRQRVALARSLAKRPKVL 175
Cdd:cd03213    83 IIGYVPQDDILHPTLTVRETLMFAAK----------------LR-------------GLSGGERKRVSIALELVSNPSLL 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 176 LLDEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHD-QEEAMTMADRIAVMSHGKVV 233
Cdd:cd03213   134 FLDEPTSGLDSS----SALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 19-233 3.57e-25

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 106.67  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP------ 92
Cdd:PRK15439    7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakahql 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  93 --YRRPvnmmfQSYALFPHMTVENNVAFGLkqdgmPK-ADIAERVAQMLKLVKlekfAKRKPHQLSG----GQRQRVALA 165
Cdd:PRK15439   87 giYLVP-----QEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALG----CQLDLDSSAGslevADRQIVEIL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 166 RSLAKRPKVLLLDEPLGALdKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK15439  153 RGLMRDSRILILDEPTASL-TPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 20-231 5.01e-25

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 106.17  E-value: 5.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPT---SGEIILDGQSL--------- 87
Cdd:PRK13549    2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqasnirdte 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 -AGIPpyrrpvnMMFQSYALFPHMTVENNVAFG--LKQDG-MPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVA 163
Cdd:PRK13549   81 rAGIA-------IIHQELALVKELSVLENIFLGneITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKlreETQFeLMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:PRK13549  154 IAKALNKQARLLILDEPTASLTES---ETAV-LLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGR 220
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 24-234 9.48e-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: 105.98  E-value: 9.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY--RRPVNMM 100
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHmTVENNVAFGLKqdgmPKADIaERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLA 169
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK----ENVSQ-DEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALL 627

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 170 KRPKVLLLDEPLGALDKKLREETQFELMDLQQElglTFVVVTHDQEEAmTMADRIAVMSHGKVVQ 234
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIE 688
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
40-187 1.49e-24

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 99.49  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  40 DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRpvNMMF---QSyALFPHMTVENN 115
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQ--DLLYlghQP-GIKTELTALEN 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 116 VAFGLKQDGMPKADiaeRVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:PRK13538   95 LRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 24-245 1.72e-24

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 105.32  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKS-TLLRMLAGFEQpTSGE---------------IILD 83
Cdd:PRK10261   13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLvqcdkmllrrrsrqvIELS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  84 GQSLAGIPPYR-RPVNMMFQS--YALFPHMTVENNVAFGLK-QDGMPKADIAERVAQMLKLVKL---EKFAKRKPHQLSG 156
Cdd:PRK10261   92 EQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 157 GQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVA 236
Cdd:PRK10261  172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251


                  ....*....
gi 1371712025 237 TPAEIYEAP 245
Cdd:PRK10261  252 SVEQIFHAP 260
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
24-244 4.80e-24

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 103.64  E-value: 4.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAV-DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP--PYRRPVNMM 100
Cdd:PRK10790  341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHmTVENNVAFGlkqdgmpkADIAE-RVAQMLKLVKLEKFAKRKP-----------HQLSGGQRQRVALARSL 168
Cdd:PRK10790  421 QQDPVVLAD-TFLANVTLG--------RDISEeQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVL 491

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025 169 AKRPKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEA 244
Cdd:PRK10790  492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 39-248 5.34e-24

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 99.39  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKS----TLLRML-AGFEQpTSGEIILDGQSLAGIPPYRRPVNMMFQS--YALFPHMT 111
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 112 VENNVAFGLKQDGMPKADiaERVAQMLKLVKLE---KFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:PRK10418   98 MHTHARETCLALGKPADD--ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 189 REETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSR 248
Cdd:PRK10418  176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-255 5.84e-24

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 103.07  E-value: 5.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----------AG 89
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  90 IPpyrrpvnMMFQSYALFPHMTVENNVAFG-LKQDG--MPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALAR 166
Cdd:PRK11288   81 VA-------IIYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 167 SLAKRPKVLLLDEPLGALDKklREETQfeLMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKvvQVATPAEIYE 243
Cdd:PRK11288  154 ALARNARVIAFDEPTSSLSA--REIEQ--LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQ 227

                         250
                  ....*....|..
gi 1371712025 244 APNSRFVADFIG 255
Cdd:PRK11288  228 VDRDQLVQAMVG 239
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 24-237 7.44e-24

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 102.60  E-value: 7.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGF--EQPTSGEIILDGQSL--AGIPPYRRP-VN 98
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERAgIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHMTVENNVAFG----LKQDGMPKADIAERVAQMLKLVKLEKFAKRKP-HQLSGGQRQRVALARSLAKRPK 173
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 174 VLLLDEPLGALDkklREETQFeLMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKvvQVAT 237
Cdd:TIGR02633 162 LLILDEPSSSLT---EKETEI-LLDIIRDLkahGVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 24-187 9.41e-24

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 97.43  E-value: 9.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA-GIPPYRRPVNMMFQ 102
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeQRDEPHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFgLKQDGMPKADIAErvaQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:TIGR01189  81 LPGLKPELSALENLHF-WAAIHGGAQRTIE---DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156


                  ....*
gi 1371712025 183 ALDKK 187
Cdd:TIGR01189 157 ALDKA 161
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 18-241 1.61e-23

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 101.64  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVT-KKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY-RR 95
Cdd:COG3845   252 EPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPReRR 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMF-----QSYALFPHMTVENNVAFGlKQDGMPKA-----DIAERVAQMLKLVklEKFAKRKPH------QLSGGQR 159
Cdd:COG3845   332 RLGVAYipedrLGRGLVPDMSVAENLILG-RYRRPPFSrggflDRKAIRAFAEELI--EEFDVRTPGpdtparSLSGGNQ 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 160 QRVALARSLAKRPKVLLLDEP-----LGAldkklREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:COG3845   409 QKVILARELSRDPKLLIAAQPtrgldVGA-----IEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVG 482


                  ....*..
gi 1371712025 235 VATPAEI 241
Cdd:COG3845   483 EVPAAEA 489
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 41-233 3.05e-23

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 96.57  E-value: 3.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP---TSGEIILDGQSLAgIPPYRRPVNMMFQSYALFPHMTVENNVA 117
Cdd:cd03234    25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK-PDQFQKCVAYVRQDDILLPGLTVRETLT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 118 FGLK---QDGMPKADIAERVAQM-LKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKlreeTQ 193
Cdd:cd03234   104 YTAIlrlPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF----TA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1371712025 194 FELMDLQQELGLT--FVVVTHDQ--EEAMTMADRIAVMSHGKVV 233
Cdd:cd03234   180 LNLVSTLSQLARRnrIVILTIHQprSDLFRLFDRILLLSSGEIV 223
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 54-245 3.39e-23

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 97.22  E-value: 3.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  54 LLGASGCGKSTLLRMLAGFeQPTSGEIILDGQSLAGIPP-----YR-------RPVNMM--FQSYALfpHMtvennvafg 119
Cdd:COG4138    27 LIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarHRaylsqqqSPPFAMpvFQYLAL--HQ--------- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 120 lkQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK-------RPKVLLLDEPL--------GAL 184
Cdd:COG4138    95 --PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMnsldvaqqAAL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 185 DKKLREETQfelmdlqqeLGLTFVVVTHDQEEAMTMADRIAVMSHGKVV------QVATP---AEIYEAP 245
Cdd:COG4138   173 DRLLRELCQ---------QGITVVMSSHDLNHTLRHADRVWLLKQGKLVasgetaEVMTPenlSEVFGVK 233
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 24-231 3.44e-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: 96.00  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVT-----KKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGqSLAGIPpyrrpvn 98
Cdd:cd03250     1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVS------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 mmfQSYALFPhMTVENNVAFGLKQDgmpkadiAERVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARS 167
Cdd:cd03250    73 ---QEPWIQN-GTIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 168 LAKRPKVLLLDEPLGALDkklrEETQFELMD--LQQEL--GLTFVVVTHdQEEAMTMADRIAVMSHGK 231
Cdd:cd03250   142 VYSDADIYLLDDPLSAVD----AHVGRHIFEncILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
24-243 3.75e-23

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 100.86  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTkkfgdFT-------AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG--IPPYR 94
Cdd:PRK11176  342 IEFRNVT-----FTypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLR 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNMMFQSYALFpHMTVENNVAFGlKQDGMPKADIaERVAQMLKLVKlekFAKRKPH-----------QLSGGQRQRVA 163
Cdd:PRK11176  417 NQVALVSQNVHLF-NDTIANNIAYA-RTEQYSREQI-EEAARMAYAMD---FINKMDNgldtvigengvLLSGGQRQRIA 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQElgLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYE 243
Cdd:PRK11176  491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLA 567
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 24-231 3.78e-23

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 100.82  E-value: 3.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD--FtAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP--YRRPVNM 99
Cdd:PRK10522  323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedYRKLFSA 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMtvennvafgLKQDGMPKADiaERVAQMLKLVKLEKFAKRKPH-----QLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK10522  402 VFTDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDI 470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 175 LLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDqEEAMTMADRIAVMSHGK 231
Cdd:PRK10522  471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 24-238 1.32e-22

