NCBI Conserved Domain Search

Conserved domains on [gi|2051267523|ref|WP_215807822|]

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putative 2-aminoethylphosphonate ABC transporter ATP-binding protein [Aeromonas jandaei]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

P-loop_NTPase super family

cl38936

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...

3-360

1.13e-174

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

The actual alignment was detected with superfamily member TIGR03265:

Pssm-ID: 476819 [Multi-domain] Cd Length: 353 Bit Score: 489.55 E-value: 1.13e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIV 82
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFL 242
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 243 DTLVLSPTQVRLNEQPLQLANQAA-AGSKLQVAIRPEAITLSAPSElslGQHGIEATIDQVEFLGAAQRLICTADTyLGP 321
Cdd:TIGR03265 242 PGTRGGGSRARVGGLTLACAPGLAqPGASVRLAVRPEDIRVSPAGN---AANLLLARVEDMEFLGAFYRLRLRLEG-LPG 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2051267523 322 QQILVERPTHELPRHeqgGWRSGMRCSLHWPAGAMQLFE 360
Cdd:TIGR03265 318 QALVADVSASEVERL---GIRAGQPIWIELPAERLRAFA 353

Name

Accession

Description

Interval

E-value

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

3-360

1.13e-174

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: 489.55 E-value: 1.13e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIV 82
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFL 242
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 243 DTLVLSPTQVRLNEQPLQLANQAA-AGSKLQVAIRPEAITLSAPSElslGQHGIEATIDQVEFLGAAQRLICTADTyLGP 321
Cdd:TIGR03265 242 PGTRGGGSRARVGGLTLACAPGLAqPGASVRLAVRPEDIRVSPAGN---AANLLLARVEDMEFLGAFYRLRLRLEG-LPG 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2051267523 322 QQILVERPTHELPRHeqgGWRSGMRCSLHWPAGAMQLFE 360
Cdd:TIGR03265 318 QALVADVSASEVERL---GIRAGQPIWIELPAERLRAFA 353

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

1-360

9.36e-174

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 486.91 E-value: 9.36e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFG 80
Cdd:COG3842     1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAlalspgllllD 160
Cdd:COG3842    81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAlapeprvlllD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:COG3842   161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 241 FLDTLVLS--PTQVRLNEQPLQLANQA--AAGSKLQVAIRPEAITLSAPSElslgQHGIEATIDQVEFLGAAQRLICTAD 316
Cdd:COG3842   241 LLPGTVLGdeGGGVRTGGRTLEVPADAglAAGGPVTVAIRPEDIRLSPEGP----ENGLPGTVEDVVFLGSHVRYRVRLG 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2051267523 317 tylGPQQILVERPTHELPRHEQggwrsGMRCSLHWPAGAMQLFE 360
Cdd:COG3842   317 ---DGQELVVRVPNRAALPLEP-----GDRVGLSWDPEDVVVLP 352

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

6-237

1.71e-119

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: 344.99 E-value: 1.71e-119

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVG 237
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

ugpC

PRK11650

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

6-362

2.42e-113

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 333.73 E-value: 2.42e-113

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQ 84
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGT--MNFL 242
Cdd:PRK11650  164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 243 DTLVL-SPTQVRLNEQ---PLQLANQAAAGSKLQVAIRPEAITLSApselslGQHGIEATIDQVEFLGAAQRLICTadty 318
Cdd:PRK11650  244 DGRVSaDGAAFELAGGialPLGGGYRQYAGRKLTLGIRPEHIALSS------AEGGVPLTVDTVELLGADNLAHGR---- 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2051267523 319 LGPQQILVERPTHELPrheqggwRSGMRCSLHWPAGAMQLFEGD 362
Cdd:PRK11650  314 WGGQPLVVRLPHQERP-------AAGSTLWLHLPANQLHLFDAD 350

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

6-312

1.67e-88

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 270.41 E-value: 1.67e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQaLKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFLD-- 243
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgv 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 244 -TLVLSPTQVRLNEQPLQLANQAAAgsKLQVAIRPEAITLSAPSELSLGQHGIEATIDQVEFLGAAQRLI 312
Cdd:NF040840  241 aEKGGEGTILDTGNIKIELPEEKKG--KVRIGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKLT 308

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

19-214

5.66e-45

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 153.72 E-value: 5.66e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDF-GIVFQSYALFPNL 92
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQkiilrRELiGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:NF038007   99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2051267523 173 HLRSEIRALQQRlGITTIMVTHdQEEALTMADRIVVMEGGRI 214
Cdd:NF038007  179 AVLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDGKL 218

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

21-164

1.73e-39

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: 137.39 E-value: 1.73e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNLTVAQNI 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFGLENQGLARDLIKERVD---HWLGLVDLTAQS-HKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEealEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

15-209

5.39e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 5.39e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  15 FGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGivfqsyALFPnLTV 94
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  95 AQNIAFGL-ENQGLARDLIKE---RVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALV 170
Cdd:NF040873   75 RDLVAMGRwARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2051267523 171 RTHLRSEIRALQQRlGITTIMVTHDQEEALTmADRIVVM 209
Cdd:NF040873  155 RERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

9-223

2.62e-17

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 2.62e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   9 QHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnisqlPPQQRDF------GIV 82
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ-----PVDAGDIatrrrvGYM 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIA-----FglenqGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:NF033858  345 SQAFSLYGELTVRQNLElharlF-----HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 158 LLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEI 223
Cdd:NF033858  420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484

GguA

NF040905

sugar ABC transporter ATP-binding protein;

6-216

1.41e-12

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 1.41e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD---SGEIWQGG-----RNISQlppqQR 77
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGevcrfKDIRD----SE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVF--QSYALFPNLTVAQNIAFGLENQ--GL---------ARDLIKErvdhwlglVDLTAQSHKYPSQISGGQQQRV 144
Cdd:NF040905   77 ALGIVIihQELALIPYLSIAENIFLGNERAkrGVidwnetnrrARELLAK--------VGLDESPDTLVTDIGVGKQQLV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQ 216
Cdd:NF040905  149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219

40850658_otr

NF000106

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

6-255

3.39e-12

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 3.39e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCG--KTTLLRAIAGldlPDSGE-IWQGGRNISQLPPQQRDFGI- 81
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrPWRF*TWCANRRALRRTIG*h 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 ------VFQSYALFPNLTVaqnIAFGLEnqgLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPG 155
Cdd:NF000106   91 rpvr*gRRESFSGRENLYM---IGR*LD---LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 156 LLLLDEPLSALDALVRTHLRSEIRALqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASF 235
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIR 243

                         250       260
                  ....*....|....*....|
gi 2051267523 236 VGTMNFLDTLVLSPTQVRLN 255
Cdd:NF000106  244 PAHAAELDRMVGAIAQAGLD 263

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

8-223

9.55e-10

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 9.55e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-----------------------Q 64
Cdd:NF033858    4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhrravcpriaympQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  65 G-GRNisqlppqqrdfgivfqsyaLFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQR 143
Cdd:NF033858   84 GlGKN-------------------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDALVRTH---LRSEIRAlqQRLGITTIMVTHDQEEALTMaDRIVVMEGGRIVQVGTP 220
Cdd:NF033858  145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221


                  ...
gi 2051267523 221 QEI 223
Cdd:NF033858  222 AEL 224

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

30-206

1.56e-07

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: 50.06 E-value: 1.56e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   30 PGEFICFLGPSGCGKTTLLRAIAGldlpdsgeiwqggrnisQLPPQQRDFGIVfqsyalfpnltvaqNIAFGLENQGLAR 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-----------------ELGPPGGGVIYI--------------DGEDILEEVLDQL 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  110 DLIKERVDHWLGlvdltaqshkypsqiSGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRA-----LQQR 184
Cdd:smart00382  50 LLIIVGGKKASG---------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114

                          170       180
                   ....*....|....*....|..
gi 2051267523  185 LGITTIMVTHDQEEALTMADRI 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136

Name

Accession

Description

Interval

E-value

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

3-360

1.13e-174

Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 489.55 E-value: 1.13e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIV 82
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFL 242
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 243 DTLVLSPTQVRLNEQPLQLANQAA-AGSKLQVAIRPEAITLSAPSElslGQHGIEATIDQVEFLGAAQRLICTADTyLGP 321
Cdd:TIGR03265 242 PGTRGGGSRARVGGLTLACAPGLAqPGASVRLAVRPEDIRVSPAGN---AANLLLARVEDMEFLGAFYRLRLRLEG-LPG 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2051267523 322 QQILVERPTHELPRHeqgGWRSGMRCSLHWPAGAMQLFE 360
Cdd:TIGR03265 318 QALVADVSASEVERL---GIRAGQPIWIELPAERLRAFA 353

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

1-360

9.36e-174

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 486.91 E-value: 9.36e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFG 80
Cdd:COG3842     1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAlalspgllllD 160
Cdd:COG3842    81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAlapeprvlllD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:COG3842   161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 241 FLDTLVLS--PTQVRLNEQPLQLANQA--AAGSKLQVAIRPEAITLSAPSElslgQHGIEATIDQVEFLGAAQRLICTAD 316
Cdd:COG3842   241 LLPGTVLGdeGGGVRTGGRTLEVPADAglAAGGPVTVAIRPEDIRLSPEGP----ENGLPGTVEDVVFLGSHVRYRVRLG 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2051267523 317 tylGPQQILVERPTHELPRHEQggwrsGMRCSLHWPAGAMQLFE 360
Cdd:COG3842   317 ---DGQELVVRVPNRAALPLEP-----GDRVGLSWDPEDVVVLP 352

MalK

COG3839

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

6-362

4.14e-155

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 439.89 E-value: 4.14e-155

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:COG3839    84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGT--MNFLD 243
Cdd:COG3839   164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 244 tLVLSPTQVRLNEQPLQL--ANQAAAGSKLQVAIRPEAITLSAPselslGQHGIEATIDQVEFLGAAQRLICTadtyLGP 321
Cdd:COG3839   244 -GTVEGGGVRLGGVRLPLpaALAAAAGGEVTLGIRPEHLRLADE-----GDGGLEATVEVVEPLGSETLVHVR----LGG 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2051267523 322 QQILVERPTHELPrheqggwRSGMRCSLHWPAGAMQLFEGD 362
Cdd:COG3839   314 QELVARVPGDTRL-------RPGDTVRLAFDPERLHLFDAE 347

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

6-311

1.00e-131

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 380.26 E-value: 1.00e-131

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-SQLPPQQRDFGIVFQ 84
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFLDT 244
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 245 LVLSPtQVRLNEQPLQLANQAAAGSKlQVAIRPEAITLSAPSElslGQHGIEATIDQVEFLGAAQRL 311
Cdd:COG1118   243 RVIGG-QLEADGLTLPVAEPLPDGPA-VAGVRPHDIEVSREPE---GENTFPATVARVSELGPEVRV 304

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

6-237

1.71e-119

Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 344.99 E-value: 1.71e-119

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVG 237
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

ugpC

PRK11650

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

6-362

2.42e-113

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 333.73 E-value: 2.42e-113

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQ 84
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGT--MNFL 242
Cdd:PRK11650  164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 243 DTLVL-SPTQVRLNEQ---PLQLANQAAAGSKLQVAIRPEAITLSApselslGQHGIEATIDQVEFLGAAQRLICTadty 318
Cdd:PRK11650  244 DGRVSaDGAAFELAGGialPLGGGYRQYAGRKLTLGIRPEHIALSS------AEGGVPLTVDTVELLGADNLAHGR---- 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2051267523 319 LGPQQILVERPTHELPrheqggwRSGMRCSLHWPAGAMQLFEGD 362
Cdd:PRK11650  314 WGGQPLVVRLPHQERP-------AAGSTLWLHLPANQLHLFDAD 350

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

1-280

3.78e-112

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 331.53 E-value: 3.78e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFG 80
Cdd:PRK09452   10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK09452   90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:PRK09452  170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 241 FLDTLVLSptqvRLNEQ-----------PLQLANQAAAGSKLQVAIRPEAI 280
Cdd:PRK09452  250 IFDATVIE----RLDEQrvranvegrecNIYVNFAVEPGQKLHVLLRPEDL 296

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

6-218

6.69e-106

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

Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 309.45 E-value: 6.69e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

1-322

3.27e-102

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 305.49 E-value: 3.27e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFG 80
Cdd:PRK11432    2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK11432   82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:PRK11432  162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDAN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 241 FLDTlVLSPTQVRLNEQPLQLANQAAAG---SKLQVAIRPEAITLSapselslgQHGIEatidqveflgaAQRLICTADT 317
Cdd:PRK11432  242 IFPA-TLSGDYVDIYGYRLPRPAAFAFNlpdGECTVGVRPEAITLS--------EQGEE-----------SQRCTIKHVA 301


                  ....*
gi 2051267523 318 YLGPQ 322
Cdd:PRK11432  302 YMGPQ 306

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

8-237

3.73e-102

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: 301.18 E-value: 3.73e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYA 87
Cdd:cd03296     5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  88 LFPNLTVAQNIAFGLENQGLAR----DLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:cd03296    85 LFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 164 SALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVG 237
Cdd:cd03296   165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238

3a0106s01

TIGR00968

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

8-242

2.05e-97

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

Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 289.01 E-value: 2.05e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYA 87
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  88 LFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:TIGR00968  83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 168 ALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFL 242
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

1-217

6.16e-97

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 288.53 E-value: 6.16e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQ--PYLDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP 74
Cdd:COG1116     1 MSAaaPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 qqrDFGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSP 154
Cdd:COG1116    81 ---DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG--GRIVQV 217
Cdd:COG1116   158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

37-306

6.91e-96

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: 288.24 E-value: 6.91e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  37 LGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERV 116
Cdd:TIGR01187   2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 117 DHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQ 196
Cdd:TIGR01187  82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 197 EEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFLDTLVL---SPTQVRLN-EQPLQLANQAA---AGS 269
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIerkSEQVVLAGvEGRRCDIYTDVpveKDQ 241

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2051267523 270 KLQVAIRPEAITLSAPSELSlGQHGIEATIDQVEFLG 306
Cdd:TIGR01187 242 PLHVVLRPEKIVIEEEDEAN-SSNAIIGHVIDITYLG 277

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

6-218

1.18e-95

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: 283.76 E-value: 1.18e-95

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

13-306

2.55e-94

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 285.77 E-value: 2.55e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYALFPNL 92
Cdd:PRK11000   11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:PRK11000   91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 173 HLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGT--MNFLDTLVLS-- 248
Cdd:PRK11000  171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkMNFLPVKVTAta 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 249 PTQVRL---NEQPLQL---ANQAAAGSKLQVAIRPEAITLSAPSELSLgqhgiEATIDQVEFLG 306
Cdd:PRK11000  251 IEQVQVelpNRQQVWLpveGRGVQVGANMSLGIRPEHLLPSDIADVTL-----EGEVQVVEQLG 309