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


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 94.87  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGD--FTAVDDLSLNIYTREFFALLGASGCGKST----LLRMLagfeQPTSGEIILDGQSLAGIPP--YRR 95
Cdd:cd03244     3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLhdLRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHmTVENNVA-FGLKQDgmpkadiaERVAQMLKLVKLEKFAKRKPHQL-----------SGGQRQRVA 163
Cdd:cd03244    79 RISIIPQDPVLFSG-TIRSNLDpFGEYSD--------EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKklreetqfELMDLQQEL------GLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:cd03244   150 LARALLRKSKILVLDEATASVDP--------ETDALIQKTireafkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDS 220


                  .
gi 1371712025 238 P 238
Cdd:cd03244   221 P 221
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 42-246 1.37e-22

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 95.38  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  42 LSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPTSGEIILDGQSLAGIPP-----YR-------RPVNMM--FQSYALF 107
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarHRaylsqqqTPPFAMpvFQYLTLH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 108 PHmtvennvafglkqDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALA-------RSLAKRPKVLLLDEP 180
Cdd:PRK03695   94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 181 L--------GALDKKLREETQfelmdlqqeLGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPN 246
Cdd:PRK03695  161 MnsldvaqqAALDRLLSELCQ---------QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 24-233 1.68e-22

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 93.75  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFE--QPTSGEIILDGQSLAGIPPY---RRPVN 98
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEeraRLGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPhmtvennvafGLKqdgmpkadiaerVAQMLKLVKlEKFakrkphqlSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03217    81 LAFQYPPEIP----------GVK------------NADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILD 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 179 EPLGALD-----------KKLREEtqfelmdlqqelGLTFVVVTHDQEEAMTM-ADRIAVMSHGKVV 233
Cdd:cd03217   130 EPDSGLDidalrlvaeviNKLREE------------GKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
24-251 3.36e-22

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 98.11  E-value: 3.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF-GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYRRPVNMM 100
Cdd:PRK13657  335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVtrASLRRNIAVV 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFpHMTVENNVafglkQDGMPKADIAErVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLA 169
Cdd:PRK13657  415 FQDAGLF-NRSIEDNI-----RVGRPDATDEE-MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALL 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 170 KRPKVLLLDEPLGALDKKLREETQFELMDLQQelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYeAPNSRF 249
Cdd:PRK13657  488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRF 563


                  ..
gi 1371712025 250 VA 251
Cdd:PRK13657  564 AA 565
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 12-232 3.79e-22

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: 97.80  E-value: 3.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  12 FAPWADPASKPFISVKNVT--KKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAG 89
Cdd:TIGR01842 305 DPAMPLPEPEGHLSVENVTivPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  90 IPP--YRRPVNMMFQSYALFPHmTVENNVA-FGLKQDgmpkadiAERVAQMLKLVKLEKFAKRKPH-----------QLS 155
Cdd:TIGR01842 385 WDRetFGKHIGYLPQDVELFPG-TVAENIArFGENAD-------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLS 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 156 GGQRQRVALARSLAKRPKVLLLDEPLGALDkklrEETQFELMDLQQEL---GLTFVVVTHdQEEAMTMADRIAVMSHGKV 232
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLD----EEGEQALANAIKALkarGITVVVITH-RPSLLGCVDKILVLQDGRI 531
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 22-229 9.58e-22

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 93.25  E-value: 9.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNmmf 101
Cdd:PRK09544    3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 qsyALFPhMTVENnvaFGLKQDGMPKADIAErvaqMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:PRK09544   80 ---TTLP-LTVNR---FLRLRPGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 182 GALDKKlreeTQFELMDL----QQELGLTFVVVTHDQEEAMTMADRIAVMSH 229
Cdd:PRK09544  149 QGVDVN----GQVALYDLidqlRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
hmuV PRK13547
heme ABC transporter ATP-binding protein;
39-241 6.94e-21

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 91.04  E-value: 6.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGfEQPTS---------GEIILDGQSLAGIPPYR----RPVnMMFQSYA 105
Cdd:PRK13547   17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRlarlRAV-LPQAAQP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 106 LFPhMTVENNVAFG----LKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAK---------RP 172
Cdd:PRK13547   95 AFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 173 KVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:PRK13547  174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 24-238 1.12e-20

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: 89.01  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFG-DFTAV-DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP--PYRRPVNM 99
Cdd:cd03369     7 IEVENLSVRYApDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHmTVENNV-AFGLKQDgmpkadiaERVAQMLKLvklekfaKRKPHQLSGGQRQRVALARSLAKRPKVLLLD 178
Cdd:cd03369    87 IPQDPTLFSG-TIRSNLdPFDEYSD--------EEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 179 EPLGALD--------KKLREETQfelmdlqqelGLTFVVVTHdqeEAMTMA--DRIAVMSHGKVVQVATP 238
Cdd:cd03369   151 EATASIDyatdaliqKTIREEFT----------NSTILTIAH---RLRTIIdyDKILVMDAGEVKEYDHP 207
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 25-238 4.64e-20

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 88.20  E-value: 4.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFE--QPTSGEIILDGQSLAGIPPY---RRPVNM 99
Cdd:COG0396     2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDeraRAGIFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYALFPHMTVEN--NVAFG-LKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQ-LSGGQRQRVALARSLAKRPKV 174
Cdd:COG0396    82 AFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 175 LLLDEPLGALD-----------KKLREEtqfelmdlqqelGLTFVVVTHDQE--EAMTmADRIAVMSHGKVVQVATP 238
Cdd:COG0396   162 AILDETDSGLDidalrivaegvNKLRSP------------DRGILIITHYQRilDYIK-PDFVHVLVDGRIVKSGGK 225
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 24-225 7.05e-20

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: 91.15  E-value: 7.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILdGQSlagippyrrpVNMMF-- 101
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET----------VKLAYvd 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSY-ALFPHMTVENNVAFGLKQDGMPKADIAERV---------AQMLKLVKlekfakrkphQLSGGQRQRVALARSLAKR 171
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKSG 461

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 172 PKVLLLDEPLGALDKklreETQFELMDLQQELGLTFVVVTHDQeeamTMADRIA 225
Cdd:TIGR03719 462 GNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDR----WFLDRIA 507
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 24-186 1.02e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 86.47  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSlAGIPPYRRPVNMMFQS 103
Cdd:PRK13539    3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLGHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGLKQDGMPKADIAErvaqMLKLVKLEKFAKRKPHQLSGGQRQRVALARSL-AKRPkVLLLDEPLG 182
Cdd:PRK13539   82 NAMKPALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILDEPTA 156


                  ....
gi 1371712025 183 ALDK 186
Cdd:PRK13539  157 ALDA 160
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 26-186 3.02e-19

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 84.85  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  26 VKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQSY 104
Cdd:cd03231     3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGHAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTVENNVAFgLKQDGmpkADiaERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGAL 184
Cdd:cd03231    83 GIKTTLSVLENLRF-WHADH---SD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156


                  ..
gi 1371712025 185 DK 186
Cdd:cd03231   157 DK 158
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-246 4.01e-19

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 86.09  E-value: 4.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKFGD-FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQslagipPYRRPV 97
Cdd:PRK15056    2 MQQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  98 NMMFQSYA--------LFPhMTVENNVAFG-LKQDGM---PKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALA 165
Cdd:PRK15056   76 QKNLVAYVpqseevdwSFP-VLVEDVVMMGrYGHMGWlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 166 RSLAKRPKVLLLDEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHDQEEAMTMADrIAVMSHGKVVQVATPAEIY 242
Cdd:PRK15056  155 RAIAQQGQVILLDEPFTGVDVK----TEARIISLLRELrdeGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229


                  ....
gi 1371712025 243 EAPN 246
Cdd:PRK15056  230 TAEN 233
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
51-233 5.23e-19

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 88.43  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  51 FFALLGAsgcGKSTLLRMLAGFEQPTSGEIILDGQSLagipPYRRPVNMMFQSYAL----------FPHMTVENNVA--- 117
Cdd:PRK11288  284 LFGLVGA---GRSELMKLLYGATRRTAGQVYLDGKPI----DIRSPRDAIRAGIMLcpedrkaegiIPVHSVADNINisa 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 118 ------FGLKQDGMPKADIAERVAQMLKlVKlekfaKRKPHQ----LSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:PRK11288  357 rrhhlrAGCLINNRWEAENADRFIRSLN-IK-----TPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1371712025 188 LREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK11288  431 AKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 30-251 1.18e-18

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: 84.38  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  30 TKKFGDFTavddLSL---NIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVNMMFQSYAL 106
Cdd:cd03237     7 KKTLGEFT----LEVeggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 107 FphmtvenNVAFGLKQDGMPKADIAervaqmlKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDK 186
Cdd:cd03237    83 S-------SITKDFYTHPYFKTEIA-------KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 187 KLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSH--GKVVQVATPAEIYEAPNsRFVA 251
Cdd:cd03237   149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGepSVNGVANPPQSLRSGMN-RFLK 214
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 22-235 1.20e-18

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 83.85  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFG-----------------------DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFE--QPT 76
Cdd:COG2401     6 PFFVLMRVTKVYSsvldlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  77 SGEIILDgqslAGIPPYRRPVnmmfqsyalfphmtVENnvaFGLKQDgmPKAdiaerVAQMLKLVKLEK--FAKRKPHQL 154
Cdd:COG2401    86 AGCVDVP----DNQFGREASL--------------IDA---IGRKGD--FKD-----AVELLNAVGLSDavLWLRRFKEL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 155 SGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQE-EAMTMADRIAVMSHGKVV 233
Cdd:COG2401   138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFVGYGGVP 217


                  ..
gi 1371712025 234 QV 235
Cdd:COG2401   218 EE 219
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 56-239 1.50e-17

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 84.08  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  56 GASGCGKSTLLRMLAGFEQPTSGEIILDGQSL--AGIPPYRrpvNMM---FQSYALFPHMtvennvafglkqDGMPKADI 130
Cdd:COG4615   365 GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtaDNREAYR---QLFsavFSDFHLFDRL------------LGLDGEAD 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 131 AERVAQMLKLVKLE--------KFAKRKphqLSGGQRQRVALARSLA-KRPkVLLLDE------PlgaldkklreetQF- 194
Cdd:COG4615   430 PARARELLERLELDhkvsvedgRFSTTD---LSQGQRKRLALLVALLeDRP-ILVFDEwaadqdP------------EFr 493

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 195 ------ELMDLQQElGLTFVVVTHDqEEAMTMADRIAVMSHGKVVQVATPA 239
Cdd:COG4615   494 rvfyteLLPELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
22-245 2.77e-17

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 81.88  E-value: 2.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP----TSGEIILDGQSLAGIPPY 93
Cdd:COG4170     2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 ------RRPVNMMFQ--SYALFPHMTVENNvafgLKQdGMPKADI-----------AERVAQMLKLVKL---EKFAKRKP 151
Cdd:COG4170    82 errkiiGREIAMIFQepSSCLDPSAKIGDQ----LIE-AIPSWTFkgkwwqrfkwrKKRAIELLHRVGIkdhKDIMNSYP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 152 HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKlreeTQ---FELMD-LQQELGLTFVVVTHDQEEAMTMADRIAVM 227
Cdd:COG4170   157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST----TQaqiFRLLArLNQLQGTSILLISHDLESISQWADTITVL 232

                         250
                  ....*....|....*...
gi 1371712025 228 SHGKVVQVATPAEIYEAP 245
Cdd:COG4170   233 YCGQTVESGPTEQILKSP 250
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 46-240 2.98e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 83.17  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  46 IYTREFFALLGASGCGKSTLLRMLAgFEQPT----SGEIILDGQSLaGIPPYRRPVNMMFQSYALFPHMTVENNVAFG-- 119
Cdd:TIGR00955  48 AKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHLMFQah 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 120 LK-QDGMPKADIAERVAQMLKLVKLEKFAKRK---PHQ---LSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREET 192
Cdd:TIGR00955 126 LRmPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371712025 193 QFELMDLQQElGLTFVVVTHD-QEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:TIGR00955 206 VQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 39-212 3.55e-17

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 78.35  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIldgqslagIPPYRrpvNMMF---QSYalfphmtvenn 115
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEGE---DLLFlpqRPY----------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 116 vafglkqdgMPKADIAERVAqmlklvklekfakrKP--HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDkklrEETQ 193
Cdd:cd03223    75 ---------LPLGTLREQLI--------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESE 127

                         170
                  ....*....|....*....
gi 1371712025 194 FELMDLQQELGLTFVVVTH 212
Cdd:cd03223   128 DRLYQLLKELGITVISVGH 146
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 38-269 7.13e-17

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: 82.75  E-value: 7.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   38 AVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQS-LAGIPPYRRPVNMMFQSYALFPHMTVENNV 116
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  117 AFGLKQDGMPKADIaERVAQM-LKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFE 195
Cdd:TIGR01257 2034 YLYARLRGVPAEEI-EKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025  196 LMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEIyeapNSRFvadfiGDVNIFDGKVTSAED 269
Cdd:TIGR01257 2113 IVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKF-----GDGYIVTMKIKSPKD 2176
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-237 1.07e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 81.37  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFISVKNVTKKfgDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPY----- 93
Cdd:PRK09700  261 AHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavkk 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 -------RRPVNMMFQSYALFPHMTVENNV-------AFGLKQDGMpKADIAERVAQMLKLvkleKFA--KRKPHQLSGG 157
Cdd:PRK09700  339 gmayiteSRRDNGFFPNFSIAQNMAISRSLkdggykgAMGLFHEVD-EQRTAENQRELLAL----KCHsvNQNITELSGG 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 158 QRQRVALARSLAKRPKVLLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:PRK09700  414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 24-225 1.54e-16

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 80.93  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILdGQSlagippyrrpVNMMF-- 101
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET----------VKLAYvd 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 QSY-ALFPHMTVENNVAFGLKQDGMPKADIAER--VA---------QmlKLVKlekfakrkphQLSGGQRQRVALARSLA 169
Cdd:PRK11819  394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSRayVGrfnfkggdqQ--KKVG----------VLSGGERNRLHLAKTLK 461

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 170 KRPKVLLLDEPLGALDKklreETqfeLMDLQQELgLTF----VVVTHDQeeamTMADRIA 225
Cdd:PRK11819  462 QGGNVLLLDEPTNDLDV----ET---LRALEEAL-LEFpgcaVVISHDR----WFLDRIA 509
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 24-222 1.55e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 77.30  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL-AGIPPYRRPVNMMFQ 102
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 103 SYALFPHMTVENNVAFGLKqdgmpKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLG 182
Cdd:PRK13540   82 RSGINPYLTLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1371712025 183 ALDKKLREETQFELMDLQQELGLtfVVVTHDQEEAMTMAD 222
Cdd:PRK13540  157 ALDELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-243 3.17e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.55  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGiPPYRRPVN----M 99
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVCpriaY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 100 MFQSYA--LFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:NF033858   81 MPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 178 DEPLGALDKKLREetQF-ELMD-LQQEL-GLTFVVVTHDQEEAMTMaDRIAVMSHGKVVQVATPAEIYE 243
Cdd:NF033858  161 DEPTTGVDPLSRR--QFwELIDrIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 42-190 4.95e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 75.68  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  42 LSLNIYTREFFALL------------GASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIP-PYrrpVNMMFQSYALFP 108
Cdd:PRK13541    7 LQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 109 HMTVENNVAFGLKqdgmpKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:PRK13541   84 EMTVFENLKFWSE-----IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158


                  ..
gi 1371712025 189 RE 190
Cdd:PRK13541  159 RD 160
GguA NF040905
sugar ABC transporter ATP-binding protein;
27-234 5.75e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 79.06  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  27 KNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFeQPT---SGEIILDGQ--SLAGIP-PYRRPVNMM 100
Cdd:NF040905    5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEvcRFKDIRdSEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 101 FQSYALFPHMTVENNVAFGLKQDGMPKADIAE---RVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:NF040905   84 HQELALIPYLSIAENIFLGNERAKRGVIDWNEtnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 178 DEPLGALDkklrEETQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:NF040905  164 DEPTAALN----EEDSAALLDLLLELkaqGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 39-232 8.20e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 78.51  E-value: 8.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRRPVN-MMFQSY-----ALFPHMTV 112
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEdrkrdGLVLGMSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 113 ENNVA------FGLKQDGMPKADIAERVAQMLKLvklekFAKRKPHQ------LSGGQRQRVALARSLAKRPKVLLLDEP 180
Cdd:PRK10762  348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 181 LGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK10762  423 TRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 26-215 9.35e-16

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 78.84  E-value: 9.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  26 VKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILdGQSL--AGIPPYRRpvnmmfqs 103
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevAYFDQHRA-------- 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 yALFPHMTVENNVAFGlKQDGMpkadIAERVAQMLKLvkLEKF---AKR--KP-HQLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:PRK11147  393 -ELDPEKTVMDNLAEG-KQEVM----VNGRPRHVLGY--LQDFlfhPKRamTPvKALSGGERNRLLLARLFLKPSNLLIL 464

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1371712025 178 DEPLGALDkklreetqFELMDLQQEL-----GlTFVVVTHDQE 215
Cdd:PRK11147  465 DEPTNDLD--------VETLELLEELldsyqG-TVLLVSHDRQ 498
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 18-232 1.24e-15

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 78.17  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKfgdftAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRR-- 95
Cdd:PRK15439  263 AAGAPVLTVEDLTGE-----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRla 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 ------PVNMmfQSYALFPHMTVENNVAfGLKQDGMP-------KADIAERVAQML--KLVKLEKFAKRkphqLSGGQRQ 160
Cdd:PRK15439  338 rglvylPEDR--QSSGLYLDAPLAWNVC-ALTHNRRGfwikparENAVLERYRRALniKFNHAEQAART----LSGGNQQ 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371712025 161 RVALARSLAKRPKVLLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK15439  411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 25-213 2.45e-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: 77.28  E-value: 2.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  25 SVKNVTKKFGDFTAV-DDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgqslagiPPYRrpVNMMFQS 103
Cdd:TIGR03719   6 TMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIK--VGYLPQE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFGL--KQDGM------------PKADIAERVAQMLKL-------------VKLEKF--AKRKP--- 151
Cdd:TIGR03719  77 PQLDPTKTVRENVEEGVaeIKDALdrfneisakyaePDADFDKLAAEQAELqeiidaadawdldSQLEIAmdALRCPpwd 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 152 ---HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKklreETQFELMDLQQELGLTFVVVTHD 213
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 21-231 2.72e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 76.97  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  21 KPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL----------AGI 90
Cdd:PRK10762    2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  91 ppyrrpvNMMFQSYALFPHMTVENNV--------AFG-LKQDGM-PKADiaervaQMLKLVKLEKFAKRKPHQLSGGQRQ 160
Cdd:PRK10762   82 -------GIIHQELNLIPQLTIAENIflgrefvnRFGrIDWKKMyAEAD------KLLARLNLRFSSDKLVGELSIGEQQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 161 RVALARSLAKRPKVLLLDEPLGALDKKlreETQ--FELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGK 231
Cdd:PRK10762  149 MVEIAKVLSFESKVIIMDEPTDALTDT---ETEslFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 35-230 3.11e-15