OpuBA

COG1125

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

8-276

1.23e-91

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

Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 276.59 E-value: 1.23e-91

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQ 84
Cdd:COG1125     4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQS--HKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:COG1125    84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTmnfl 242
Cdd:COG1125   164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA---- 239

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2051267523 243 DTLVLSPTQVRLNEQPLQLANQAAAGSKLQVAIR 276
Cdd:COG1125   240 DRGLRRLSLLRVEDLMLPEPPTVSPDASLREALS 273

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

6-217

7.13e-90

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

Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 268.96 E-value: 7.13e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPqqrDFGI 81
Cdd:cd03293     1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG--GRIVQV 217
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

1-282

1.58e-88

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 271.32 E-value: 1.58e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFG 80
Cdd:PRK11607   15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK11607   95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:PRK11607  175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 241 FL---------DTLVL-SPTQVrlneQPLQLANQAAA--GSKLQVAIRPEAITL 282
Cdd:PRK11607  255 VFegvlkerqeDGLVIdSPGLV----HPLKVDADASVvdNVPVHVALRPEKIML 304

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

6-312

1.67e-88

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 270.41 E-value: 1.67e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQaLKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFLD-- 243
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgv 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 244 -TLVLSPTQVRLNEQPLQLANQAAAgsKLQVAIRPEAITLSAPSELSLGQHGIEATIDQVEFLGAAQRLI 312
Cdd:NF040840  241 aEKGGEGTILDTGNIKIELPEEKKG--KVRIGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKLT 308

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

6-289

5.80e-87

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 266.56 E-value: 5.80e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGL----ENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK10851   83 YALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNF 241
Cdd:PRK10851  163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 242 LDTLVLSpTQVRLNEQPLQLANQAAAGSKLQVAIRPEAITLSAPSELS 289
Cdd:PRK10851  243 LQGTIRG-GQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLD 289

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

6-240

8.35e-83

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: 251.87 E-value: 8.35e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQaLKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03299     1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMN 240
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

6-237

8.67e-83

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: 251.84 E-value: 8.67e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA-FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIV 82
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQS--HKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVG 237
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

1-225

8.06e-82

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: 249.13 E-value: 8.06e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD-- 78
Cdd:COG1127     1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 ---FGIVFQSYALFPNLTVAQNIAFGL-ENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAlalsp 154
Cdd:COG1127    81 rrrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAlaldp 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 155 gllllDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYH 225
Cdd:COG1127   161 eillyDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

13-236

3.89e-77

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 238.31 E-value: 3.89e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ------RDFGIVFQSY 86
Cdd:cd03294    32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 ALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:cd03294   112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 167 DALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFV 236
Cdd:cd03294   192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

6-239

1.95e-76

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 235.27 E-value: 1.95e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS----QLPPQQRDFGI 81
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLEN-QGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALD-ALVRTHLRSeIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTM 239
Cdd:COG1126   162 EPTSALDpELVGEVLDV-MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

6-223

4.54e-75

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: 232.01 E-value: 4.54e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDFG 80
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGL-ENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224

LolD

COG1136

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

3-215

5.50e-75

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 231.47 E-value: 5.50e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD 78
Cdd:COG1136     2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 ------FGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALAL 152
Cdd:COG1136    82 rlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 153 SPGLLLLDEPLSALDalvrTHLRSEI----RALQQRLGITTIMVTHDqEEALTMADRIVVMEGGRIV 215
Cdd:COG1136   162 RPKLILADEPTGNLD----SKTGEEVlellRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

6-214

4.04e-72

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: 223.52 E-value: 4.04e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA----FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD--- 78
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 ---FGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPG 155
Cdd:cd03255    81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 156 LLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALtMADRIVVMEGGRI 214
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218

proV

TIGR01186

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...

13-276

5.65e-71

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: 225.89 E-value: 5.65e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ------RDFGIVFQSY 86
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 ALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 167 DALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGTMNFLDTLV 246
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2051267523 247 LSPTQVRLNEQPLQLanqaAAGSKLQVAIR 276
Cdd:TIGR01186 241 AERIAQRMNTGPITK----TADKGPRSALQ 266

AbcC

COG1135

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

8-299

1.49e-69

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 221.10 E-value: 1.49e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RD 78
Cdd:COG1135     4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:COG1135    84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 159 LDEPLSALD--------ALVRthlrsEIRalqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:COG1135   164 CDEATSALDpettrsilDLLK-----DIN---RELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 231 FVASFVGTmnfldtlvlsPTQVRLNEQPLQ-LANQAAAGSKLQVAIRPEAITLSAPSELSlGQHGIEATI 299
Cdd:COG1135   236 LTRRFLPT----------VLNDELPEELLArLREAAGGGRLVRLTFVGESADEPLLSELA-RRFGVDVNI 294

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

16-227

4.94e-69

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: 216.04 E-value: 4.94e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQS--YALFpN 91
Cdd:COG1122    12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:COG1122    91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 172 THLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:COG1122   171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

6-213

1.06e-68

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: 213.59 E-value: 1.06e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI----SQLPPQQRDFGI 81
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLenqglardlikervdhwlglvdltaqshkypsqiSGGQQQRVALARALALSPGLLLLDE 161
Cdd:cd03229    81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

1-227

8.57e-68

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: 221.70 E-value: 8.57e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF-----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ 75
Cdd:COG1123   256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 Q-----RDFGIVFQ--SYALFPNLTVAQNIAFGLENQGLA-RDLIKERVDHWLGLVDLTAQS-HKYPSQISGGQQQRVAL 146
Cdd:COG1123   336 SlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPDLaDRYPHELSGGQRQRVAI 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 147 ARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:COG1123   416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495


                  .
gi 2051267523 227 P 227
Cdd:COG1123   496 P 496

CcmA

COG1131

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

6-226

2.39e-66

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.53 E-value: 2.39e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFGIVFQ 84
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 165 ALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

12-218

5.12e-66

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: 207.92 E-value: 5.12e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  12 NKQFGAFQaLKgISLTIePGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI------WQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03297     7 EKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRKIGLVFQQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLenQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03297    84 YALFPHLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03297   162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

6-327

1.12e-64

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis

Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 209.19 E-value: 1.12e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQhLNKQFGAFqALKgISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI------WQGGRNISQLPPQQRDF 79
Cdd:COG4148     3 LEVD-FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQDSARGIFLPPHRRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFGLENQGLARDLIK-ERVDHWLGLVDLTAQshkYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:COG4148    80 GYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISfDEVVELLGIGHLLDR---RPATLSGGERQRVAIGRALLSSPRLLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 159 LDEPLSALDAlvrtHLRSEI----RALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVAS 234
Cdd:COG4148   157 MDEPLAALDL----ARKAEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 235 FVGTMNFLDTLVLSP------TQVRLNEQPLQLANQAAA-GSKLQVAIRPE--AITLSAPSELSLgQHGIEATIDQVEFL 305
Cdd:COG4148   233 GEEAGSVLEATVAAHdpdyglTRLALGGGRLWVPRLDLPpGTRVRVRIRARdvSLALEPPEGSSI-LNILPGRVVEIEPA 311

                         330       340
                  ....*....|....*....|..
gi 2051267523 306 GAAQRLICTAdtyLGPQQILVE 327
Cdd:COG4148   312 DGGQVLVRLD---LGGQTLLAR 330

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

3-229

2.19e-64

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: 212.84 E-value: 2.19e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQF--GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD----SGEIWQGGRNISQLPPQQ 76
Cdd:COG1123     2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHggriSGEVLLDGRDLLELSEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 R--DFGIVFQS--YALFPnLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALAL 152
Cdd:COG1123    81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 153 SPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPAS 229
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

8-227

2.85e-64

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: 203.97 E-value: 2.85e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP-----QQRD 78
Cdd:cd03258     4 LKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkARRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:cd03258    84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 159 LDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:cd03258   164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

6-214

2.93e-63

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: 200.83 E-value: 2.93e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ----QRDFGI 81
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLEN-QGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 161 EPLSALDA-LVRTHLRSeIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:cd03262   161 EPTSALDPeLVGEVLDV-MKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213

FtsE

COG2884

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

8-218

4.23e-63

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 200.66 E-value: 4.23e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDFGI 81
Cdd:COG2884     4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:COG2884    84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 162 PLSALDAlvrtHLRSEI-RALQQ--RLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:COG2884   164 PTGNLDP----ETSWEImELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

16-213

6.45e-61

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: 194.61 E-value: 6.45e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQsyalFP--- 90
Cdd:cd03225    12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ----NPddq 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  91 --NLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:cd03225    88 ffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2051267523 169 LVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:cd03225   168 AGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211

TauB

COG4525

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

6-217

1.13e-60

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.85 E-value: 1.13e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAF----QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQlPPQQRdfGI 81
Cdd:COG4525     4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR--GV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:COG4525    81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG--GRIVQV 217
Cdd:COG4525   161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

6-223

1.39e-60

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: 195.02 E-value: 1.39e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA----FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDF 79
Cdd:COG1124     2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSY--ALFPNLTVAQNIAFGLENQGLARdlIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGL 156
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 157 LLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

6-226

1.91e-59

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: 193.03 E-value: 1.91e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF--GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGG---RNISQLPPQQRDFG 80
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQsyalfpN-------LTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALS 153
Cdd:TIGR04520  81 MVFQ------NpdnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 154 PGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALtMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226

ThiQ

COG3840

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

6-238

8.94e-59

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.97 E-value: 8.94e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFqaLKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:COG3840     2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLeNQGL---ARDliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:COG3840    80 NNLFPHLTVAQNIGLGL-RPGLkltAEQ--RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVGT 238
Cdd:COG3840   157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

6-218

1.40e-58

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: 189.25 E-value: 1.40e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR---- 77
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 -DFGIVFQSY--ALFPNLTVAQNIAFGLENQGLARD--LIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALA 151
Cdd:cd03257    82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKkeARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 152 LSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

21-223

1.41e-57

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: 186.90 E-value: 1.41e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPqqrDFGIVFQSYALFPNLTVAQNIAF 100
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 101 GLE--NQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEI 178
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2051267523 179 RALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202

ECF_ATPase_2

TIGR04521

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

17-227

1.19e-54

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: 180.73 E-value: 1.19e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  17 AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS-----QLPPQQRDFGIVFQ--SYALF 89
Cdd:TIGR04521  17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQfpEHQLF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  90 PNlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLT-AQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:TIGR04521  97 EE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 169 LVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

6-223

8.31e-54

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: 177.36 E-value: 8.31e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFGIVFQ 84
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:COG4555    82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 165 ALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG4555   162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

4-223

1.30e-53

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.17 E-value: 1.30e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----R 77
Cdd:COG3638     1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQNIAFG-LENQGLARDLI-------KERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARA 149
Cdd:COG3638    81 RIGMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRSLLglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 150 LALSPGLLLLDEPLSALD-ALVRTHLRSeIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG3638   161 LVQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

6-223

1.73e-53

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: 176.22 E-value: 1.73e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-----DLPDSGEIWQGGRNISQLPPQ----Q 76
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 RDFGIVFQSYALFPnLTVAQNIAFGLENQGLA-RDLIKERVDHWLGLVDLTAQ--SHKYPSQISGGQQQRVALARALALS 153
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 154 PGLLLLDEPLSALDALVRTHLRSEIRALQQRlgITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

1-222

3.52e-53

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: 175.70 E-value: 3.52e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ 76
Cdd:COG4181     4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 R------DFGIVFQSYALFPNLTVAQNIAFGLENQGlARDLiKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAL 150
Cdd:COG4181    84 RarlrarHVGFVFQSFQLLPTLTALENVMLPLELAG-RRDA-RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 151 ALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALtMADRIVVMEGGRIVQVGTPQE 222
Cdd:COG4181   162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

7-234

5.69e-53

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 178.46 E-value: 5.69e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   7 DIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----R 77
Cdd:PRK11153    3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:PRK11153   83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 158 LLDEPLSALD-ALVRTHLrSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP----ASRFV 232
Cdd:PRK11153  163 LCDEATSALDpATTRSIL-ELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFI 241


                  ..
gi 2051267523 233 AS 234
Cdd:PRK11153  242 QS 243

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

6-223

6.85e-53

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

Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 175.62 E-value: 6.85e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVF 83
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 QSYALFPNLTVAQNIAFG-LENQGL-----ARDliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:COG1120    82 QEPPAPFGLTVRELVALGrYPHLGLfgrpsAED--REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 158 LLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG1120   160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

13-235

1.52e-52

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.13 E-value: 1.52e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDF----GIVFQSYAL 88
Cdd:PRK09493    9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  89 FPNLTVAQNIAFG-LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK09493   89 FPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 168 AlvrtHLRSEIRALQQRL---GITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASF 235
Cdd:PRK09493  169 P----ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

1-224

2.22e-51

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 172.51 E-value: 2.22e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF--GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-- 76
Cdd:PRK13635    1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 RDFGIVFQSY-ALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPG 155
Cdd:PRK13635   81 RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 156 LLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13635  161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

6-214

2.37e-51

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: 168.73 E-value: 2.37e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFGIVFQ 84
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFglenqglardlikervdhwlglvdltaqshkypsqiSGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:cd03230    81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2051267523 165 ALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173

FetA

COG4619

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

6-214

2.56e-51

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 2.56e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVF 83
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 QSYALFPNlTVAQNIAFGLENQGLARDliKERVDHWLGLVDLTAQSHKYP-SQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:COG4619    81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:COG4619   158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

6-228

7.21e-51

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: 172.16 E-value: 7.21e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLP----DSGEIWQGGRNISQLPPQQ- 76
Cdd:COG0444     2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGL-LPppgiTSGEILFDGEDLLKLSEKEl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 -----RDFGIVFQ-SY-ALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDLTAQS---HKYPSQISGGQQQRVA 145
Cdd:COG0444    81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYH 225
Cdd:COG0444   161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                  ...
gi 2051267523 226 QPA 228
Cdd:COG0444   241 NPR 243

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

2-228

1.24e-50

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

Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 169.83 E-value: 1.24e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFG 80
Cdd:COG0411     1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IV--FQSYALFPNLTVAQNIAFGLENQG---------------LARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQR 143
Cdd:COG0411    81 IArtFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG0411   161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240


                  ....*
gi 2051267523 224 YHQPA 228
Cdd:COG0411   241 RADPR 245

FtsE

TIGR02673

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...