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: 73.90  E-value: 3.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  35 DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEI-----ILDGQSLAGIPPYRR-PVNMMFQSYALFp 108
Cdd:cd03290    13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRySVAYAAQKPWLL- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 109 HMTVENNVAFGLKQDgmpkadiAERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLL 177
Cdd:cd03290    92 NATVEENITFGSPFN-------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371712025 178 DEPLGALDKKLREE-TQFELMDLQQELGLTFVVVTHdQEEAMTMADRIAVMSHG 230
Cdd:cd03290   165 DDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PLN03211 PLN03211
ABC transporter G-25; Provisional
 50-231 5.83e-15

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 76.46  E-value: 5.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  50 EFFALLGASGCGKSTLLRMLAGFEQPTS--GEIILDGQSLAgiPPYRRPVNMMFQSYALFPHMTVENNVAFG-------- 119
Cdd:PLN03211   95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQDDILYPHLTVRETLVFCsllrlpks 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 120 -LKQDgmpKADIAERVAQMLKLVKLEK--FAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFEL 196
Cdd:PLN03211  173 lTKQE---KILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371712025 197 MDLQQElGLTFVVVTHD-QEEAMTMADRIAVMSHGK 231
Cdd:PLN03211  250 GSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
13-252 1.61e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.84  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASKPFISVKNVTKKFGDFtavddlSLN-----IYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgQSL 87
Cdd:PRK13409  330 PPRDESERETLVEYPDLTKKLGDF------SLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  88 AGIPPYRRPVnmmfqsyalfPHMTVE-----NNVAFGlkqDGMPKADIAERvaqmlklVKLEKFAKRKPHQLSGGQRQRV 162
Cdd:PRK13409  403 SYKPQYIKPD----------YDGTVEdllrsITDDLG---SSYYKSEIIKP-------LQLERLLDKNVKDLSGGELQRV 462

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 163 ALARSLAKRPKVLLLDEPLGALD-----------KKLREETqfelmdlqqelGLTFVVVTHDQeeAM--TMADRIAVMS- 228
Cdd:PRK13409  463 AIAACLSRDADLYLLDEPSAHLDveqrlavakaiRRIAEER-----------EATALVVDHDI--YMidYISDRLMVFEg 529

                         250       260
                  ....*....|....*....|....*...
gi 1371712025 229 ----HGKvvqVATPAEIYEAPNsRFVAD 252
Cdd:PRK13409  530 epgkHGH---ASGPMDMREGMN-RFLKE 553
PLN03232 PLN03232
ABC transporter C family member; Provisional
 42-249 1.62e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 75.40  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   42 LSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVNMMFQSYALFPHmTVENNV-AF 118
Cdd:PLN03232  1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLSIIPQSPVLFSG-TVRFNIdPF 1333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  119 GLKQDgmpkADIAErvaqMLKLVKLEKFAKRKPHQL-----------SGGQRQRVALARSLAKRPKVLLLDEPLGALD-- 185
Cdd:PLN03232  1334 SEHND----ADLWE----ALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDvr 1405

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  186 ------KKLREETQfelmdlqqelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRF 249
Cdd:PLN03232  1406 tdsliqRTIREEFK----------SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 22-232 2.98e-14

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 74.05  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIL-DGQSLAGIP----PYRRP 96
Cdd:PRK10636  311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAqhqlEFLRA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 VNMMFQSYALFPHMTVENNV-----AFGLKQDGMpkADIAERvaqmlklvklekfakrkphqLSGGQRQRVALARSLAKR 171
Cdd:PRK10636  391 DESPLQHLARLAPQELEQKLrdylgGFGFQGDKV--TEETRR--------------------FSGGEKARLVLALIVWQR 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 172 PKVLLLDEPLGALDKKLREETQFELMDLQQELgltfVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK10636  449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
PLN03130 PLN03130
ABC transporter C family member; Provisional
 42-249 3.10e-14

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 74.39  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   42 LSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVNMMFQSYALFPHmTVENNV-AF 118
Cdd:PLN03130  1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRKVLGIIPQAPVLFSG-TVRFNLdPF 1336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  119 GLKQDgmpkADIAERvaqmLKLVKLEKFAKRKPHQL-----------SGGQRQRVALARSLAKRPKVLLLDEPLGALD-- 185
Cdd:PLN03130  1337 NEHND----ADLWES----LERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDvr 1408

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  186 ------KKLREETQfelmdlqqelGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAPNSRF 249
Cdd:PLN03130  1409 tdaliqKTIREEFK----------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
35-245 3.47e-14

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 73.98  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  35 DFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGI--PPYRRPVNMMFQSYALFPHmTV 112
Cdd:PRK10789  327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqlDSWRSRLAVVSQTPFLFSD-TV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 113 ENNVAFGlkqdgMPKADiAERVAQMLKLVKLEKFAKRKPH-----------QLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:PRK10789  406 ANNIALG-----RPDAT-QQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDAL 479

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 182 GALDKklREETQFeLMDLQQ-ELGLTFVVVTHdQEEAMTMADRIAVMSHGKVVQVATPAEIYEAP 245
Cdd:PRK10789  480 SAVDG--RTEHQI-LHNLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
PTZ00243 PTZ00243
ABC transporter; Provisional
 41-233 3.84e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 74.43  E-value: 3.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgQSLAGIPPyrrpvnmmfQSYALfpHMTVENNVAFGL 120
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQ---------QAWIM--NATVRGNILFFD 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  121 KQDGMPKADiAERVAQMLKLVK-----LEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFE 195
Cdd:PTZ00243   746 EEDAARLAD-AVRVSQLEADLAqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEE 824

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1371712025  196 LMdLQQELGLTFVVVTHdQEEAMTMADRIAVMSHGKVV 233
Cdd:PTZ00243   825 CF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 298-379 3.90e-14

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: 66.87  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 298 VAIRPEKIRIgrqppaHAPVNAAEGEIWDIGYLGDMTVFHIRLKDGKVVKASSLNAVRaveDPLGYDQQVWISFGDDAGV 377
Cdd:pfam08402   1 LAIRPEKIRL------AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHA---RPPAPGDRVGLGWDPEDAH 71


                  ..
gi 1371712025 378 VL 379
Cdd:pfam08402  72 VL 73
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 27-234 3.92e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 74.30  E-value: 3.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   27 KNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLrmlagFEQptSGEIILDGQSLA--GIPPYRRPVNMMFQSY 104
Cdd:PTZ00265  1233 TNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTV-----FKN--SGKILLDGVDICdyNLKDLRNLFSIVSQEP 1305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  105 ALFpHMTVENNVAFGlKQDGMpkadiAERVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARSLAKRPK 173
Cdd:PTZ00265  1306 MLF-NMSIYENIKFG-KEDAT-----REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPK 1378

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025  174 VLLLDEPLGALD---KKLREETqfeLMDLQQELGLTFVVVTHdQEEAMTMADRIAVMSH----GKVVQ 234
Cdd:PTZ00265  1379 ILLLDEATSSLDsnsEKLIEKT---IVDIKDKADKTIITIAH-RIASIKRSDKIVVFNNpdrtGSFVQ 1442
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 27-233 4.09e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 73.61  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  27 KNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSL---AGIPPYRRPVNMMFQS 103
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 104 YALFPHMTVENNVAFG--------LKQDGMPKADIAervaqMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVL 175
Cdd:PRK10982   82 LNLVLQRSVMDNMWLGryptkgmfVDQDKMYRDTKA-----IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371712025 176 LLDEPLGALDKKlREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK10982  157 IMDEPTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 19-213 5.16e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 73.23  E-value: 5.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  19 ASKPFI-SVKNVTKKFGDFTAV-DDLSLNiytreFF-----ALLGASGCGKSTLLRMLAGFEQPTSGEIILDgqslagiP 91
Cdd:PRK11819    1 MMAQYIyTMNRVSKVVPPKKQIlKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-------P 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 PYRrpVNMMFQSYALFPHMTVENNVAFGL-----KQD---------GMPKADIAERVAQMLKL-------------VKLE 144
Cdd:PRK11819   69 GIK--VGYLPQEPQLDPEKTVRENVEEGVaevkaALDrfneiyaayAEPDADFDALAAEQGELqeiidaadawdldSQLE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 145 KF--AKRKPH------QLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKklreET-----QFelmdLQQELGlTFVVVT 211
Cdd:PRK11819  147 IAmdALRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESvawleQF----LHDYPG-TVVAVT 217


                  ..
gi 1371712025 212 HD 213
Cdd:PRK11819  218 HD 219
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 13-185 5.50e-14