6-213

1.55e-50

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

Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 168.20 E-value: 1.55e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS-----QLPPQQRDF 79
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 160 DEPLSALDAlvrtHLRSEIRALQQRL---GITTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:TIGR02673 162 DEPTGNLDP----DLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

8-219

2.93e-50

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 168.27 E-value: 2.93e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGR--NISQLP-PQQ-----RDF 79
Cdd:PRK11124    5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsDKAirelrRNV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQN-IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:PRK11124   85 GMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 159 LDEPLSALDALVRTHLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGT 219
Cdd:PRK11124  165 FDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224

AppF

COG4608

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

1-228

1.07e-49

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 169.53 E-value: 1.07e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF----GAF-------QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI 69
Cdd:COG4608     3 MAEPLLEVRDLKKHFpvrgGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  70 SQLPPQQ-----RDFGIVFQ-SYA-LFPNLTVAQNIAFGLENQGLA-RDLIKERVDHWLGLVDL-TAQSHKYPSQISGGQ 140
Cdd:COG4608    83 TGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSGGQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 141 QQRVALARALALSPGLLLLDEPLSALDAlvrthlrSeIRA--------LQQRLGITTIMVTHDqeeaLTM----ADRIVV 208
Cdd:COG4608   163 RQRIGIARALALNPKLIVCDEPVSALDV-------S-IQAqvlnlledLQDELGLTYLFISHD----LSVvrhiSDRVAV 230

                         250       260
                  ....*....|....*....|
gi 2051267523 209 MEGGRIVQVGTPQEIYHQPA 228
Cdd:COG4608   231 MYLGKIVEIAPRDELYARPL 250

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

21-222

1.25e-49

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 165.73 E-value: 1.25e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPD---SGEIWQGGRNISQLPPQQRDFGIVFQSYALFPNLTVAQN 97
Cdd:COG4136    17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENqGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAlvrtHLRSE 177
Cdd:COG4136    97 LAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA----ALRAQ 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2051267523 178 IRAL----QQRLGITTIMVTHDQEEALtmadrivvmEGGRIVQVGTPQE 222
Cdd:COG4136   172 FREFvfeqIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQH 211

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

6-223

3.31e-49

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: 165.30 E-value: 3.31e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIV-- 82
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGrt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDL----------IKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALAL 152
Cdd:cd03219    81 FQIPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 153 SPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

11-298

3.38e-49

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: 169.14 E-value: 3.38e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQaLKgISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI------WQGGRNISQLPPQQRDFGIVFQ 84
Cdd:TIGR02142   5 FSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtLFDSRKGIFLPPEKRRIGYVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLEnqglaRDLIKERVDHWLGLVDLTAQSH---KYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:TIGR02142  83 EARLFPHLSVRGNLRYGMK-----RARPSERRISFERVIELLGIGHllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVA-SFVGTMN 240
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLArEDQGSLI 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 241 FLDTLVLSP----TQVRLNEQPLQLA-NQAAAGSKLQVAIRpeaitlsaPSELSLGQHGIEAT 298
Cdd:TIGR02142 238 EGVVAEHDQhyglTALRLGGGHLWVPeNLGPTGARLRLRVP--------ARDVSLALQKPEAT 292

ArtP

COG4161

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

6-235

6.35e-49

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 6.35e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGR--NISQLPPQQ------R 77
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQN-IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGL 156
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 157 LLLDEPLSALDALVRTHLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTpQEIYHQPASRFVASF 235
Cdd:COG4161   163 LLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

6-223

1.19e-48

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 163.31 E-value: 1.19e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFGIVFQ 84
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:cd03265    81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03265   161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

6-223

1.99e-48

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: 163.51 E-value: 1.99e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA-FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP-----QQRDF 79
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFGLEN-----QGLAR---DLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALA 151
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGRLGrrstwRSLFGlfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 152 LSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03256   161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

6-214

2.96e-47

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: 159.50 E-value: 2.96e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA-FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDF 79
Cdd:cd03292     1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 160 DEPLSALDAlvrTHLRSEIRALQQ--RLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:cd03292   161 DEPTGNLDP---DTTWEIMNLLKKinKAGTTVVVATHAKELVDTTRHRVIALERGKL 214

HisP

COG4598

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

2-234

9.68e-47

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.58 E-value: 9.68e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLP-------- 73
Cdd:COG4598     5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvp 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  74 --PQQRD-----FGIVFQSYALFPNLTVAQNIAFG-LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVA 145
Cdd:COG4598    85 adRRQLQrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLLLDEPLSALDA-LVRTHLRSeIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:COG4598   165 IARALAMEPEVMLFDEPTSALDPeLVGEVLKV-MRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242

                         250
                  ....*....|....
gi 2051267523 225 HQPAS----RFVAS 234
Cdd:COG4598   243 GNPKSerlrQFLSS 256

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

6-216

3.09e-46

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 158.32 E-value: 3.09e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQlPPQQRdfGIVFQS 85
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVME--GGRIVQ 216
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

7-218

4.22e-46

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: 155.29 E-value: 4.22e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   7 DIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRdfgivfqsy 86
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 alfpnltvAQNIAFglenqglardlikerVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:cd03214    72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 167 DALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03214   129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

6-223

6.68e-46

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: 156.13 E-value: 6.68e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG--AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-SQLPPQQRDFGIV 82
Cdd:cd03263     1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGIttIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219

PRK11264

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

6-227

1.10e-45

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.83 E-value: 1.10e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQG------GRNISQLPPQQRDF 79
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIRQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 ----GIVFQSYALFPNLTVAQNIAFG-LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSP 154
Cdd:PRK11264   84 rqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK11264  164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235

ABC_phnC

TIGR02315

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...

6-226

3.78e-45

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]

Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 155.15 E-value: 3.78e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG-AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-----QRDF 79
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFG-LENQGLARDLI-------KERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALA 151
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLLgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 152 LSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

6-214

4.82e-45

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 155.22 E-value: 4.82e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLppqQRDFGIVFQS 85
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLenQGLARDLIKERvdhwLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:PRK11247   90 ARLLPWKKVIDNVGLGL--KGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK11247  164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

19-214

5.66e-45

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 153.72 E-value: 5.66e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDF-GIVFQSYALFPNL 92
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQkiilrRELiGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:NF038007   99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2051267523 173 HLRSEIRALQQRlGITTIMVTHdQEEALTMADRIVVMEGGRI 214
Cdd:NF038007  179 AVLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDGKL 218

PRK10070

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

20-235

1.57e-44

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 157.89 E-value: 1.57e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP------QQRDFGIVFQSYALFPNLT 93
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 174 LRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASF 235
Cdd:PRK10070  203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

9-230

1.63e-44

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 153.20 E-value: 1.63e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   9 QHLNKQFgafqalkgiSLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYAL 88
Cdd:PRK10771   12 HHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  89 FPNLTVAQNIAFGLeNQGLARDLI-KERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK10771   83 FSHLTVAQNIGLGL-NPGLKLNAAqREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 168 ALvrthLRSEIRAL-----QQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY--HQPASR 230
Cdd:PRK10771  162 PA----LRQEMLTLvsqvcQER-QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLsgKASASA 226

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

25-218

3.85e-44

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: 151.55 E-value: 3.85e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  25 SLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYALFPNLTVAQNIAFGLeN 104
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL-H 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 105 QGLARDLIK----ERVDHWLGLVDLTAqshKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRA 180
Cdd:TIGR01277  97 PGLKLNAEQqekvVDAAQQVGIADYLD---RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2051267523 181 LQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

11-227

7.38e-44

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: 158.69 E-value: 7.38e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPPQQ-----RDFGIVFQS 85
Cdd:COG4172   292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQD 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 -YA-LFPNLTVAQNIAFGLE--NQGLARDLIKERVDHWLGLVDLTAQS-HKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:COG4172   371 pFGsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:COG4172   451 EPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517

cbiO

PRK13637

energy-coupling factor transporter ATPase;

20-226

1.16e-43

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.51 E-value: 1.16e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS----QLPPQQRDFGIVFQ--SYALFPNlT 93
Cdd:PRK13637   22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEE-T 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHK--YPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK13637  101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 172 THLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK13637  181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

6-223

1.37e-43

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.

Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 150.28 E-value: 1.37e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIVF- 83
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRAGIGYv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 -QSYALFPNLTVAQNIAFGLENqgLARDLIKERVDHWLGLV-DLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:cd03224    81 pEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

25-218

2.74e-43

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: 149.18 E-value: 2.74e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  25 SLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYALFPNLTVAQNIAFGLEN 104
Cdd:cd03298    18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 105 QGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQR 184
Cdd:cd03298    98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2051267523 185 LGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03298   178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211

3a0107s01c2

TIGR00972

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...

6-236

3.02e-43

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

Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 150.14 E-value: 3.02e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DLPD----SGEIWQGGRNISQlppQQRD-- 78
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQDIYD---KKIDvv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 -----FGIVFQSYALFPnLTVAQNIAFGLENQGL-ARDLIKERVDHWL---GLVD-LTAQSHKYPSQISGGQQQRVALAR 148
Cdd:TIGR00972  79 elrrrVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLkkaALWDeVKDRLHDSALGLSGGQQQRLCIAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 149 ALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPA 228
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPK 235


                  ....*...
gi 2051267523 229 SRFVASFV 236
Cdd:TIGR00972 236 EKRTEDYI 243

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

20-223

4.93e-43

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

Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 158.46 E-value: 4.93e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFpNLTVAQN 97
Cdd:COG2274   490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGlenqglARDLIKERVDHWLGLVDLT----AQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:COG2274   569 ITLG------DPDATDEEIIEAARLAGLHdfieALPMGYDTVVgeggsnlSGGQRQRLAIARALLRNPRILILDEATSAL 642

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 167 DAlvrthlRSE---IRALQQRL-GITTIMVTHDqEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG2274   643 DA------ETEaiiLENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696

ZnuC

COG1121

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

1-223

7.72e-43

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 7.72e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLP------P 74
Cdd:COG1121     2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 QQRDFGivfqsyALFPnLTVAQNIAFGLENQ-GLARDL---IKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAL 150
Cdd:COG1121    82 QRAEVD------WDFP-ITVRDVVLMGRYGRrGLFRRPsraDREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 151 ALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQvGTPQEI 223
Cdd:COG1121   155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

6-230

1.56e-42

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: 147.69 E-value: 1.56e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIVF- 83
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 -QSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:cd03218    81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRlGItTIMVT-HDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDR-GI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

6-213

2.06e-41

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: 144.16 E-value: 2.06e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFGIVFQ 84
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:COG4133    83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGItTIMVTHDQEEALtmADRIVVMEGGR 213
Cdd:COG4133   161 ALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELA--AARVLDLGDFK 206

L_ocin_972_ABC

TIGR03608

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...

8-207

2.29e-41

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: 143.91 E-value: 2.29e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDF-GI 81
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREKlGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEAlTMADRIV 207
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRVI 204

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

6-218

3.41e-41

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

Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 143.58 E-value: 3.41e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPpqQRDFGIVFQS 85
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 166 LDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03269   159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

19-213

6.97e-41

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

Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 141.37 E-value: 6.97e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQ 96
Cdd:cd03228    16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLF-SGTIRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIafglenqglardlikervdhwlglvdltaqshkypsqISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRS 176
Cdd:cd03228    95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2051267523 177 EIRALQQrlGITTIMVTHDqEEALTMADRIVVMEGGR 213
Cdd:cd03228   138 ALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

6-218

1.54e-40

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: 142.12 E-value: 1.54e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA----FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFG 80
Cdd:cd03266     2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 161 EPLSALDALVRTHLRSEIRALqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03266   162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218

PhnK

COG1101

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

6-215

1.66e-40

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 143.30 E-value: 1.66e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGA-----FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR--D 78
Cdd:COG1101     2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYAL--FPNLTVAQNIAFGL---ENQGLARDLIKERVDHW--------LGLVD-LTAQShkypSQISGGQQQRV 144
Cdd:COG1101    82 IGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFrellatlgLGLENrLDTKV----GLLSGGQRQAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 145 ALARALALSPGLLLLDEPLSALD----ALVrTHLRSEIralQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:COG1101   158 SLLMATLTKPKLLLLDEHTAALDpktaALV-LELTEKI---VEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

8-213

1.96e-40

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: 140.07 E-value: 1.96e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQs 85
Cdd:cd00267     2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 yalfpnltvaqniafglenqglardlikervdhwlglvdltaqshkypsqISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd00267    81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 166 LDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:cd00267   111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157

cbiO

PRK13650

energy-coupling factor transporter ATPase;

21-224

2.31e-40

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.72 E-value: 2.31e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSY-ALFPNLTVAQN 97
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSE 177
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 178 IRALQQRLGITTIMVTHDQEEaLTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228

YhaQ

COG4152

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

6-275

4.55e-40

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.33 E-value: 4.55e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISqlPPQQRDFGivfqs 85
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 Y-----ALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:COG4152    75 YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ-PASRFVASFVGTM 239
Cdd:COG4152   155 EPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLEADGDA 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2051267523 240 NFLDTLvlsPTQVRLNEQP----LQLANQAAAGSKLQVAI 275
Cdd:COG4152   234 GWLRAL---PGVTVVEEDGdgaeLKLEDGADAQELLRALL 270

MdlB

COG1132

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

19-222

7.18e-40

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.39 E-value: 7.18e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFpNLTVAQ 96
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRE 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLENqglARDlikERVDHWLGLVDL----TAQSHKYPSQI-------SGGQQQRVALARAlalspgllllDEPLSA 165
Cdd:COG1132   433 NIRYGRPD---ATD---EEVEEAAKAAQAhefiEALPDGYDTVVgergvnlSGGQRQRIAIARAllkdppililDEATSA 506

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 166 LDAlvrthlRSEiRALQQRL-----GITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:COG1132   507 LDT------ETE-ALIQEALerlmkGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

4-228

8.77e-40

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

Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 140.89 E-value: 8.77e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIV 82
Cdd:COG0410     2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 F--QSYALFPNLTVAQNIAFGLENQGlARDLIKERVDHWLGLV-DLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:COG0410    82 YvpEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPA 228
Cdd:COG0410   161 DEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

11-236

1.52e-39

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: 141.10 E-value: 1.52e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDFGIVFQ- 84
Cdd:TIGR02769  17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQd 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALF-PNLTVAQNIAFGLEN-QGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:TIGR02769  97 SPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIV--QVGTPQEIYHQPASRFVASFV 236
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeeCDVAQLLSFKHPAGRNLQSAV 253

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

21-164

1.73e-39

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.39 E-value: 1.73e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNLTVAQNI 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFGLENQGLARDLIKERVD---HWLGLVDLTAQS-HKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEealEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

19-223

2.04e-39

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.90 E-value: 2.04e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSY-ALFPNLTVA 95
Cdd:PRK13632   23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQNPdNQFIGATVE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLR 175
Cdd:PRK13632  103 DDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 176 SEIRALQQRLGITTIMVTHDQEEALtMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK13632  183 KIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

24-253

2.21e-39

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 140.67 E-value: 2.21e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-----SQLPPQQRDFGIVFQSYALFPNLTVAQNI 98
Cdd:PRK11831   26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFGL-ENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSE 177
Cdd:PRK11831  106 AYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 178 IRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRfvasfvgTMNFLDTLVLSPTQVR 253
Cdd:PRK11831  186 ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-------VRQFLDGIADGPVPFR 254