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: 73.28  E-value: 5.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  13 APWADPASKPFISVKNVTKKFGDFTavddLSLN---IYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgQSLAG 89
Cdd:COG1245   331 APRREKEEETLVEYPDLTKSYGGFS----LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISY 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  90 IPPYRRPvnmmfqSYalfpHMTVE------NNVAFGlkqDGMPKADIAERVaqmlklvKLEKFAKRKPHQLSGGQRQRVA 163
Cdd:COG1245   406 KPQYISP------DY----DGTVEeflrsaNTDDFG---SSYYKTEIIKPL-------GLEKLLDKNVKDLSGGELQRVA 465

                         170       180
                  ....*....|....*....|..
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALD 185
Cdd:COG1245   466 IAACLSRDADLYLLDEPSAHLD 487
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 41-244 7.04e-14

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: 73.44  E-value: 7.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVNMMFQSYALFPHMTVENNVAF 118
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiGLHDLRFKITIIPQDPVLFSGSLRMNLDPF 1383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  119 GLKQDgmpkadiaERVAQMLKLVKLEKFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:TIGR00957 1384 SQYSD--------EEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025  188 LRE------ETQFElmdlqqelGLTFVVVTHDQEEAMTMAdRIAVMSHGKVVQVATPAEIYEA 244
Cdd:TIGR00957 1456 TDNliqstiRTQFE--------DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 41-230 1.07e-13

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 70.66  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQslagippyrrpVNMMFQSYALFPHmTVENNVAFGL 120
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 121 KQDgmpkadiAERVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKVLLLDEPLGALDkKLR 189
Cdd:cd03291   123 SYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VFT 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1371712025 190 EETQFELMDLQQELGLTFVVVTHDQEEaMTMADRIAVMSHG 230
Cdd:cd03291   195 EKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 39-232 1.31e-13

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: 71.78  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAG-FEQPTSGEIILDGQSLAgippYRRPVNMMFQSYALFPH-------- 109
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVD----IRNPAQAIRAGIAMVPEdrkrhgiv 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 110 --MTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPH------QLSGGQRQRVALARSLAKRPKVLLLDEPL 181
Cdd:TIGR02633 352 piLGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 182 GALDKKLREETqFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:TIGR02633 432 RGVDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
24-233 1.51e-13

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 70.92  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCG--KSTLLRMLAGfeqPTSGE-------IILDGQSLAGIPPYR 94
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*tWCANRRALRRTIG*H 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  95 RPVNM-MFQSYAlfphmTVENNVAFGLKQDgMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPK 173
Cdd:NF000106   91 RPVR*gRRESFS-----GRENLYMIGR*LD-LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 174 VLLLDEPLGALDKKLREETQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
22-245 1.60e-13

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 70.60  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  22 PFISVKNVTKKF----GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQP----TSGEIILDGQSLAGIPPY 93
Cdd:PRK15093    2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RR------PVNMMFQ--SYALFPHMTVENNVA---------------FGLKQdgmpkadiaERVAQMLKLV--KLEKFAK 148
Cdd:PRK15093   82 ERrklvghNVSMIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWRK---------RRAIELLHRVgiKDHKDAM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 149 RK-PHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAVM 227
Cdd:PRK15093  153 RSfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232

                         250
                  ....*....|....*...
gi 1371712025 228 SHGKVVQVATPAEIYEAP 245
Cdd:PRK15093  233 YCGQTVETAPSKELVTTP 250
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 24-229 1.64e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 72.37  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   24 ISVKNV-----TKKfgDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIIL-DGQSLAGI--PPYRR 95
Cdd:PTZ00265   383 IQFKNVrfhydTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDInlKWWRS 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   96 PVNMMFQSYALFPHmTVENNVAFGL-------------------KQDGMPKADIAE------------------------ 132
Cdd:PTZ00265   461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndSQENKNKRNSCRakcagdlndmsnttdsneliemrk 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  133 --------RVAQMLKLVKLEKFAKRKP-----------HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQ 193
Cdd:PTZ00265   540 nyqtikdsEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1371712025  194 FELMDLQQELGLTFVVVTHdQEEAMTMADRIAVMSH 229
Cdd:PTZ00265   620 KTINNLKGNENRITIIIAH-RLSTIRYANTIFVLSN 654
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
24-253 3.53e-13

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 69.07  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF--------------------GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILD 83
Cdd:PRK13546    5 VNIKNVTKEYriyrtnkermkdalipkhknKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  84 GQslagippyrrpVNMMFQSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVA 163
Cdd:PRK13546   85 GE-----------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 164 LARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLqQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI-- 241
Cdd:PRK13546  154 FSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlp 232

                         250
                  ....*....|...
gi 1371712025 242 -YEApnsrFVADF 253
Cdd:PRK13546  233 kYEA----FLNDF 241
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 23-233 4.50e-13

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: 67.29  E-value: 4.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  23 FISVKNVT----KKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAG----FEQPtSGEIILDGQSLAGIP-PY 93
Cdd:cd03233     3 TLSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYNGIPYKEFAeKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  94 RRPVNMMFQSYALFPHMTVENNVAFGLKQDGmpkadiaervAQMLKLVklekfakrkphqlSGGQRQRVALARSLAKRPK 173
Cdd:cd03233    82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKG----------NEFVRGI-------------SGGERKRVSIAEALVSRAS 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 174 VLLLDEPLGALD--------KKLREetqfelmdLQQELGLT-FVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:cd03233   139 VLCWDNSTRGLDsstaleilKCIRT--------MADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 24-234 4.71e-13

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: 68.73  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTL----LRMLAgfeqpTSGEIILDGQSLAGIP--PYRR 95
Cdd:cd03289     3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPlqKWRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 PVNMMFQSYALFPHMTVENNVAFGLKQDgMPKADIAERVAqmLKLVkLEKFAKRKPHQL-------SGGQRQRVALARSL 168
Cdd:cd03289    78 AFGVIPQKVFIFSGTFRKNLDPYGKWSD-EEIWKVAEEVG--LKSV-IEQFPGQLDFVLvdggcvlSHGHKQLMCLARSV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 169 AKRPKVLLLDEPLGALD----KKLREEtqfelmdLQQELGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQ 234
Cdd:cd03289   154 LSKAKILLLDEPSAHLDpityQVIRKT-------LKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 41-230 5.71e-13

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 70.71  E-value: 5.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   41 DLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQslagippyrrpVNMMFQSYALFPHmTVENNVAFGL 120
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGL 511

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  121 KQDGMpkadiaeRVAQMLKLVKLEKFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKVLLLDEPLGALDkKLR 189
Cdd:TIGR01271  512 SYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD-VVT 583

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1371712025  190 EETQFELMDLQQELGLTFVVVThDQEEAMTMADRIAVMSHG 230
Cdd:TIGR01271  584 EKEIFESCLCKLMSNKTRILVT-SKLEHLKKADKILLLHEG 623
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 24-233 9.76e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.59  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGfEQP-TSGEIILDGQ----SLAGIPPyrRPVN 98
Cdd:PRK11147    4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQDlivaRLQQDPP--RNVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MmfqsyalfphmTVENNVAFGLK-----------------QDGMPK-----ADIAE------------RVAQMLKLVKLE 144
Cdd:PRK11147   81 G-----------TVYDFVAEGIEeqaeylkryhdishlveTDPSEKnlnelAKLQEqldhhnlwqlenRINEVLAQLGLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 145 kfAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDkklreetqFELMDLQQELGLTF----VVVTHDQEEAMTM 220
Cdd:PRK11147  150 --PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IETIEWLEGFLKTFqgsiIFISHDRSFIRNM 219

                         250
                  ....*....|...
gi 1371712025 221 ADRIAVMSHGKVV 233
Cdd:PRK11147  220 ATRIVDLDRGKLV 232
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 48-226 1.58e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 64.70  E-value: 1.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   48 TREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGqslagippyrrpvnmmfqsyalfphmtvennvafglkqdgmpk 127
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  128 adiAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFE-----LMDLQQE 202
Cdd:smart00382  38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 1371712025  203 LGLTFVVVTHDQEEAMTMADRIAV 226
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 9-241 7.39e-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: 7.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025    9 RRSFAPWADPAskpfISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGqS 86
Cdd:TIGR00957  626 RRTIKPGEGNS----ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-S 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   87 LAGIPpyrrpvnmmfqSYALFPHMTVENNVAFGLKQDGMPKADIAERVAQMLKLVKLEKFAK----RKPHQLSGGQRQRV 162
Cdd:TIGR00957  701 VAYVP-----------QQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRteigEKGVNLSGGQKQRV 769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  163 ALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQEL-GLTFVVVTHDQeEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:TIGR00957  770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 43-241 1.04e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 66.19  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  43 SLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDgqslagippYRRPVNMMF-QSYALFPHMTVENN---VAF 118
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---------FSHITRLSFeQLQKLVSDEWQRNNtdmLSP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 119 GLKQDGMPKADI-------AERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREE 191
Cdd:PRK10938   94 GEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371712025 192 TQFELMDLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATPAEI 241
Cdd:PRK10938  174 LAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
PTZ00243 PTZ00243
ABC transporter; Provisional
 42-249 1.12e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 66.73  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   42 LSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLA--GIPPYRRPVNMMFQSYALFPHmTVENNVafg 119
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGayGLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  120 lkqDGMPKADIAErVAQMLKLVKL-EKFAKRKP----------HQLSGGQRQRVALARSLAKR-PKVLLLDEPLGALDKK 187
Cdd:PTZ00243  1405 ---DPFLEASSAE-VWAALELVGLrERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPA 1480