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

16-226

2.31e-39

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: 146.83 E-value: 2.31e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPnLT 93
Cdd:COG4988   348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQNPYLFA-GT 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGlenqglARDLIKERVDHWLGLVDLT----AQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEP 162
Cdd:COG4988   427 IRENLRLG------RPDASDEELEAALEAAGLDefvaALPDGLDTPLgeggrglSGGQAQRLALARALLRDAPLLLLDEP 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 163 LSALDALVRTHLRSEIRALQQrlGITTIMVTHDqEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:COG4988   501 TAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

6-222

2.70e-39

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.29 E-value: 2.70e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVF 83
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 QSYAL-FPnLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL--- 159
Cdd:PRK13548   83 QHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPprw 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 160 ---DEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:PRK13548  162 lllDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

20-228

3.52e-39

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.93 E-value: 3.52e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS------QLPPQQRDFGIVFQ--SYALFPN 91
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 lTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALV 170
Cdd:PRK13634  102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 171 RTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPA 228
Cdd:PRK13634  181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238

COG4559

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

6-222

5.07e-39

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.48 E-value: 5.07e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVF 83
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 QSYAL-FPnLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL--- 159
Cdd:COG4559    82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGgpr 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 160 ----DEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:COG4559   161 wlflDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226

PstB

COG1117

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

2-227

5.41e-39

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.40 E-value: 5.41e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DL-PD---SGEIWQGGRNI--SQLPP 74
Cdd:COG1117     8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLiPGarvEGEILLDGEDIydPDVDV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 QQ--RDFGIVFQSYALFPnLTVAQNIAFGLENQGLA-RDLIKERVDHWL---GLVD-----LtaqsHKYPSQISGGQQQR 143
Cdd:COG1117    88 VElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKsKSELDEIVEESLrkaALWDevkdrL----KKSALGLSGGQQQR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDAlVRThLRSE--IRALQQRLGIttIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQ 221
Cdd:COG1117   163 LCIARALAVEPEVLLMDEPTSALDP-IST-AKIEelILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238


                  ....*.
gi 2051267523 222 EIYHQP 227
Cdd:COG1117   239 QIFTNP 244

MglA

COG1129

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

2-223

5.96e-39

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.78 E-value: 5.96e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDFG 80
Cdd:COG1129     1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 I--VFQSYALFPNLTVAQNIAFGLE--NQGL---------ARDLIKErvdhwLGL-VDLTAQShkypSQISGGQQQRVAL 146
Cdd:COG1129    81 IaiIHQELNLVPNLSVAENIFLGREprRGGLidwramrrrARELLAR-----LGLdIDPDTPV----GDLSVAQQQLVEI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 147 ARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG1129   152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

6-215

2.26e-38

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: 136.19 E-value: 2.26e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQS 85
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPNLTVAQNiafgLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03268    81 PGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2051267523 166 LDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:cd03268   157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

1-222

3.95e-38

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 142.47 E-value: 3.95e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDF 79
Cdd:COG3845     1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GI--VFQSYALFPNLTVAQNIAFGLENQGL-------ARDLIKERVDHwLGL-VDLTAqshkYPSQISGGQQQRV----A 145
Cdd:COG3845    81 GIgmVHQHFMLVPNLTVAENIVLGLEPTKGgrldrkaARARIRELSER-YGLdVDPDA----KVEDLSVGEQQRVeilkA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARalalspgllllDEPLSAL-----DALVRThlrseIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTP 220
Cdd:COG3845   156 LYRgari----lilDEPTAVLtpqeaDELFEI-----LRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225


                  ..
gi 2051267523 221 QE 222
Cdd:COG3845   226 AE 227

PRK13633

energy-coupling factor transporter ATPase;

20-226

5.57e-38

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.53 E-value: 5.57e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGG---RNISQLPPQQRDFGIVFQSyalfP-NLTVA 95
Cdd:PRK13633   25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PdNQIVA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 ----QNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK13633  101 tiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 172 THLRSEIRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK13633  181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

16-228

3.97e-37

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: 140.67 E-value: 3.97e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFpNLT 93
Cdd:COG4987   346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFG------------LENQGLArDLIK---ERVDHWLGlvdltaqshKYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:COG4987   425 LRENLRLArpdatdeelwaaLERVGLG-DWLAalpDGLDTWLG---------EGGRRLSGGERRRLALARALLRDAPILL 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 159 LDEPLSALDALVRTHLRSEIR-ALQQRlgiTTIMVTHDqEEALTMADRIVVMEGGRIVQVGTPQEIYHQPA 228
Cdd:COG4987   495 LDEPTEGLDAATEQALLADLLeALAGR---TVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

1-228

4.04e-37

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: 140.20 E-value: 4.04e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGA----FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD-----SGEIWQGGRNISQ 71
Cdd:COG4172     2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRL-LPDpaahpSGSILFDGQDLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  72 LPPQQ------RDFGIVFQ--SYALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDLTAQSHK---YPSQISGG 139
Cdd:COG4172    81 LSERElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 140 QQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDqeeaLT----MADRIVVMEGGRIV 215
Cdd:COG4172   161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIV 236

                         250
                  ....*....|...
gi 2051267523 216 QVGTPQEIYHQPA 228
Cdd:COG4172   237 EQGPTAELFAAPQ 249

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

7-223

1.26e-36

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.90 E-value: 1.26e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   7 DIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQ 84
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGL--ENQG--LARDliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:COG4604    83 ENHINSRLTVRELVAFGRfpYSKGrlTAED--REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 161 EPLSALD-----ALVRThlrseIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG4604   161 EPLNNLDmkhsvQMMKL-----LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

8-218

1.56e-36

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: 131.50 E-value: 1.56e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLP------PQQRDFGi 81
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 vfqsyALFPnLTVAQNIAFGLENQ----GLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:cd03235    81 -----RDFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 158 LLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMeGGRIVQVG 218
Cdd:cd03235   155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

19-227

1.59e-36

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 133.28 E-value: 1.59e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI----SQLPPQQRDFGIVFQSY--ALF-Pn 91
Cdd:PRK13639   16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVGIVFQNPddQLFaP- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 lTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK13639   95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 172 THLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK13639  174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

6-230

2.36e-36

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 131.69 E-value: 2.36e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIvfq 84
Cdd:COG1137     4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRaRLGI--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SY-----ALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:COG1137    81 GYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRlGItTIMVT-HDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:COG1137   161 DEPFAGVDPIAVADIQKIIRHLKER-GI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

20-215

8.00e-36

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

Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 130.02 E-value: 8.00e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQN 97
Cdd:cd03245    19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLenqGLARDLIKERVDHWLGLVDLTAQS-HKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDal 169
Cdd:cd03245    98 ITLGA---PLADDERILRAAELAGVTDFVNKHpNGLDLQIgergrglSGGQRQAVALARALLNDPPILLLDEPTSAMD-- 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2051267523 170 vrthLRSE---IRALQQRL-GITTIMVTHDQeEALTMADRIVVMEGGRIV 215
Cdd:cd03245   173 ----MNSEerlKERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217

SapF

COG4167

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

4-227

1.73e-35

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 130.34 E-value: 1.73e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQF---------GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP 74
Cdd:COG4167     3 ALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 QQRDFGI--VFQ--SYALFPNLTVAQNIAFGLEnqgLARDLI----KERVDHWLGLVDLTA-QSHKYPSQISGGQQQRVA 145
Cdd:COG4167    83 KYRCKHIrmIFQdpNTSLNPRLNIGQILEEPLR---LNTDLTaeerEERIFATLRLVGLLPeHANFYPHMLSSGQKQRVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYH 225
Cdd:COG4167   160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239


                  ..
gi 2051267523 226 QP 227
Cdd:COG4167   240 NP 241

PRK10619

histidine ABC transporter ATP-binding protein HisP;

1-236

1.90e-35

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.09 E-value: 1.90e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS---------- 70
Cdd:PRK10619    1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  71 -----QLPPQQRDFGIVFQSYALFPNLTVAQNIAFG-LENQGLARDLIKERVDHWLGLVDLTAQSH-KYPSQISGGQQQR 143
Cdd:PRK10619   81 vadknQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDAlvrtHLRSEIRALQQRL---GITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTP 220
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236

                         250
                  ....*....|....*.
gi 2051267523 221 QEIYHQPASRFVASFV 236
Cdd:PRK10619  237 EQLFGNPQSPRLQQFL 252

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

6-215

2.51e-35

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

Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 126.77 E-value: 2.51e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDFGIvfq 84
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 syalfpnltvaqniafglenqglardlikervdhwlGLVdltaqshkypSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:cd03216    78 ------------------------------------AMV----------YQLSVGERQMVEIARALARNARLLILDEPTA 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 165 ALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:cd03216   112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

6-230

9.06e-35

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 128.65 E-value: 9.06e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF---------GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ 76
Cdd:PRK10419    4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 -----RDFGIVFQSY--ALFPNLTVAQNIAFGLEN-QGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALA 147
Cdd:PRK10419   84 rkafrRDIQMVFQDSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 148 RALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQ---VGTPQEIY 224
Cdd:PRK10419  164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLTFS 243


                  ....*.
gi 2051267523 225 HqPASR 230
Cdd:PRK10419  244 S-PAGR 248

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

21-215

1.09e-34

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 134.47 E-value: 1.09e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP------QQRDFGIVFQSYALFPNLTV 94
Cdd:PRK10535   24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLTA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  95 AQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHL 174
Cdd:PRK10535  104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2051267523 175 RSEIRALQQRlGITTIMVTHDQEEAlTMADRIVVMEGGRIV 215
Cdd:PRK10535  184 MAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

19-226

4.17e-34

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: 125.73 E-value: 4.17e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQ 96
Cdd:cd03249    17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFDG-TIAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLEnqglarDLIKERVDHWLGLVDLTAQSHKYP-----------SQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03249    96 NIRYGKP------DATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 166 LDAlvrthlRSEIR---ALQQ-RLGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:cd03249   170 LDA------ESEKLvqeALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227

PRK10908

cell division ATP-binding protein FtsE;

9-215

4.18e-34

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.37 E-value: 4.18e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   9 QHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQL-----PPQQRDFGIV 82
Cdd:PRK10908    5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQIGMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:PRK10908   85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 163 LSALD-ALVRTHLR--SEIralqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:PRK10908  165 TGNLDdALSEGILRlfEEF----NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216

LPS_export_lptB

TIGR04406

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...

6-232

5.16e-34

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

Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 125.85 E-value: 5.16e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIVF- 83
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERaRLGIGYl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 -QSYALFPNLTVAQNIAFGLENQG-LARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:TIGR04406  82 pQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFV 232
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV 231

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

20-224

6.49e-34

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.40 E-value: 6.49e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQS-YALFPNLTVAQ 96
Cdd:PRK13648   24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQNpDNQFVGSIVKY 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRS 176
Cdd:PRK13648  104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 177 EIRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13648  184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

21-214

7.13e-34

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: 123.10 E-value: 7.13e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDF-GIVFQSYALFPNlTVAQNI 98
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHvGYLPQDDELFSG-SIAENI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 afglenqglardlikervdhwlglvdltaqshkypsqISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEI 178
Cdd:cd03246    97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2051267523 179 RALQQRlGITTIMVTHdQEEALTMADRIVVMEGGRI 214
Cdd:cd03246   140 AALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

6-218

8.53e-34

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: 124.23 E-value: 8.53e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGeFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD-FGIVFQ 84
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 165 ALDALVRTHLRSeiraLQQRLGITTIMV--THDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03264   160 GLDPEERIRFRN----LLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

16-227

1.51e-33

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 1.51e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSY--ALFpN 91
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNPddQIF-S 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK13652   94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 172 THLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK13652  174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

6-233

1.60e-33

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: 124.17 E-value: 1.60e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGI--V 82
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIayV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLENQGLARDLIKERVdhwLGLVD-LTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI---YELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVA 233
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

19-221

2.76e-33

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.85 E-value: 2.76e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSY--ALFPNlTV 94
Cdd:PRK13647   19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVFSS-TV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  95 AQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHL 174
Cdd:PRK13647   98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 175 RSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQ 221
Cdd:PRK13647  178 MEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223

cbiO

PRK13644

energy-coupling factor transporter ATPase;

20-232

3.30e-33

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.71 E-value: 3.30e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRN---ISQLPPQQRDFGIVFQS-YALFPNLTVA 95
Cdd:PRK13644   17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLVGIVFQNpETQFVGRTVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLR 175
Cdd:PRK13644   97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 176 SEIRALQQRlGITTIMVTHDQEEaLTMADRIVVMEGGRIVQVGTPQEIYHQPASRFV 232
Cdd:PRK13644  177 ERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

1-226

6.53e-33

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.11 E-value: 6.53e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGR-----NISQLPPQ 75
Cdd:PRK11701    2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 QR------DFGIVFQSYA--LFPNLTVAQNIAFGLENQGlARDL--IKERVDHWLGLVDL-TAQSHKYPSQISGGQQQRV 144
Cdd:PRK11701   82 ERrrllrtEWGFVHQHPRdgLRMQVSAGGNIGERLMAVG-ARHYgdIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG------ 218
Cdd:PRK11701  161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdqvl 240


                  ....*....
gi 2051267523 219 -TPQEIYHQ 226
Cdd:PRK11701  241 dDPQHPYTQ 249

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

17-227

1.01e-32

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.82 E-value: 1.01e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  17 AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-----DFGIVFQS--YALF 89
Cdd:PRK15079   33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLN 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  90 PNLTVAQNIAFGLE--NQGLARDLIKERVDHWLGLVDLTAQS-HKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:PRK15079  113 PRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 167 DALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK15079  193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253

type_I_sec_LssB

TIGR03375

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...