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371712025  188 LREETQFELMDLQQelGLTFVVVTHdqeEAMTMA--DRIAVMSHGKVVQVATPAEIYEAPNSRF 249
Cdd:PTZ00243  1481 LDRQIQATVMSAFS--AYTVITIAH---RLHTVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 18-217 1.41e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.81  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  18 PASKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAG------------F-EQPTSGEIILDG 84
Cdd:PRK10938  255 PANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFgRRRGSGETIWDI 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  85 QSLAGippyrrpvnmmFQSYALfpHM------TVENNV------AFGLKQDgmpkadIAER----VAQMLKLVKLEKFAK 148
Cdd:PRK10938  335 KKHIG-----------YVSSSL--HLdyrvstSVRNVIlsgffdSIGIYQA------VSDRqqklAQQWLDILGIDKRTA 395

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 149 RKP-HQLSGGQrQRVAL-ARSLAKRPKVLLLDEPLGALDKKLREET-QF-ELMDLQQELGLTFvvVTHDQEEA 217
Cdd:PRK10938  396 DAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVrRFvDVLISEGETQLLF--VSHHAEDA 465
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 39-232 3.12e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 64.57  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAG-FEQPTSGEIILDGQSL----------AGI---PPYRRpvnmmfqSY 104
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVkirnpqqaiaQGIamvPEDRK-------RD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTVENNV--------AFGLKQDGMPKADIAERVAQMLKLvklekfakRKPH------QLSGGQRQRVALARSLAK 170
Cdd:PRK13549  351 GIVPVMGVGKNItlaaldrfTGGSRIDDAAELKTILESIQRLKV--------KTASpelaiaRLSGGNQQKAVLAKCLLL 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371712025 171 RPKVLLLDEPLGALDKKLREETqFELM-DLQQElGLTFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK13549  423 NPKILILDEPTRGIDVGAKYEI-YKLInQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PLN03232 PLN03232
ABC transporter C family member; Provisional
 22-244 3.92e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.00  E-value: 3.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   22 PFISVKNvtkkfGDFT--------AVDDLSLNIYTREFFALLGASGCGKSTLLR-MLAGFEQPTSGEIILDGqSLAGIPP 92
Cdd:PLN03232   613 PAISIKN-----GYFSwdsktskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVPQ 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   93 yrrpVNMMFQSyalfphmTVENNVAFGLKQDgmpkadiAERVAQMLKLVKLEK----FAKRKPHQL-------SGGQRQR 161
Cdd:PLN03232   687 ----VSWIFNA-------TVRENILFGSDFE-------SERYWRAIDVTALQHdldlLPGRDLTEIgergvniSGGQKQR 748

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  162 VALARSLAKRPKVLLLDEPLGALDKKLREETQFELMdlQQEL-GLTFVVVThDQEEAMTMADRIAVMSHGKVVQVATPAE 240
Cdd:PLN03232   749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM--KDELkGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAE 825


                   ....
gi 1371712025  241 IYEA 244
Cdd:PLN03232   826 LSKS 829
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 20-233 5.65e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 62.35  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFE--QPTSGEIILDGQSLAGIPPYRRP- 96
Cdd:CHL00131    4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAh 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  97 --VNMMFQsyalFPhmtVE----NNVAF-------GLKQDGMPKAD---IAERVAQMLKLVKL-EKFAKRKPHQ-LSGGQ 158
Cdd:CHL00131   84 lgIFLAFQ----YP---IEipgvSNADFlrlaynsKRKFQGLPELDpleFLEIINEKLKLVGMdPSFLSRNVNEgFSGGE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 159 RQRVALARSLAKRPKVLLLDEPLGALD-KKLRE--ETQFELMDLQQelglTFVVVTHDQE-EAMTMADRIAVMSHGKVV 233
Cdd:CHL00131  157 KKRNEILQMALLDSELAILDETDSGLDiDALKIiaEGINKLMTSEN----SIILITHYQRlLDYIKPDYVHVMQNGKII 231
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 53-233 9.52e-11

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 60.33  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  53 ALLGASGCGKSTLLRMLAGFEQP--TSGEIILDGQSLAgiPPYRRPVNMMFQSYALFPHMTVENNVAFGLKQDGmpkadi 130
Cdd:cd03232    37 ALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVREALRFSALLRG------ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 131 aervaqmlklvklekfakrkphqLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKklreETQFELMDLQQEL---GLTF 207
Cdd:cd03232   109 -----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKKLadsGQAI 161

                         170       180
                  ....*....|....*....|....*....
gi 1371712025 208 VVVTHdQEEAMTMA--DRIAVM-SHGKVV 233
Cdd:cd03232   162 LCTIH-QPSASIFEkfDRLLLLkRGGKTV 189
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
53-185 1.33e-10

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 60.63  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  53 ALL--GASGCGKSTLLRMLAGFEQPTSGEIILDGQslagipPYRRPVNMMFQSY-----ALFPHMTVENNVAF-----GL 120
Cdd:PRK13543   39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLENLHFlcglhGR 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371712025 121 KQDGMPkadiaervAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALD 185
Cdd:PRK13543  113 RAKQMP--------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
PLN03130 PLN03130
ABC transporter C family member; Provisional
 22-237 2.03e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.83  E-value: 2.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   22 PFISVKNVTKKF---GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTS-GEIILDGqSLAGIPPyrrpV 97
Cdd:PLN03130   613 PAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG-TVAYVPQ----V 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   98 NMMFQSyalfphmTVENNVAFGLKQDGmPKADIAERVAQM---LKLV---KLEKFAKRKPHqLSGGQRQRVALARSLAKR 171
Cdd:PLN03130   688 SWIFNA-------TVRDNILFGSPFDP-ERYERAIDVTALqhdLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSN 758

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025  172 PKVLLLDEPLGALDKKLREETqFELMdLQQEL-GLTFVVVThDQEEAMTMADRIAVMSHGKVVQVAT 237
Cdd:PLN03130   759 SDVYIFDDPLSALDAHVGRQV-FDKC-IKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 26-233 2.22e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.83  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  26 VKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQslAGIPPYRRPVNMMF-QSY 104
Cdd:PRK15064  322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--ANIGYYAQDHAYDFeNDL 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 105 ALFPHMTvennvafglkQDGMPKADIaERVAQML-KLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGA 183
Cdd:PRK15064  400 TLFDWMS----------QWRQEGDDE-QAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371712025 184 LDKKLREETQFELMDLQQelglTFVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:PRK15064  469 MDMESIESLNMALEKYEG----TLIFVSHDREFVSSLATRIIEITPDGVV 514
PLN03073 PLN03073
ABC transporter F family; Provisional
 53-232 6.77e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 60.64  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  53 ALLGASGCGKSTLLRMLAGFEQPTSGEI---------ILDGQSLAGIPPYRRPVNMMFQSYALFPHMTVENNV-AFGLKQ 122
Cdd:PLN03073  539 AMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLgSFGVTG 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 123 DgmpkadiaervaqmlklvklekFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREEtqfelmdLQQE 202
Cdd:PLN03073  619 N----------------------LALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA-------LIQG 669

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371712025 203 LGL---TFVVVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PLN03073  670 LVLfqgGVLMVSHDEHLISGSVDELWVVSEGKV 702
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 39-212 1.32e-09

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: 59.76  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  39 VDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDG-QSLAGIPpyRRP--VNMMFQSYALFPhMTVENn 115
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkGKLFYVP--QRPymTLGTLRDQIIYP-DSSED- 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 116 vafgLKQDGMPKADIAervaQMLKLVKLEKFAKRK---------PHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDK 186
Cdd:TIGR00954 544 ----MKRRGLSDKDLE----QILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615

                         170       180
                  ....*....|....*....|....*.
gi 1371712025 187 KLrEETQFELMdlqQELGLTFVVVTH 212
Cdd:TIGR00954 616 DV-EGYMYRLC---REFGITLFSVSH 637
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 53-230 1.84e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 59.74  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   53 ALLGASGCGKSTLLRMLAgfEQPTSGeIILDGQSLAGIPP----YRRPVNMMFQSYALFPHMTVENNVAFG--LKQ-DGM 125
Cdd:TIGR00956  793 ALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPldssFQRSIGYVQQQDLHLPTSTVRESLRFSayLRQpKSV 869

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  126 PKADIAERVAQMLKLVKLEKFAKR---KPHQ-LSGGQRQRVALARSLAKRPKVLL-LDEPLGALDkklrEETQFELMDLQ 200
Cdd:TIGR00956  870 SKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWSICKLM 945

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1371712025  201 QEL---GLTFVVVTHdQEEAMTMA--DRIAVMSHG 230
Cdd:TIGR00956  946 RKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 50-233 5.11e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.20  E-value: 5.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   50 EFFALLGASGCGKSTLLRMLA----GFEQPTSGEIILDGQSLAGIPP-YRRPVNMMFQSYALFPHMTVENNVAF------ 118
Cdd:TIGR00956   88 ELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKhYRGDVVYNAETDVHFPHLTVGETLDFaarckt 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  119 -GLKQDGMPKADIAERVAQM------LKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKlree 191
Cdd:TIGR00956  168 pQNRPDGVSREEYAKHIADVymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA---- 243

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1371712025  192 TQFELMDLQQE----LGLT-FVVVTHDQEEAMTMADRIAVMSHGKVV 233
Cdd:TIGR00956  244 TALEFIRALKTsaniLDTTpLVAIYQCSQDAYELFDKVIVLYEGYQI 290
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 24-240 6.25e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 57.43  E-value: 6.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKfgDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRrPVNMMF-- 101
Cdd:PRK10982  251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGFal 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 102 -----QSYALFPHMTVENNV----------AFGLKQDGMPKADIAERVAQMLklvklekfAKRKPHQ-----LSGGQRQR 161
Cdd:PRK10982  328 vteerRSTGIYAYLDIGFNSlisnirnyknKVGLLDNSRMKSDTQWVIDSMR--------VKTPGHRtqigsLSGGNQQK 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 162 VALARSLAKRPKVLLLDEPLGALDKKlreeTQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIAVMSHGKVVQVATP 238
Cdd:PRK10982  400 VIIGRWLLTQPEILMLDEPTRGIDVG----AKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 475


                  ..
gi 1371712025 239 AE 240
Cdd:PRK10982  476 KT 477
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 24-185 6.40e-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: 58.00  E-value: 6.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   24 ISVKNVTKKF--GDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQpTSGEIILDGQSLAGIP--PYRRPVNM 99
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTlqTWRKAFGV 1296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  100 MFQSYALFPHmTVENNVAFGLKQDGMPKADIAERVAqmLKLVkLEKFAKRKPHQL-------SGGQRQRVALARSLAKRP 172
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQWSDEEIWKVAEEVG--LKSV-IEQFPDKLDFVLvdggyvlSNGHKQLMCLARSILSKA 1372

                          170
                   ....*....|...
gi 1371712025  173 KVLLLDEPLGALD 185
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 54-213 6.61e-09

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: 56.22  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  54 LLGASGCGKSTLLRMLAG--------FEQPTSGEIILD---GQSL---------AGIPPYRRPvnmmfQSYALFPHmTVE 113
Cdd:cd03236    31 LVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrGSELqnyftklleGDVKVIVKP-----QYVDLIPK-AVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 114 NNVAFGLKqdgmpKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQ 193
Cdd:cd03236   105 GKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179

                         170       180
                  ....*....|....*....|
gi 1371712025 194 FELMDLQQElGLTFVVVTHD 213
Cdd:cd03236   180 RLIRELAED-DNYVLVVEHD 198
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 30-226 8.94e-09

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 54.50  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  30 TKKFGDFTAVDDLSlNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQSLAGIPPYRrpvnmmfqsyalfph 109
Cdd:cd03222     7 VKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI--------------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 110 mtvennvafglkqdgmpkadiaervaqmlklvklekfakrkphQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLR 189
Cdd:cd03222    71 -------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371712025 190 EETQFELMDLQQELGLTFVVVTHDQEEAMTMADRIAV 226
Cdd:cd03222   108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 56-249 1.57e-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: 54.91  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  56 GASGCGKSTL----LRMLAGFEqptsGEIILDGQSLAGIPPY--RRPVNMMFQSYALFphmtvENNVAFGLKQDGMPKAD 129
Cdd:cd03288    54 GRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-----SGSIRFNLDPECKCTDD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 130 I---AERVAQMLKLVK-----LEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQ 201
Cdd:cd03288   125 RlweALEIAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371712025 202 ElgLTFVVVTHDQEEAMTmADRIAVMSHGKVVQVATPAEIYEAPNSRF 249
Cdd:cd03288   205 D--RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 24-234 1.87e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 54.80  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFE--QPTSGEIILDGQSLAGIPPYRRP---VN 98
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  99 MMFQSYALFPHM-------TVENNVAFGLKQDGMPKADIAERVAQMLKLVKL-EKFAKRKPHQ-LSGGQRQRVALARSLA 169
Cdd:PRK09580   82 MAFQYPVEIPGVsnqfflqTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371712025 170 KRPKVLLLDEPLGALD---KKLREETQFELMDLQQelglTFVVVTHDQE-EAMTMADRIAVMSHGKVVQ 234
Cdd:PRK09580  162 LEPELCILDESDSGLDidaLKIVADGVNSLRDGKR----SFIIVTHYQRiLDYIKPDYVHVLYQGRIVK 226
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 20-212 3.25e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 55.28  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFISVKNVTKKFGD---FTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLAGFEQPTSGEIILDGQ-SLAGIppyrr 95
Cdd:PRK13545   18 NKPFDKLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAI----- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  96 pvnmmfqSYALFPHMT-VENNVAFGLKQdGMPKADIAERVAQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKV 174
Cdd:PRK13545   93 -------SSGLNGQLTgIENIELKGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371712025 175 LLLDEPLGALDKKLREETqFELMDLQQELGLTFVVVTH 212
Cdd:PRK13545  165 LVIDEALSVGDQTFTKKC-LDKMNEFKEQGKTIFFISH 201
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 154-247 1.01e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 53.86  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSL-AKRPKVL-LLDEPLGALDKKLREETQFELMDLqQELGLTFVVVTHDqEEAMTMADRIAVMS--- 228
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIGpga 566

                          90       100
                  ....*....|....*....|..
gi 1371712025 229 --H-GKVVQVATPAEIYEAPNS 247
Cdd:TIGR00630 567 geHgGEVVASGTPEEILANPDS 588
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
54-213 1.37e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 53.27  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  54 LLGASGCGKSTLLRMLAG--------FEQPTSGEIILDgqslagippyrrpvnmMFQSYALFPHMT--VENNVAFGLK-Q 122
Cdd:PRK13409  104 ILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLK----------------RFRGTELQNYFKklYNGEIKVVHKpQ 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 123 --DGMPKA------DIAERVA------QMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKL 188
Cdd:PRK13409  168 yvDLIPKVfkgkvrELLKKVDergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247

                         170       180
                  ....*....|....*....|....*..
gi 1371712025 189 ReetqFELMDLQQEL--GLTFVVVTHD 213
Cdd:PRK13409  248 R----LNVARLIRELaeGKYVLVVEHD 270
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 20-185 1.52e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 52.97  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  20 SKPFIsvKNVTKKFGDFtavddlslNIYtreffALLGASGCGKSTLLRMLAGFEQPTSGEIILD-GQSLA-------GIP 91
Cdd:PRK15064   13 AKPLF--ENISVKFGGG--------NRY-----GLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGklrqdqfAFE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  92 PYR-RPVNMMFQS------------YALfPHMTVEnnvafglkqDGMPKADIAERVAQM-----------LKL---VKLE 144
Cdd:PRK15064   78 EFTvLDTVIMGHTelwevkqerdriYAL-PEMSEE---------DGMKVADLEVKFAEMdgytaearageLLLgvgIPEE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1371712025 145 KfakrkpH-----QLSGGQRQRVALARSLAKRPKVLLLDEPLGALD 185
Cdd:PRK15064  148 Q------HyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 51-224 5.43e-07

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: 49.53  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  51 FFALLGASGCGKSTLLRML--AGF-EQPTSGEIILDGQSLAGIPPYRRPVNMMFQS-----YALFPHMTVENNVAFgLKQ 122
Cdd:cd03240    24 LTLIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF-CHQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 123 DgmpkaDIAERVAQMLKlvklekfakrkphQLSGGQRQ------RVALARSLAKRPKVLLLDEPLGALDKKLREETQFEL 196
Cdd:cd03240   103 G-----ESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEI 164

                         170       180
                  ....*....|....*....|....*....
gi 1371712025 197 MDLQQELG-LTFVVVTHDqEEAMTMADRI 224
Cdd:cd03240   165 IEERKSQKnFQLIVITHD-EELVDAADHI 192
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
154-247 6.10e-07

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 51.57  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSL-AKRPKVL-LLDEP------------LGALdKKLReetqfelmdlqqELGLTFVVVTHDqEEAMT 219
Cdd:COG0178   486 LSGGEAQRIRLATQIgSGLVGVLyVLDEPsiglhqrdndrlIETL-KRLR------------DLGNTVIVVEHD-EDTIR 551

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1371712025 220 MADRIAVM-----SH-GKVVQVATPAEIYEAPNS 247
Cdd:COG0178   552 AADYIIDIgpgagEHgGEVVAQGTPEEILKNPDS 585
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 41-230 7.38e-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: 48.86  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  41 DLSLNIYTREFFALLGASGCGKSTLLrmLAGFEQPTSGEIILDGQSlagipPYRRPVNMMFQSYALfphmtVENNvafgl 120
Cdd:cd03238    13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLPK-----FSRNKLIFIDQLQFL-----IDVG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 121 kqdgmpkadiaervaqmLKLVKLEkfakRKPHQLSGGQRQRVALARSLAKRPK--VLLLDEPLGALDkklrEETQFELMD 198
Cdd:cd03238    76 -----------------LGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH----QQDINQLLE 130

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371712025 199 LQQEL---GLTFVVVTHDqEEAMTMADRIAVMSHG 230
Cdd:cd03238   131 VIKGLidlGNTVILIEHN-LDVLSSADWIIDFGPG 164
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 53-213 8.02e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 50.94  E-value: 8.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  53 ALLGASGCGKSTLLRMLAG--------FEQPTSGEIILDgqslagippyrrpvnmMFQSYALFPHMT--VENNVAFGLK- 121
Cdd:COG1245   103 GILGPNGIGKSTALKILSGelkpnlgdYDEEPSWDEVLK----------------RFRGTELQDYFKklANGEIKVAHKp 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 122 Q--DGMPKA------DIAERV------AQMLKLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:COG1245   167 QyvDLIPKVfkgtvrELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246