20-223

2.66e-32

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: 127.67 E-value: 2.66e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQN 97
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGlenQGLARDLIKERVDHWLGLVDLTAQSHK-YPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDAl 169
Cdd:TIGR03375 559 IALG---APYADDEEILRAAELAGVTEFVRRHPDgLDMQIgergrslSGGQRQAVALARALLRDPPILLLDEPTSAMDN- 634

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 170 vrthlRSE---IRALQQRL-GITTIMVTHDQeEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR03375 635 -----RSEerfKDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

21-223

3.06e-32

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: 126.79 E-value: 3.06e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQNI 98
Cdd:COG4618   348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 A-FG-------LENQGLAR--DLIkervdhwLGLVD-----LTAQSHkypsQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:COG4618   427 ArFGdadpekvVAAAKLAGvhEMI-------LRLPDgydtrIGEGGA----RLSGGQRQRIGLARALYGDPRLVVLDEPN 495

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 164 SALDALVRTHLRSEIRALQQRlGITTIMVTHDQeEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG4618   496 SNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

19-227

1.07e-31

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.61 E-value: 1.07e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-----RDFGIVFQS-YA-LFPN 91
Cdd:PRK11308   29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDL-TAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PRK11308  109 KKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 170 VRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK11308  189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246

livG

PRK11300

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

1-227

1.29e-31

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.71 E-value: 1.29e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDF 79
Cdd:PRK11300    1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIV--FQSYALFPNLTVAQNIAFGLE---NQGLARDLIK------------ERVDHWLGLVDLTAQSHKYPSQISGGQQQ 142
Cdd:PRK11300   81 GVVrtFQHVRLFREMTVIENLLVAQHqqlKTGLFSGLLKtpafrraesealDRAATWLERVGLLEHANRQAGNLAYGQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 143 RVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:PRK11300  161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240


                  ....*
gi 2051267523 223 IYHQP 227
Cdd:PRK11300  241 IRNNP 245

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

6-224

2.82e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 2.82e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG-AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ----LPPQQRDFG 80
Cdd:PRK13636    6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQS--YALFpNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLL 158
Cdd:PRK13636   86 MVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 159 LDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13636  165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230

cbiO

PRK13640

energy-coupling factor transporter ATPase;

20-227

3.97e-31

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 3.97e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGE---IWQGGRNISQLPPQQ-RD-FGIVFQSY-ALFPNLT 93
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDiREkVGIVFQNPdNQFVGAT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:PRK13640  102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 174 LRSEIRALQQRLGITTIMVTHDQEEAlTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK13640  182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

7-215

4.83e-31

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

Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.59 E-value: 4.83e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   7 DIQHLNKQFGAFQ-ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQlPPQQRDFGIVFQS 85
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 --YALFPNlTVAQNIAFGLENQGLArdliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:cd03226    80 vdYQLFTD-SVREELLLGLKELDAG----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 164 SALDalvRTHLRS---EIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:cd03226   155 SGLD---YKNMERvgeLIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

6-211

5.25e-31

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.57 E-value: 5.25e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR---- 77
Cdd:PRK10584    7 VEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 --DFGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPG 155
Cdd:PRK10584   87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 156 LLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:PRK10584  167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

38-230

6.86e-31

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.98 E-value: 6.86e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  38 GPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ------LPPQQRDFGIVFQSYALFPNLTVAQNIAFGLEnqglardl 111
Cdd:PRK11144   31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA-------- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 112 iKERVDHWLGLVDLTAQSH---KYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGIT 188
Cdd:PRK11144  103 -KSMVAQFDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2051267523 189 TIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:PRK11144  182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223

PRK14239

phosphate transporter ATP-binding protein; Provisional

1-230

1.17e-30

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 1.17e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DL-PD---SGEIWQGGRNIsqLPPQ 75
Cdd:PRK14239    1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMnDLnPEvtiTGSIVYNGHNI--YSPR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 ------QRDFGIVFQSYALFPnLTVAQNIAFGLENQGLaRDliKERVDH-----------WLGLVDltaQSHKYPSQISG 138
Cdd:PRK14239   79 tdtvdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGI-KD--KQVLDEavekslkgasiWDEVKD---RLHDSALGLSG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 139 GQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:PRK14239  152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229

                         250
                  ....*....|..
gi 2051267523 219 TPQEIYHQPASR 230
Cdd:PRK14239  230 DTKQMFMNPKHK 241

CP_lyasePhnK

TIGR02323

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...

3-227

1.17e-30

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: 117.24 E-value: 1.17e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-----QGGRNISQLPPQQR 77
Cdd:TIGR02323   1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsGAELELYQLSEAER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 ------DFGIVFQSYA--LFPNLTVAQNIAFGLENQGlARDL--IKERVDHWLGLVDL-TAQSHKYPSQISGGQQQRVAL 146
Cdd:TIGR02323  81 rrlmrtEWGFVHQNPRdgLRMRVSAGANIGERLMAIG-ARHYgnIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 147 ARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239


                  .
gi 2051267523 227 P 227
Cdd:TIGR02323 240 P 240

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

3-223

1.58e-30

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 121.83 E-value: 1.58e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQF-----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW----QGGRNISQLP 73
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgDEWVDMTKPG 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  74 PQQRD-----FGIVFQSYALFPNLTVAQNI--AFGLEnqgLARDLIKERVDHWL---GLVDLTAQS--HKYPSQISGGQQ 141
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNLteAIGLE---LPDELARMKAVITLkmvGFDEEKAEEilDKYPDELSEGER 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 142 QRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQ 221
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513


                  ..
gi 2051267523 222 EI 223
Cdd:TIGR03269 514 EI 515

nickel_nikD

TIGR02770

nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...

23-237

1.62e-30

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

Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 116.31 E-value: 1.62e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  23 GISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPD----SGEIWQGGRNISQLPPQQRDFGIVFQS--YALFPNLTVAQ 96
Cdd:TIGR02770   4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 N------IAFGLENQglARDLIKERVDHwLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALV 170
Cdd:TIGR02770  84 HaietlrSLGKLSKQ--ARALILEALEA-VGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 171 RTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFVG 237
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227

cbiO

PRK13642

energy-coupling factor transporter ATPase;

21-224

2.00e-30

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.12 E-value: 2.00e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS--QLPPQQRDFGIVFQSY-ALFPNLTVAQN 97
Cdd:PRK13642   23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSE 177
Cdd:PRK13642  103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 178 IRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13642  183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

19-222

3.69e-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: 115.02 E-value: 3.69e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQ 96
Cdd:cd03254    17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIME 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLENqglARDLIKERVDHWLGLVDLTAQSHK-YPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:cd03254    96 NIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPNgYDTVLgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDT 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 169 LVRTHLRSEIRALQQrlGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:cd03254   173 ETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223

cbiO

PRK13641

energy-coupling factor transporter ATPase;

19-243

4.35e-30

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.47 E-value: 4.35e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS------QLPPQQRDFGIVFQ--SYALFP 90
Cdd:PRK13641   21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  91 NlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PRK13641  101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 170 VRTHLrSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP------------ASRFVASF-V 236
Cdd:PRK13641  180 GRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkkhyldepaTSRFASKLeK 258


                  ....*..
gi 2051267523 237 GTMNFLD 243
Cdd:PRK13641  259 GGFKFSE 265

cbiO

PRK13645

energy-coupling factor transporter ATPase;

18-224

5.74e-30

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.26 E-value: 5.74e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGE-------IWQGGRNISQLPPQQRDFGIVFQ--SYAL 88
Cdd:PRK13645   24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVKRLRKEIGLVFQfpEYQL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  89 FPNlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK13645  104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 168 ALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13645  183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

1-223

6.06e-30

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.44 E-value: 6.06e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD-F 79
Cdd:PRK13537    3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 GIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:PRK13537   83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK13537  163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

1-216

1.48e-29

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 1.48e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF--GAFQA--LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP-- 74
Cdd:PRK11629    1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 ----QQRDFGIVFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAL 150
Cdd:PRK11629   81 kaelRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 151 ALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMaDRIVVMEGGRIVQ 216
Cdd:PRK11629  161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

16-218

3.03e-29

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: 112.63 E-value: 3.03e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLppqqrDFGIVFQsyalfPNLTVA 95
Cdd:cd03220    33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLR 175
Cdd:cd03220   103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2051267523 176 SEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03220   183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

20-226

3.22e-29

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: 112.71 E-value: 3.22e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS--QLPPQQRDFGIVFQSYALFpNLTVAQN 97
Cdd:cd03251    17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDTVAEN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYP-----SQISGGQQQRVALARALALSPGLLLLDEPLSALDalvrt 172
Cdd:cd03251    96 IAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVigergVKLSGGQRQRIAIARALLKDPPILILDEATSALD----- 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 173 hLRSEiRALQQRL-----GITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:cd03251   171 -TESE-RLVQAALerlmkNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

6-236

4.14e-29

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.01 E-value: 4.14e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DLPDS----GEIWQGGRNI--SQLPPQQ-- 76
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELNEEarveGEVRLFGRNIysPDVDPIEvr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 RDFGIVFQSYALFPNLTVAQNIAFGLENQGLAR--DLIKERVDHWLGLVDLTAQS----HKYPSQISGGQQQRVALARAL 150
Cdd:PRK14267   85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIARAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 151 ALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:PRK14267  165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242


                  ....*.
gi 2051267523 231 FVASFV 236
Cdd:PRK14267  243 LTEKYV 248

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

20-214

5.78e-29

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: 110.60 E-value: 5.78e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIVF-----QSYALFPNLT 93
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFglenqglardlikervdhwlglvdltaqshkyPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:cd03215    95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2051267523 174 LRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:cd03215   143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182

PRK09984

phosphonate ABC transporter ATP-binding protein;

3-222

6.12e-29

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 112.80 E-value: 6.12e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDS---GEIWQGGRNISQLPPQQRDF 79
Cdd:PRK09984    2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  80 -------GIVFQSYALFPNLTVAQNIAFG-LENQGLARDLI-------KERVDHWLGLVDLTAQSHKYPSQISGGQQQRV 144
Cdd:PRK09984   82 rksrantGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTCFswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:PRK09984  162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

18-222

1.18e-28

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: 111.17 E-value: 1.18e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS--QLPPQQRDFGIVFQSYALFpNLTVA 95
Cdd:cd03253    14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTVLF-NDTIG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGLENqglARDlikERVDHwlglVDLTAQSH--------KYPSQ-------ISGGQQQRVALARALALSPGLLLLD 160
Cdd:cd03253    93 YNIRYGRPD---ATD---EEVIE----AAKAAQIHdkimrfpdGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 161 EPLSALDalvrTHlrSEiRALQQRL-----GITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQE 222
Cdd:cd03253   163 EATSALD----TH--TE-REIQAALrdvskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

3-223

1.50e-28

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: 111.33 E-value: 1.50e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSG-EIW-----QGGRNISQLPPQq 76
Cdd:COG1119     1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerRGGEDVWELRKR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 rdFGIVfqSYALF----PNLTVAQNIAFGLENQ-GLAR---DLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALAR 148
Cdd:COG1119    80 --IGLV--SPALQlrfpRDETVLDVVLSGFFDSiGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 149 ALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG1119   156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

16-209

1.82e-28

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: 115.85 E-value: 1.82e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNlT 93
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-T 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGlenQGLARDLIKERVDHWLGLVDLTA---QSHKYP-----SQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:TIGR02857 412 IAENIRLA---RPDASDAEIREALERAGLDEFVAalpQGLDTPigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2051267523 166 LDALVRTHLRSEIRALQQrlGITTIMVTHDqEEALTMADRIVVM 209
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

13-213

2.26e-28

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: 109.48 E-value: 2.26e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGlDLP-DSGEIWQGGRnisqlppqqrdFGIVFQSyALFPN 91
Cdd:cd03250    13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEkLSGSVSVPGS-----------IAYVSQE-PWIQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNIAFG-----------LENQGLARDLikERVDHwlGlvDLTaqshkypsQI-------SGGQQQRVALARALALS 153
Cdd:cd03250    80 GTIRENILFGkpfdeeryekvIKACALEPDL--EILPD--G--DLT--------EIgekginlSGGQKQRISLARAVYSD 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 154 PGLLLLDEPLSALDALVRTHLRSeiRALQQRL--GITTIMVTHdQEEALTMADRIVVMEGGR 213
Cdd:cd03250   146 ADIYLLDDPLSAVDAHVGRHIFE--NCILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNGR 204

fecE

PRK11231

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

6-223

2.42e-28

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.87 E-value: 2.42e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQrdfgiVFQS 85
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 YALFPN-------LTVAQNIAFG----LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSP 154
Cdd:PRK11231   78 LALLPQhhltpegITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK11231  158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

6-236

2.60e-28

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 2.60e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-----DLPDSGEIWQGGRNISQLP--PQQRD 78
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDviELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYALFPNLTVAQNIAFGLENQGLA--RDLIKERVDHWL---GLVDLTAQSHKYPS-QISGGQQQRVALARALAL 152
Cdd:PRK14247   84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVksKKELQERVRWALekaQLWDEVKDRLDAPAgKLSGGQQQRLCIARALAF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 153 SPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGIttIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFV 232
Cdd:PRK14247  164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241


                  ....
gi 2051267523 233 ASFV 236
Cdd:PRK14247  242 EKYV 245

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

2-231

3.13e-28

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.19 E-value: 3.13e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQF-----------GAFQALKGISLTIEPGEFICFLGPSGCGKTT----LLRAIAGldlpdSGEIWQGG 66
Cdd:PRK15134  272 ASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDG 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  67 RNISQLPPQQ-----RDFGIVFQ--SYALFPNLTVAQNIAFGLE--NQGLARDLIKERVDHWLGLVDLTAQS-HKYPSQI 136
Cdd:PRK15134  347 QPLHNLNRRQllpvrHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEF 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 137 SGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQ 216
Cdd:PRK15134  427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506

                         250
                  ....*....|....*
gi 2051267523 217 VGTPQEIYHQPASRF 231
Cdd:PRK15134  507 QGDCERVFAAPQQEY 521

PRK13651

cobalt transporter ATP-binding subunit; Provisional

17-223

3.99e-28

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.72 E-value: 3.99e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  17 AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-----------------WQGGRNISQLPPQQ--- 76
Cdd:PRK13651   19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKkik 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 ------RDFGIVFQ--SYALFPNlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTaQSH--KYPSQISGGQQQRVAL 146
Cdd:PRK13651   99 kikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD-ESYlqRSPFELSGGQKRRVAL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 147 ARALALSPGLLLLDEPLSALDA-------LVRTHLRSEiralqqrlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGT 219
Cdd:PRK13651  177 AGILAMEPDFLVFDEPTAGLDPqgvkeilEIFDNLNKQ--------GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248


                  ....
gi 2051267523 220 PQEI 223
Cdd:PRK13651  249 TYDI 252

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

16-218

4.86e-28

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: 108.41 E-value: 4.86e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  16 GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL--DLPDSGEIWQGGRNISQLPPQQRdFGIVFQSYALFPNLT 93
Cdd:cd03213    20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGlardlikervdhwlglvdltaqshkypsqISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:cd03213    99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2051267523 174 LRSEIRALQQrLGITTIMVTHD-QEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03213   150 VMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

20-223

5.03e-28

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.

Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 114.80 E-value: 5.03e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNlTVAQN 97
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAelRARMALVPQDPVLFAA-SVMEN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYP-----SQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:TIGR02204 434 IRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYlgergVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQ 513

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 173 HLRSEIRALQQrlGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR02204 514 LVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAEL 561

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

1-213

6.53e-28

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: 109.06 E-value: 6.53e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTqPYLDIQHLNKQF------GA-FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW---QGGR-NI 69
Cdd:COG4778     1 MT-TLLEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhDGGWvDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  70 SQLPPQQ------RDFGIVFQSYALFPNLT----VAQniafGLENQGLARDLIKERVDHWLG-------LVDLtaqshkY 132
Cdd:COG4778    80 AQASPREilalrrRTIGYVSQFLRVIPRVSaldvVAE----PLLERGVDREEARARARELLArlnlperLWDL------P 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 133 PSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGG 212
Cdd:COG4778   150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228


                  .
gi 2051267523 213 R 213
Cdd:COG4778   229 S 229

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

4-228

9.34e-28

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.65 E-value: 9.34e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGI 81
Cdd:PRK10247    6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNlTVAQNIAF-------GLENQGLARDLIKervdhwLGLVDLTAQshKYPSQISGGQQQRVALARALALSP 154
Cdd:PRK10247   86 CAQTPTLFGD-TVYDNLIFpwqirnqQPDPAIFLDDLER------FALPDTILT--KNIAELSGGEKQRISLIRNLQFMP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEaLTMADRIVVMEGgrivQVGTPQEIYHQPA 228
Cdd:PRK10247  157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQP----HAGEMQEARYELA 225

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

4-218

1.05e-27

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.61 E-value: 1.05e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP-QQRDFGI- 81
Cdd:PRK15439   10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPaKAHQLGIy 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 -VFQSYALFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQShkypSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK15439   90 lVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSA----GSLEVADRQIVEILRGLMRDSRILILD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:PRK15439  166 EPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

18-223

1.70e-27

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 1.70e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLppqqrDFGIVFQsyalfPNLTVAQN 97
Cdd:COG1134    39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH-----PELTGREN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKERVDHwlgLVDLtaqshkypSQI-----------SGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:COG1134   109 IYLNGRLLGLSRKEIDEKFDE---IVEF--------AELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 167 DALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG1134   178 DAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233

PRK14243

phosphate transporter ATP-binding protein; Provisional

2-236

2.47e-27

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 108.33 E-value: 2.47e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DLPDS----GEIWQGGRNI--SQLPP 74
Cdd:PRK14243    7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNLyaPDVDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 QQ--RDFGIVFQSYALFPNlTVAQNIAFGLENQGLARDLiKERVDH-------WLGLVDLTAQShkyPSQISGGQQQRVA 145
Cdd:PRK14243   87 VEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDM-DELVERslrqaalWDEVKDKLKQS---GLSLSGGQQQRLC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLgiTTIMVTHDQEEALTMADRI------VVMEGGRI---VQ 216
Cdd:PRK14243  162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTaffnveLTEGGGRYgylVE 239

                         250       260
                  ....*....|....*....|
gi 2051267523 217 VGTPQEIYHQPASRFVASFV 236
Cdd:PRK14243  240 FDRTEKIFNSPQQQATRDYV 259

cbiO

PRK13649

energy-coupling factor transporter ATPase;

20-226

2.52e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 2.52e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS------QLPPQQRDFGIVFQsyalFPNL- 92
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 ----TVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK13649   98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 168 ALVRTHLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK13649  178 PKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

19-218

8.47e-27

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: 106.20 E-value: 8.47e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPD---SGEIWQGGRnisQLPPQ--QRDFGIVFQSYALFPNLT 93
Cdd:cd03234    21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDqfQKCVAYVRQDDILLPGLT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFG--LENQGLARDLIKERVDHWLGLVDLTAQS--HKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:cd03234    98 VRETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 170 VRTHLRSEIR--ALQQRLGITTImvtHD-QEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03234   178 TALNLVSTLSqlARRNRIVILTI---HQpRSDLFRLFDRILLLSSGEIVYSG 226

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

20-223

1.63e-26

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: 105.65 E-value: 1.63e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQN 97
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAfgLENQGLARdlikERVDHWLGLVDLTAQSHKYP-----------SQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:cd03252    96 IA--LADPGMSM----ERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 167 DalvrthLRSEiRALQQRL-----GITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03252   170 D------YESE-HAIMRNMhdicaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

20-215

1.69e-26

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

Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.49 E-value: 1.69e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnisqLPPQQRD-----FGIVF-QSYALFPNLT 93
Cdd:cd03267    36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKkflrrIGVVFgQKTQLWWDLP 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:cd03267   112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2051267523 174 LRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:cd03267   192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

21-236

2.01e-26

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.90 E-value: 2.01e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DLPDS-----GEIWQGGRNISQLPP--QQRDFGIVFQSYALFPNL 92
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAikLRKEVGMVFQQPNPFPHL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLA-RDLIKERVDHWLGLVDLTAQSHKY----PSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK14246  106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 168 ALVRTHLRSEIRALQQRlgITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASFV 236
Cdd:PRK14246  186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

4-238

2.19e-26

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 2.19e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGI 81
Cdd:PRK09536    2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQNIAFG----LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:PRK09536   82 VPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 158 LLDEPLSALDalvrthLRSEIRALQ--QRL---GITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR-- 230
Cdd:PRK09536  162 LLDEPTASLD------INHQVRTLElvRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRaa 235


                  ....*....
gi 2051267523 231 FVA-SFVGT 238
Cdd:PRK09536  236 FDArTAVGT 244

cbiO

PRK13646

energy-coupling factor transporter ATPase;

18-226

3.31e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.02 E-value: 3.31e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ------LPPQQRDFGIVFQ--SYALF 89
Cdd:PRK13646   20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQfpESQLF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  90 PNlTVAQNIAFGLENQGLARDLIKERVDHWL---GLV-DLTAQShkyPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:PRK13646  100 ED-TVEREIIFGPKNFKMNLDEVKNYAHRLLmdlGFSrDVMSQS---PFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 166 LDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK13646  176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

6-235

7.27e-26

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 108.35 E-value: 7.27e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLD--LPDSGEI-----------WQG-----GR 67
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  68 NI----SQLPPQQRDF---------------GIVFQ-SYALFPNLTVAQNIAFGLENQGLARdliKERVDHWLGLVDLTA 127
Cdd:TIGR03269  81 PCpvcgGTLEPEEVDFwnlsdklrrrirkriAIMLQrTFALYGDDTVLDNVLEALEEIGYEG---KEAVGRAVDLIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 128 QSHKY---PSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMAD 204
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2051267523 205 RIVVMEGGRIVQVGTPQEIyhqpASRFVASF 235
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV----VAVFMEGV 264

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

20-223

7.92e-26

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: 108.65 E-value: 7.92e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQN 97
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQDVVLF-NDTIANN 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLenqglARDLIKERVDHWLGLVDLTAQSHKYP-----------SQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:TIGR02203 426 IAYGR-----TEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 167 DALVRTHLRSEIRALQQrlGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR02203 501 DNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

6-223

9.15e-26

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 9.15e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGrniSQLPPQQR----DFGI 81
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARlaraRIGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 VFQSYALFPNLTVAQN-IAFGLENQGLARDlIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK13536  119 VPQFDNLDLEFTVRENlLVFGRYFGMSTRE-IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 161 EPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK13536  198 EPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

21-223

1.13e-25

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

Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 1.13e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQNI 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 A-FGlenqglaRDLIKERVDHWLGLvdltAQSHK--------YPSQI-------SGGQQQRVALARALALSPGLLLLDEP 162
Cdd:TIGR01842 413 ArFG-------ENADPEKIIEAAKL----AGVHElilrlpdgYDTVIgpggatlSGGQRQRIALARALYGDPKLVVLDEP 481

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRlGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540

cbiO

PRK13643

energy-coupling factor transporter ATPase;

17-226

1.80e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 1.80e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  17 AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS------QLPPQQRDFGIVFQ--SYAL 88
Cdd:PRK13643   18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfpESQL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  89 FPNlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQS-HKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK13643   98 FEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 168 ALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK13643  177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

6-228

6.13e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 6.13e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHL-----NKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-----------QGGRNI 69
Cdd:PRK13631   22 LRVKNLycvfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknNHELIT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  70 SQLPPQQRDF-------GIVFQ--SYALFPNlTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQS-HKYPSQISGG 139
Cdd:PRK13631  102 NPYSKKIKNFkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSGG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 140 QQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGT 219
Cdd:PRK13631  181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259


                  ....*....
gi 2051267523 220 PQEIYHQPA 228
Cdd:PRK13631  260 PYEIFTDQH 268

PRK10261

glutathione transporter ATP-binding protein; Provisional

11-227

6.43e-25

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.09 E-value: 6.43e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-----SQLPPQQRDFGIVFQS 85
Cdd:PRK10261  330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQD 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 -YA-LFPNLTVAQNIAFGLENQGLAR-DLIKERVDHWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK10261  410 pYAsLDPRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK10261  490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555

PRK11174

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

19-227

1.11e-24

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.31 E-value: 1.11e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQ 96
Cdd:PRK11174  364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRD 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLEN-------QGLARDLIKERVD-HWLGLvDLTAQSHKypSQISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:PRK11174  442 NVLLGNPDasdeqlqQALENAWVSEFLPlLPQGL-DTPIGDQA--AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 169 lvrthlRSE---IRALQQ-RLGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK11174  519 ------HSEqlvMQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574

MglA

COG1129

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

4-215

2.64e-24

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 2.64e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQfgafQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIV 82
Cdd:COG1129   255 VVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiRAGIA 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 F-----QSYALFPNLTVAQNIA---------FGLenqgLARDLIKERVDHWLGLVDLTAQSHKYP-SQISGGQQQRVALA 147
Cdd:COG1129   331 YvpedrKGEGLVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLA 406

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 148 RALALSPGLLLLDEPLSALDalVRThlRSEIRALQQRL---GITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:COG1129   407 KWLATDPKVLILDEPTRGID--VGA--KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

15-209

5.39e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 5.39e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  15 FGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGivfqsyALFPnLTV 94
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  95 AQNIAFGL-ENQGLARDLIKE---RVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALV 170
Cdd:NF040873   75 RDLVAMGRwARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2051267523 171 RTHLRSEIRALQQRlGITTIMVTHDQEEALTmADRIVVM 209
Cdd:NF040873  155 RERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

6-227

7.43e-24

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 100.20 E-value: 7.43e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGL-DLP-----DSGEIwqGGRNISQLPPQ 75
Cdd:PRK11022    4 LNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvmaEKLEF--NGQDLQRISEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 QR------DFGIVFQS--YALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLV---DLTAQSHKYPSQISGGQQQR 143
Cdd:PRK11022   82 ERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK11022  162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241


                  ....
gi 2051267523 224 YHQP 227
Cdd:PRK11022  242 FRAP 245

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

19-224

7.99e-24

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 7.99e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQG-GRNISQ--LPPQQRDFGIVFQ--SYALFPNl 92
Cdd:PRK13638   15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlWQGkPLDYSKrgLLALRQQVATVFQdpEQQIFYT- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:PRK13638   94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 173 HLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PRK13638  174 QMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

6-194

8.29e-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: 97.04 E-value: 8.29e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQLPPQQRDFGIVFQ 84
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQRDEPHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFglenqgLARDLIKERVDHW--LGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:TIGR01189  81 LPGLKPELSALENLHF------WAAIHGGAQRTIEdaLAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRLGItTIMVTH 194
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGI-VLLTTH 185

PRK13549

xylose transporter ATP-binding subunit; Provisional

1-219

1.11e-23

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 1.11e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD---SGEI-WQG----GRNISQl 72
Cdd:PRK13549    1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIiFEGeelqASNIRD- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  73 pPQQRDFGIVFQSYALFPNLTVAQNIAFGLE---NQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARA 149
Cdd:PRK13549   79 -TERAGIAIIHQELALVKELSVLENIFLGNEitpGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 150 LALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRivQVGT 219
Cdd:PRK13549  158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

6-218

2.58e-23

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.

Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.07 E-value: 2.58e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG--AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRD-FGIV 82
Cdd:cd03247     1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFpNLTVAQNIAfglenqglardlikervdhwlglvdltaqshkypSQISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:cd03247    81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 163 LSALDALVRTHLRSEIraLQQRLGITTIMVTHdQEEALTMADRIVVMEGGRIVQVG 218
Cdd:cd03247   126 TVGLDPITERQLLSLI--FEVLKDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

4-227

5.63e-23

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 5.63e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDsGEIWQGGR-------------NIS 70
Cdd:PRK14258    6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffnqniyerrvNLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  71 QLppqQRDFGIVFQSYALFPnLTVAQNIAFG---------LENQGLARDLIKErVDHWlglVDLTAQSHKYPSQISGGQQ 141
Cdd:PRK14258   85 RL---RRQVSMVHPKPNLFP-MSVYDNVAYGvkivgwrpkLEIDDIVESALKD-ADLW---DEIKHKIHKSALDLSGGQQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 142 QRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG-----GRIVQ 216
Cdd:PRK14258  157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236

                         250
                  ....*....|.
gi 2051267523 217 VGTPQEIYHQP 227
Cdd:PRK14258  237 FGLTKKIFNSP 247

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

2-216

6.63e-23

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.60 E-value: 6.63e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnisqlpPQQ----R 77
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRfastT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 D-----FGIVFQSYALFPNLTVAQNI-------AFGLENQGLARDLIKERVDHwLGL-VDLTAQShKYpsqISGGQQQRV 144
Cdd:PRK11288   75 AalaagVAIIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEH-LGVdIDPDTPL-KY---LSIGQRQMV 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQ 216
Cdd:PRK11288  150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220

livF

PRK11614

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

1-215

7.58e-23

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.72 E-value: 7.58e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ---R 77
Cdd:PRK11614    1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQNIAFGlenqGL--ARDLIKERVDHWLGLVD-LTAQSHKYPSQISGGQQQRVALARALALSP 154
Cdd:PRK11614   81 AVAIVPEGRRVFSRMTVEENLAMG----GFfaERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:PRK11614  157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

6-219

8.69e-23

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: 99.13 E-value: 8.69e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD---SGEI-WQG----GRNISQlpPQQR 77
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIyWSGsplkASNIRD--TERA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQNIAFGLE---NQGL-ARDLIKERVDHWLGLVDLTAQSHKYP-SQISGGQQQRVALARALAL 152
Cdd:TIGR02633  79 GIVIIHQELTLVPELSVAENIFLGNEitlPGGRmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 153 SPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRivQVGT 219
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222

PRK11160

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

2-222

1.04e-22

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 1.04e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNkqFG----AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ- 76
Cdd:PRK11160  335 DQVSLTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAl 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 RD-FGIVFQSYALFP-----NLTVAQNIA-----------FGLENqgLARDliKERVDHWLGlvdltaqshKYPSQISGG 139
Cdd:PRK11160  413 RQaISVVSQRVHLFSatlrdNLLLAAPNAsdealievlqqVGLEK--LLED--DKGLNAWLG---------EGGRQLSGG 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 140 QQQRVALARALALSPGLLLLDEPLSALDAlvRThlRSEIRAL--QQRLGITTIMVTHdQEEALTMADRIVVMEGGRIVQV 217
Cdd:PRK11160  480 EQRRLGIARALLHDAPLLLLDEPTEGLDA--ET--ERQILELlaEHAQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQ 554


                  ....*
gi 2051267523 218 GTPQE 222
Cdd:PRK11160  555 GTHQE 559

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

4-237

1.72e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.55 E-value: 1.72e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLD-----LPDSGEIWQGGRNI---SQLPPQ 75
Cdd:PRK14271   20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIfnyRDVLEF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 QRDFGIVFQSYALFPnLTVAQNIAFGL---------ENQGLARDLIKErVDHWLGLVDLTAQShkyPSQISGGQQQRVAL 146
Cdd:PRK14271  100 RRRVGMLFQRPNPFP-MSIMDNVLAGVrahklvprkEFRGVAQARLTE-VGLWDAVKDRLSDS---PFRLSGGQQQLLCL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 147 ARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK14271  175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252

                         250
                  ....*....|....*
gi 2051267523 227 P----ASRFVASFVG 237
Cdd:PRK14271  253 PkhaeTARYVAGLSG 267

BtuD

COG4138

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

21-223

2.02e-22

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.52 E-value: 2.02e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNLTVAQNI 98
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFGLEnQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARA-------LALSPGLLLLDEPLSALDALVR 171
Cdd:COG4138    91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVllqvwptINPEGQLLLLDEPMNSLDVAQQ 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 172 THLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG4138   170 AALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

20-220

3.99e-22

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 93.33 E-value: 3.99e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQN 97
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLE------NQGLARDLIKERVDHWLGLVDLTAQSHKypSQISGGQQQRVALARALALSPGLLLLDEPLSALD---- 167
Cdd:cd03244    98 LDPFGEysdeelWQALERVGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASVDpetd 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 168 ALVRTHLRSEIRalqqrlGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTP 220
Cdd:cd03244   176 ALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

19-222

5.16e-22

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: 97.20 E-value: 5.16e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQ 96
Cdd:COG5265   372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAY 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGleNQGLARDLIKE--RVDHWLGLVDLTAQshKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:COG5265   451 NIAYG--RPDASEEEVEAaaRAAQIHDFIESLPD--GYDTRVgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALD 526

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 168 AlvrthlRSEiRALQQRL-----GITTIMVTH------DqeealtmADRIVVMEGGRIVQVGTPQE 222
Cdd:COG5265   527 S------RTE-RAIQAALrevarGRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578

3a01208

TIGR00958

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

19-227

5.71e-22

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.49 E-value: 5.71e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQ 96
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLF-SGSVRE 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLEN-----------QGLARDLIKERVDHWLGLVDLTAqshkypSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:TIGR00958 574 NIAYGLTDtpdeeimaaakAANAHDFIMEFPNGYDTEVGEKG------SQLSGGQKQRIAIARALVRKPRVLILDEATSA 647

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 166 LDALVRtHLRSEIRALQQRlgiTTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:TIGR00958 648 LDAECE-QLLQESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

9-223

8.16e-22

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.51 E-value: 8.16e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   9 QHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSY 86
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 ALFPNLTVAQNIAFG-LENQGLARDLIKERVD------HWLGLVDLTAQShkyPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:PRK10253   91 TTPGDITVQELVARGrYPHQPLFTRWRKEDEEavtkamQATGITHLADQS---VDTLSGGQRQRAWIAMVLAQETAIMLL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK10253  168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

20-223

1.02e-21

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.25 E-value: 1.02e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQ-RDFGIVF-----QSYALFPNLT 93
Cdd:COG3845   273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipedrLGRGLVPDMS 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIA-----------FGLENQGLARDLIKERVDHWlglvDLTAQSHKYP-SQISGGQQQRVALARalalspglllldE 161
Cdd:COG3845   353 VAENLIlgryrrppfsrGGFLDRKAIRAFAEELIEEF----DVRTPGPDTPaRSLSGGNQQKVILAR------------E 416

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 162 PLSALDALVRTH------------LRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:COG3845   417 LSRDPKLLIAAQptrgldvgaiefIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

1-223

1.11e-21

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 1.11e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ---QR 77
Cdd:PRK09700    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVFQSYALFPNLTVAQNIAFG--LENQGLARDLI-----KERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARAL 150
Cdd:PRK09700   81 GIGIIYQELSVIDELTVLENLYIGrhLTKKVCGVNIIdwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 151 ALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK09700  161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

20-220

1.13e-21

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: 97.01 E-value: 1.13e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-SQLPPQQRDFGIVFQSYALFPNLTVAQNI 98
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 AFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEI 178
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2051267523  179 raLQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTP 220
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

6-219

1.72e-21

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]

Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 1.72e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFG-AFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLppqqrDFGIVFQ 84
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-----DRHTLRQ 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNL------TVAQNIAFGlENQGLARDLIKERVDhwlgLVDLTAQSHKYP-----------SQISGGQQQRVALA 147
Cdd:TIGR01193 549 FINYLPQEpyifsgSILENLLLG-AKENVSQDEIWAACE----IAEIKDDIENMPlgyqtelseegSSISGGQKQRIALA 623

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 148 RALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlgiTTIMVTHDQEEAlTMADRIVVMEGGRIVQVGT 219
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGS 691

PRK10261

glutathione transporter ATP-binding protein; Provisional

2-243

3.28e-21

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 3.28e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKT----TLLRAI--AGLDLpDSGEIWQGGRN--- 68
Cdd:PRK10261    9 ARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLV-QCDKMLLRRRSrqv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  69 ---ISQLPPQQR-----DFGIVFQS--YALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDL-TAQS--HKYPS 134
Cdd:PRK10261   88 ielSEQSAAQMRhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpEAQTilSRYPH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 135 QISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK10261  168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2051267523 215 VQVGTPQEIYHQPASRFVASF------VGTMNFLD 243
Cdd:PRK10261  248 VETGSVEQIFHAPQHPYTRALlaavpqLGAMKGLD 282

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

4-195

3.80e-21

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: 94.73 E-value: 3.80e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQF-GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIV 82
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 F--QSYALFpNLTVAQNIAFG------------LENQGLArDLIKERVDHWLGLVDLTAQShkypsqISGGQQQRVALAR 148
Cdd:TIGR02868 413 VcaQDAHLF-DTTVRENLRLArpdatdeelwaaLERVGLA-DWLRALPDGLDTVLGEGGAR------LSGGERQRLALAR 484

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 149 ALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQrlGITTIMVTHD 195
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

6-213

5.61e-21

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: 87.89 E-value: 5.61e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGgrnisqlppqqrdfgivfqs 85
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 yalfPNLTVAqniafglenqglardlikervdhwlglvdltaqshkYPSQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03221    61 ----STVKIG------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 166 LDALVRTHLRSEIRALQQrlgiTTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:cd03221   101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

6-215

5.93e-21

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 5.93e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGR-NISQLpPQQRDfgivfq 84
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvKIGYF-DQHQE------ 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 syALFPNLTVAQNIafglenQGLARDLIKERVDHWLGLVDLT-AQSHKYPSQISGGQQQRVALARALALSPGLLLLDEP- 162
Cdd:COG0488   389 --ELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPt 460

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 163 ----LSALDALvrthlrseIRALQQRLGiTTIMVTHDQE--EALtmADRIVVMEGGRIV 215
Cdd:COG0488   461 nhldIETLEAL--------EEALDDFPG-TVLLVSHDRYflDRV--ATRILEFEDGGVR 508

PRK15112

peptide ABC transporter ATP-binding protein SapF;

6-237

9.48e-21

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 9.48e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQF----GAF-----QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWqggrnISQLPPQQ 76
Cdd:PRK15112    5 LEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-----IDDHPLHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 RDFG-------IVFQ--SYALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDLTA-QSHKYPSQISGGQQQRVA 145
Cdd:PRK15112   80 GDYSyrsqrirMIFQdpSTSLNPRQRISQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIY- 224
Cdd:PRK15112  160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLa 239

                         250
                  ....*....|....*.
gi 2051267523 225 ---HQPASRFVASFVG 237
Cdd:PRK15112  240 splHELTKRLIAGHFG 255

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

6-223

1.43e-20

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 1.43e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR---DFGIV 82
Cdd:PRK10895    4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK10895   84 PQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK10895  164 PFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

8-214

4.16e-20

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.16e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-QGGRNISQLPpqqrdfgivfQSY 86
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSiPKGLRIGYLP----------QEP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 ALFPNLTVAQNIAFGL--------------------ENQGLARDLIKERVDH---W------------LGLVDltAQSHK 131
Cdd:COG0488    71 PLDDDLTVLDTVLDGDaelraleaeleeleaklaepDEDLERLAELQEEFEAlggWeaearaeeilsgLGFPE--EDLDR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 132 YPSQISGGQQQRVALARALALSPGLLLLDEPlsaldalvrT-HLRSE-IRALQQRL---GITTIMVTHDQE--EAltMAD 204
Cdd:COG0488   149 PVSELSGGWRRRVALARALLSEPDLLLLDEP---------TnHLDLEsIEWLEEFLknyPGTVLVVSHDRYflDR--VAT 217

                         250
                  ....*....|
gi 2051267523 205 RIVVMEGGRI 214
Cdd:COG0488   218 RILELDRGKL 227

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

23-194

7.27e-20

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 7.27e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  23 GISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQgGRNISQLPPQqrdfgivFQSYALF--------PNLT 93
Cdd:PRK13538   19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlWQ-GEPIRRQRDE-------YHQDLLYlghqpgikTELT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFgleNQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD----AL 169
Cdd:PRK13538   91 ALENLRF---YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvAR 167

                         170       180
                  ....*....|....*....|....*
gi 2051267523 170 VRTHLRSEIRAlqqrlGITTIMVTH 194
Cdd:PRK13538  168 LEALLAQHAEQ-----GGMVILTTH 187

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

21-194

7.36e-20

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: 86.39 E-value: 7.36e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQLPPQQRDFGIVFQSYALFPNLTVAQNIA 99
Cdd:cd03231    16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVlLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 100 FglenqgLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIR 179
Cdd:cd03231    96 F------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169

                         170
                  ....*....|....*
gi 2051267523 180 ALQQRLGItTIMVTH 194
Cdd:cd03231   170 GHCARGGM-VVLTTH 183

COG4586

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

19-215

7.89e-20

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 7.89e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNisqlpPQQ------RDFGIVF-QSYALFPN 91
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaRRIGVVFgQRSQLWWD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNiaFGLeNQ---GLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:COG4586   111 LPAIDS--FRL-LKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2051267523 169 LVRTHLRSEIRALQQRLGITTIMVTHDQE--EALtmADRIVVMEGGRIV 215
Cdd:COG4586   188 VSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRII 234

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

19-223

2.04e-19

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 2.04e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpNLTVAQ 96
Cdd:PRK13657  349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIED 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLENQGLARDLIKERVDHWLGLVDltAQSHKYP-------SQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PRK13657  428 NIRVGRPDATDEEMRAAAERAQAHDFIE--RKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 170 VRTHLRSEIRALQQrlGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK13657  506 TEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

19-214

4.22e-19

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: 84.83 E-value: 4.22e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNlTVAQ 96
Cdd:cd03248    28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLenQGLARDLIKERVD--HWLGLVDLTAQSH-----KYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:cd03248   107 NIAYGL--QSCSFECVKEAAQkaHAHSFISELASGYdtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2051267523 170 VRTHLRseiRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:cd03248   185 SEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

PRK10762

D-ribose transporter ATP binding protein; Provisional

2-212

4.31e-19

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 4.31e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   2 TQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPP---QQRD 78
Cdd:PRK10762    1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYALFPNLTVAQNIAFGLE-NQGLARDLIKE---RVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSP 154
Cdd:PRK10762   81 IGIIHQELNLIPQLTIAENIFLGREfVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQ-QRLGITTImvTHDQEEALTMADRIVVMEGG 212
Cdd:PRK10762  161 KVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVYI--SHRLKEIFEICDDVTVFRDG 217

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

6-226

3.73e-18

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: 81.80 E-value: 3.73e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGldLPD----SGEIWQGGRNISQLPPQQR---D 78
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEERarlG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  79 FGIVFQSYALFPNLTVAQNIAFglENQGLardlikervdhwlglvdltaqshkypsqiSGGQQQRVALARALALSPGLLL 158
Cdd:cd03217    79 IFLAFQYPPEIPGVKNADFLRY--VNEGF-----------------------------SGGEKKRNEILQLLLLEPDLAI 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 159 LDEPLSALD-------ALVRTHLRSEiralqqrlGITTIMVTHDQEEALTM-ADRIVVMEGGRIVQVGtPQEIYHQ 226
Cdd:cd03217   128 LDEPDSGLDidalrlvAEVINKLREE--------GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194

PRK11176

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

20-223

7.21e-18

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 7.21e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTllraIAGL-----DLpDSGEIWQGGRNIS--QLPPQQRDFGIVFQSYALFpNL 92
Cdd:PRK11176  358 ALRNINFKIPAGKTVALVGRSGSGKST----IANLltrfyDI-DEGEILLDGHDLRdyTLASLRNQVALVSQNVHLF-ND 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQ------------GLARDLIkERVDHwlGLVDLTAQSHkypSQISGGQQQRVALARALALSPGLLLLD 160
Cdd:PRK11176  432 TIANNIAYARTEQysreqieeaarmAYAMDFI-NKMDN--GLDTVIGENG---VLLSGGQRQRIAIARALLRDSPILILD 505

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 161 EPLSALDAlvrthlRSEiRALQQRLGI-----TTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK11176  506 EATSALDT------ESE-RAIQAALDElqknrTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

21-194

9.65e-18

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 9.65e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQLPPQQ------RDfgivfqsyALFPNLT 93
Cdd:PRK13539   18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDPDVAEAchylghRN--------AMKPALT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQGLARDLIKERVDHWlGLVDLTAQSHKYpsqISGGQQQRVALARALALSPGLLLLDEPLSALDA----- 168
Cdd:PRK13539   90 VAENLEFWAAFLGGEELDIAAALEAV-GLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAaaval 165

                         170       180
                  ....*....|....*....|....*....
gi 2051267523 169 ---LVRTHLRSeiralqqrlGITTIMVTH 194
Cdd:PRK13539  166 faeLIRAHLAQ---------GGIVIAATH 185

PRK03695

vitamin B12-transporter ATPase; Provisional

24-223

1.08e-17

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 1.08e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPP------------QQRDFGI--VFQSYALF 89
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarhraylsqQQTPPFAmpVFQYLTLH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  90 -PNLTVAQNIAFGLenqglardlikERVDHWLGLVDLTAQShkyPSQISGGQQQRVALA-------RALALSPGLLLLDE 161
Cdd:PRK03695   94 qPDKTRTEAVASAL-----------NEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQrLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK03695  160 PMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220

PRK10789

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

20-227

1.17e-17

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.38 E-value: 1.17e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS--QLPPQQRDFGIVFQSYALFPNlTVAQN 97
Cdd:PRK10789  330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TVANN 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLEnqglarDLIKERVDHWLGLV----DLTAQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:PRK10789  409 IALGRP------DATQQEIEHVARLAsvhdDILRLPQGYDTEVgergvmlSGGQKQRISIARALLLNAEILILDDALSAV 482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 167 DALVRTHLRSEIRalQQRLGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PRK10789  483 DGRTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540