                         170       180
                  ....*....|....*....|....*.
gi 1371712025 188 LREETQFELMDLQQElGLTFVVVTHD 213
Cdd:COG1245   247 QRLNVARLIRELAEE-GKYVLVVEHD 271
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 35-230 4.77e-06

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 46.88  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  35 DFTAVDDlslniytREFFALLGASGCGKSTllrmlagfeqptsgeiILDGQSLA--GIPPYRRPVNMMfqsYALFPHMTV 112
Cdd:cd03279    21 DFTGLDN-------NGLFLICGPTGAGKST----------------ILDAITYAlyGKTPRYGRQENL---RSVFAPGED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 113 ENNVAFGLKQDG-------MPKADIAE--RVAqMLKLVKLEKFAKRKPHQLSGGQRQRV------ALARSLAKRPKV--- 174
Cdd:cd03279    75 TAEVSFTFQLGGkkyrverSRGLDYDQftRIV-LLPQGEFDRFLARPVSTLSGGETFLAslslalALSEVLQNRGGArle 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 175 -LLLDEPLGALDKKLREETQfELMDLQQELGLTFVVVTHDQEEAMTMADRIAVMSHG 230
Cdd:cd03279   154 aLFIDEGFGTLDPEALEAVA-TALELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
GguA NF040905
sugar ABC transporter ATP-binding protein;
154-233 8.27e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.48  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRPKVLLLDEP-----LGAldkklreetQFELMDLQQEL---GLTFVVVTHDQEEAMTMADRIA 225
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIY 475


                  ....*...
gi 1371712025 226 VMSHGKVV 233
Cdd:NF040905  476 VMNEGRIT 483
PLN03073 PLN03073
ABC transporter F family; Provisional
 24-215 1.15e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  24 ISVKNVTKKFGDFTAVDDLSLNIYTREFFALLGASGCGKSTLLRMLA-----GFeqPTSGEIILDGQSLAGI-------- 90
Cdd:PLN03073  178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILHVEQEVVGDdttalqcv 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  91 --PPYRRPVNMMFQSYALFPHMTVENNVAFGLKQ----DGMPKADIAERVAQMLKLVKL--------------------E 144
Cdd:PLN03073  256 lnTDIERTQLLEEEAQLVAQQRELEFETETGKGKgankDGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsftP 335

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371712025 145 KFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDkkLREETQFELMDLQQElgLTFVVVTHDQE 215
Cdd:PLN03073  336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLLKWP--KTFIVVSHARE 402
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 152-227 2.16e-05

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: 44.27  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 152 HQLSGGQRQRVALARSLA----KRPKVLLLDEPLGALDkklREETQ--FELMDLQQELGLTFVVVTHDqEEAMTMADRIA 225
Cdd:cd03227    76 LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD---PRDGQalAEAILEHLVKGAQVIVITHL-PELAELADKLI 151


                  ..
gi 1371712025 226 VM 227
Cdd:cd03227   152 HI 153
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 130-224 4.16e-05

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 44.56  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 130 IAERVAQMLKlVKLEKFA-KRKPHQLSGGQRQRVALARSL-AKRPKVL-LLDEPLGALDKKLREETQFELMDLQQeLGLT 206
Cdd:cd03270   114 IRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRD-LGNT 191

                          90
                  ....*....|....*...
gi 1371712025 207 FVVVTHDqEEAMTMADRI 224
Cdd:cd03270   192 VLVVEHD-EDTIRAADHV 208
uvrA PRK00349
excinuclease ABC subunit UvrA;
154-247 5.76e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 45.06  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALA----RSLAKrpkVL-LLDEP------------LGALdKKLREetqfelmdlqqeLGLTFVVVTHDqEE 216
Cdd:PRK00349  490 LSGGEAQRIRLAtqigSGLTG---VLyVLDEPsiglhqrdndrlIETL-KHLRD------------LGNTLIVVEHD-ED 552

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1371712025 217 AMTMADRIAVM-----SHG-KVVQVATPAEIYEAPNS 247
Cdd:PRK00349  553 TIRAADYIVDIgpgagVHGgEVVASGTPEEIMKNPNS 589
PLN03140 PLN03140
ABC transporter G family member; Provisional
 53-187 6.05e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 45.22  E-value: 6.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025   53 ALLGASGCGKSTLLRMLAGfeQPTSGEIILDGQsLAGIPP----YRRPVNMMFQSYALFPHMTVENNVAFGL-------- 120
Cdd:PLN03140   910 ALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKkqetFARISGYCEQNDIHSPQVTVRESLIYSAflrlpkev 986

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  121 -KQDGMPKADiaeRVAQMLKLVKLEKFAKRKP--HQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKK 187
Cdd:PLN03140   987 sKEEKMMFVD---EVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 154-287 1.28e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  154 LSGGQRQRVALARSLAKRPK--VLLLDEP-LGaldkkLREETQFELMDLQQEL---GLTFVVVTHDqEEAMTMADRI--- 224
Cdd:PRK00635   477 LSGGEQERTALAKHLGAELIgiTYILDEPsIG-----LHPQDTHKLINVIKKLrdqGNTVLLVEHD-EQMISLADRIidi 550

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371712025  225 ---AVMSHGKVVQVATPAEiyeapnsrfvadfigdvniFDGKVTSAEDGYIRVETTGGIPVRMASP 287
Cdd:PRK00635   551 gpgAGIFGGEVLFNGSPRE-------------------FLAKSDSLTAKYLRQELTIPIPEKRTNS 597
PRK15177 PRK15177
Vi polysaccharide ABC transporter ATP-binding protein VexC;
50-232 2.28e-04

Vi polysaccharide ABC transporter ATP-binding protein VexC;


Pssm-ID: 185099 [Multi-domain]  Cd Length: 213  Bit Score: 41.97  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025  50 EFFALLGASGCGKSTLLRMLAGFEQPTSGEII-LDGQSLAgippyrrpvnmMFQSYALFPHMTVENNVAFGLKQDGMPKA 128
Cdd:PRK15177   14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIgLRGDALP-----------LGANSFILPGLTGEENARMMASLYGLDGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 129 DIAERVAQmlkLVKLEKFAKRKPHQLSGGQRQRVALARSLAKRPKVLLLDEPLGALDKKLREETQFELMDLQQELGLtfV 208
Cdd:PRK15177   83 EFSHFCYQ---LTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGL--I 157

                         170       180
                  ....*....|....*....|....
gi 1371712025 209 VVTHDQEEAMTMADRIAVMSHGKV 232
Cdd:PRK15177  158 VLTHNPRLIKEHCHAFGVLLHGKI 181
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 154-241 4.38e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 42.31  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKR---PKVLLLDEPLGALdkklreetQFE----LMDLQQEL---GLTFVVVTHDQeEAMTMADR 223
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL--------HFDdikkLLEVLQRLvdkGNTVVVIEHNL-DVIKTADY 900

                          90       100
                  ....*....|....*....|....
gi 1371712025 224 IAVM------SHGKVVQVATPAEI 241
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
154-235 6.81e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQ------RVALARSLAKRPKVLLLDEPLGALD----KKLREETQFELMDLQQelgltFVVVTHDqEEAMTMADR 223
Cdd:PRK03918  789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQ-----VIIVSHD-EELKDAADY 862

                          90
                  ....*....|...
gi 1371712025 224 -IAVMSHGKVVQV 235
Cdd:PRK03918  863 vIRVSLEGGVSKV 875
uvrA PRK00349
excinuclease ABC subunit UvrA;
154-247 1.59e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRP--KVL-LLDEPLGAL---D-KKLreetqfeLMDLQQ--ELGLTFVVVTHDQeEAMTMADRI 224
Cdd:PRK00349  831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLhfeDiRKL-------LEVLHRlvDKGNTVVVIEHNL-DVIKTADWI 902

                          90       100
                  ....*....|....*....|....*....
gi 1371712025 225 AVM------SHGKVVQVATPAEIYEAPNS 247
Cdd:PRK00349  903 IDLgpeggdGGGEIVATGTPEEVAKVEAS 931
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
154-180 1.67e-03

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 40.39  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1371712025 154 LSGGQRQRVALARSLAKRPK---VLLLDEP 180
Cdd:COG0178   827 LSGGEAQRVKLASELSKRSTgktLYILDEP 856
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 154-213 7.32e-03

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: 37.59  E-value: 7.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371712025 154 LSGGQRQRVALARSLAKR---PKVLLLDEPLGALD----KKLreetqFELMDLQQELGLTFVVVTHD 213
Cdd:cd03271   170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHfhdvKKL-----LEVLQRLVDKGNTVVVIEHN 231
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
127-213 7.94e-03

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 37.30  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371712025 127 KADIAERVAQMLKLVKLEK--FAK----RKPHQLSGGQRQRVALARSLAkrpkvLLLDepLGALDkklrEETQFELMDLQ 200
Cdd:COG0419   126 EEALESALEELAELQKLKQeiLAQlsglDPIETLSGGERLRLALADLLS-----LILD--FGSLD----EERLERLLDAL 194

                          90
                  ....*....|...
gi 1371712025 201 QELGltfvVVTHD 213
Cdd:COG0419   195 EELA----IITHV 203
 
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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