3a01204

TIGR00955

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

21-222

1.40e-17

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 1.40e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPD---SGEIWQGGRNISqLPPQQRDFGIVFQSYALFPNLTVAQN 97
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQgLARDLIK----ERVDHWL---GLV---DLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:TIGR00955 120 LMFQAHLR-MPRRVTKkekrERVDEVLqalGLRkcaNTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 168 ALVRTHLRSEIRALQQRlGITTIMVTHD-QEEALTMADRIVVMEGGRIVQVGTPQE 222
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

6-220

2.14e-17

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 2.14e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDL--PDSGEIWQGGRNISQLPPQQR-DFGI- 81
Cdd:COG0396     1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaRAGIf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 -VFQSYALFPNLTVAQNIAFGLENQGL----ARDLIKErVDHWLGLVDLtaqSHKYPSQ-----ISGGQQQRVALARALA 151
Cdd:COG0396    81 lAFQYPVEIPGVSVSNFLRTALNARRGeelsAREFLKL-LKEKMKELGL---DEDFLDRyvnegFSGGEKKRNEILQMLL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 152 LSPGLLLLDEPLSALD--ALvRThLRSEIRALQQRlGITTIMVTHdQEEALTM--ADRIVVMEGGRIVQVGTP 220
Cdd:COG0396   157 LEPKLAILDETDSGLDidAL-RI-VAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

13-215

2.20e-17

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: 79.61 E-value: 2.20e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  13 KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPD---SGEIWQGGRNISQLPPQ-QRDFGIVFQSYAL 88
Cdd:cd03233    15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  89 FPNLTVAQNIAFGLENQGlardlikervdhwlglvdltaqsHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:cd03233    95 FPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 169 LVRTHLRSEIRALQQRLGITTIM-VTHDQEEALTMADRIVVMEGGRIV 215
Cdd:cd03233   152 STALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

1-228

2.27e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 2.27e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLN----KQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD------SGEIWQGGRNIS 70
Cdd:PRK15134    1 MTQPLLAIENLSvafrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  71 QLPPQQ------RDFGIVFQS--YALFPNLTVAQNIAFGLE-NQGLARDLIK-------ERVdhwlGLVDLTAQSHKYPS 134
Cdd:PRK15134   80 HASEQTlrgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSlHRGMRREAARgeilnclDRV----GIRQAAKRLTDYPH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 135 QISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK15134  156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235

                         250
                  ....*....|....
gi 2051267523 215 VQVGTPQEIYHQPA 228
Cdd:PRK15134  236 VEQNRAATLFSAPT 249

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

9-223

2.62e-17

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 2.62e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   9 QHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnisqlPPQQRDF------GIV 82
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ-----PVDAGDIatrrrvGYM 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 FQSYALFPNLTVAQNIA-----FglenqGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLL 157
Cdd:NF033858  345 SQAFSLYGELTVRQNLElharlF-----HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 158 LLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEI 223
Cdd:NF033858  420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

21-212

2.83e-17

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 2.83e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIwqggrnisQLPPQQRdfgIVF---QSYalFPNLTVAQN 97
Cdd:COG4178   379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPY--LPLGTLREA 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 IAFGLENQGLARDLIKE-----RVDHWLGLVDLTAQSHKypsQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:COG4178   446 LLYPATAEAFSDAELREaleavGLGHLAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2051267523 173 HLrseIRALQQRL-GITTIMVTHdQEEALTMADRIVVMEGG 212
Cdd:COG4178   523 AL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559

PRK10575

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

21-223

3.00e-17

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 3.00e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNLTVAQNI 98
Cdd:PRK10575   27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFG-------LENQGLARdliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK10575  107 AIGrypwhgaLGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 172 THLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK10575  184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

1-228

3.36e-17

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.31 E-value: 3.36e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIwQG-----GRNISQ 71
Cdd:PRK09473    8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRI-GGsatfnGREILN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  72 LPPQQ------RDFGIVFQS--YALFPNLTVAQNIAFGLE-NQGLARDLIKERVDHWLGLVDLtAQSHK----YPSQISG 138
Cdd:PRK09473   86 LPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKM-PEARKrmkmYPHEFSG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 139 GQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:PRK09473  165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244

                         250
                  ....*....|
gi 2051267523 219 TPQEIYHQPA 228
Cdd:PRK09473  245 NARDVFYQPS 254

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

18-217

5.99e-17

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 5.99e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI---SQLPPQQRDFGIVFQSY---ALFPN 91
Cdd:PRK09700  276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYITESRrdnGFFPN 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  92 LTVAQNIAfglenqgLARDLIKERVDHWLGLVD-----LTAQSHKYPSQI------------SGGQQQRVALARALALSP 154
Cdd:PRK09700  356 FSIAQNMA-------ISRSLKDGGYKGAMGLFHevdeqRTAENQRELLALkchsvnqnitelSGGNQQKVLISKWLCCCP 428

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQV 217
Cdd:PRK09700  429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

8-235

7.87e-17

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 7.87e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIwqggrnisQLPPQQRdFGIVFQSYA 87
Cdd:PRK09544    7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQKLY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  88 LFPN--LTVAQniaFGLENQGLARDLIK---ERVDhwlglvdlTAQSHKYPSQ-ISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK09544   78 LDTTlpLTVNR---FLRLRPGTKKEDILpalKRVQ--------AGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDE 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEgGRIVQVGTPQEIYHQPasRFVASF 235
Cdd:PRK09544  147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

24-214

7.89e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 7.89e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQR-DFGIVF-----QSYALFPNLTVAQN 97
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 I-AFGLENQGL----ARD-LIKERVDHWLGL----VDLTAQShkypsqISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK15439  362 VcALTHNRRGFwikpAREnAVLERYRRALNIkfnhAEQAART------LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 168 ALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK15439  436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

6-228

1.37e-16

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 1.37e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGlDLPDS---------GEIWQGGRNISQLPPQQ 76
Cdd:PRK13547    2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 --RDFGIVFQ-SYALFPnLTVAQNIAFG----LENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARA 149
Cdd:PRK13547   81 laRLRAVLPQaAQPAFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 150 ---------LALSPGLLLLDEPLSALDALVRTHLRSEIRALQQ--RLGITTIMvtHDQEEALTMADRIVVMEGGRIVQVG 218
Cdd:PRK13547  160 laqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIV--HDPNLAARHADRIAMLADGAIVAHG 237

                         250
                  ....*....|
gi 2051267523 219 TPQEIYhQPA 228
Cdd:PRK13547  238 APADVL-TPA 246

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

21-223

1.56e-16

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: 81.15 E-value: 1.56e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGrNISQLPPQqrdfgivfqsyALFPNLTVAQNIAF 100
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQ-----------AWIQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  101 GlenQGLARDLIKERVDHWLGLVDLTAQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDALVRTH 173
Cdd:TIGR00957  722 G---KALNEKYYQQVLEACALLPDLEILPSGDRTEIgekgvnlSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523  174 LRSEIRALQQRL-GITTIMVTHDQeEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR00957  799 IFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848

PLN03211

ABC transporter G-25; Provisional

21-218

2.76e-16

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 2.76e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDS--GEIWQGGRNISQlpPQQRDFGIVFQSYALFPNLTVAQNI 98
Cdd:PLN03211   84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AF----GLENQgLARD---LIKERVDHWLGLVDL--TAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PLN03211  162 VFcsllRLPKS-LTKQekiLVAESVISELGLTKCenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2051267523 170 VRTHLRSEIRALQQRlGITTIMVTHD-QEEALTMADRIVVMEGGRIVQVG 218
Cdd:PLN03211  241 AAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289

SapD

COG4170

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

4-227

4.14e-16

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.41 E-value: 4.14e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHL----NKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEI-----WQGGRNISQLPP 74
Cdd:COG4170     2 PLLDIRNLtieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  75 QQR------DFGIVFQ--SYALFPNLTVAQNIAFGLENQGL---------ARdliKERVDHWLGLVDLtaQSHK-----Y 132
Cdd:COG4170    81 RERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFkgkwwqrfkWR---KKRAIELLHRVGI--KDHKdimnsY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 133 PSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGG 212
Cdd:COG4170   156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG 235

                         250
                  ....*....|....*
gi 2051267523 213 RIVQVGTPQEIYHQP 227
Cdd:COG4170   236 QTVESGPTEQILKSP 250

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

6-204

4.38e-16

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 4.38e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ-LPPQQRDFGIVFQ 84
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 SYALFPNLTVAQNIAFGLENQGLARDLIKervdhwlgLVDLTAQSH--KYP-SQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK13540   82 RSGINPYLTLRENCLYDIHFSPGAVGITE--------LCRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGitTIMVTHDQEEALTMAD 204
Cdd:PRK13540  154 PLVALDELSLLTIITKIQEHRAKGG--AVLLTSHQDLPLNKAD 194

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

22-230

1.63e-15

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 1.63e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  22 KGISLTIEPGEFICFLGPSGCGKTtlLRAIAGLD-LP-----DSGEIWQGGRNISQLPPQQRDFGIVFQS--YALFPNLT 93
Cdd:PRK10418   20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGiLPagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFGLENQG-LARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:PRK10418   98 MHTHARETCLALGkPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 173 HLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASR 230
Cdd:PRK10418  178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235

PRK10762

D-ribose transporter ATP binding protein; Provisional

21-214

4.98e-15

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 4.98e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGlDLP-DSGEIWQGGRNISQLPPQQR-DFGIVFQSY-----ALFPNLT 93
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPrTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMS 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VAQNIAFG----LENQGLARDLIKER--VDHWLGLVDLtaqshKYPSQ------ISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK10762  347 VKENMSLTalryFSRAGGSLKHADEQqaVSDFIRLFNI-----KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK10762  422 PTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473

PLN03130

ABC transporter C family member; Provisional

21-223

1.19e-14

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 1.19e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGldlpdsgeiwqggrnisQLPPQQRDFGIVFQSYALFP------NLTV 94
Cdd:PLN03130   633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPqvswifNATV 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   95 AQNIAFGLENQ-----------GLARDLikervdHWLGLVDLTAQSHKyPSQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:PLN03130   696 RDNILFGSPFDperyeraidvtALQHDL------DLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523  164 SALDALV-----RTHLRSEIRalqqrlGITTIMVThDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PLN03130   769 SALDAHVgrqvfDKCIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826

PTZ00243

ABC transporter; Provisional

21-227

2.48e-14

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 2.48e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWqGGRNISQLPPQqrdfgivfqsyALFPNLTVAQNIAF 100
Cdd:PTZ00243   676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSIAYVPQQ-----------AWIMNATVRGNILF 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  101 GLENQglARDLIKE-RVDHWLGlvDLTAQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:PTZ00243   744 FDEED--AARLADAvRVSQLEA--DLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523  173 HLRSEIrALQQRLGITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQP 227
Cdd:PTZ00243   820 RVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

21-211

3.70e-14

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: 69.49 E-value: 3.70e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdlpdsgeiWQGGRNISQLPPQQRDFGIVFQSYalFPNLTVAQNIAf 100
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL--------WPWGSGRIGMPEGEDLLFLPQRPY--LPLGTLREQLI- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 101 glenqglardlikervdhwlglvdltaqshkYPSQ--ISGGQQQRVALARALALSPGLLLLDEPLSALDAlvrthlRSEI 178
Cdd:cd03223    86 -------------------------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE------ESED 128

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2051267523 179 RALQ--QRLGITTIMVTHdQEEALTMADRIVVMEG 211
Cdd:cd03223   129 RLYQllKELGITVISVGH-RPSLWKFHDRVLDLDG 162

PLN03232

ABC transporter C family member; Provisional

21-224

4.50e-14

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.86 E-value: 4.50e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGldlpdsgeiwqggrnisQLPPQQRDFGIVFQSYALFP------NLTV 94
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPqvswifNATV 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   95 AQNIAFG--LENQGLARDLIKERVDHWLGLV---DLTAQSHKyPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PLN03232   696 RENILFGsdFESERYWRAIDVTALQHDLDLLpgrDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  170 VRTH-----LRSEIRalqqrlGITTIMVThDQEEALTMADRIVVMEGGRIVQVGTPQEIY 224
Cdd:PLN03232   775 VAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

21-195

5.79e-14

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 5.79e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-QGGRNISQLPpqqrdfgivfQSYALFPNLTVAQNIA 99
Cdd:TIGR03719  21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpQPGIKVGYLP----------QEPQLDPTKTVRENVE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 100 FGLEN--QGLAR----------------DLIKE------RVDHWLGL-----VDLTAQSHKYP------SQISGGQQQRV 144
Cdd:TIGR03719  91 EGVAEikDALDRfneisakyaepdadfdKLAAEqaelqeIIDAADAWdldsqLEIAMDALRCPpwdadvTKLSGGERRRV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRseiRALQQRLGiTTIMVTHD 195
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHD 217

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

18-197

6.80e-14

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 6.80e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAG--LDLPDSGEIwqggrNISQLPPQQRDFGIvfqsYALFPNLTVA 95
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV-----DVPDNQFGREASLI----DAIGRKGDFK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFgLENQGLArdlikervDHWLGLvdltaqshKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLR 175
Cdd:COG2401   114 DAVEL-LNAVGLS--------DAVLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176

                         170       180
                  ....*....|....*....|..
gi 2051267523 176 SEIRALQQRLGITTIMVTHDQE 197
Cdd:COG2401   177 RNLQKLARRAGITLVVATHHYD 198

3a01205

TIGR00956

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

18-242

1.02e-13

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.02e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   18 FQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIA----GLDLPDSGEIWQGGRNISQLPPQQRdfGIVFQSYAL---FP 90
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYR--GDVVYNAETdvhFP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   91 NLTVAQNIAF-------GLENQGLARdliKERVDHwlgLVDLTAQ----SHKYPSQ--------ISGGQQQRVALARALA 151
Cdd:TIGR00956  152 HLTVGETLDFaarcktpQNRPDGVSR---EEYAKH---IADVYMAtyglSHTRNTKvgndfvrgVSGGERKRVSIAEASL 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  152 LSPGLLLLDEPLSALDAlvRTHLRSeIRALQQRLGI--TTIMVTHDQ--EEALTMADRIVVMEGGRIvqvgtpqeIYHQP 227
Cdd:TIGR00956  226 GGAKIQCWDNATRGLDS--ATALEF-IRALKTSANIldTTPLVAIYQcsQDAYELFDKVIVLYEGYQ--------IYFGP 294

                          250
                   ....*....|....*
gi 2051267523  228 ASRfVASFVGTMNFL 242
Cdd:TIGR00956  295 ADK-AKQYFEKMGFK 308

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

24-221

1.16e-13

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: 72.14 E-value: 1.16e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGE--FICflGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnisQLPPQQRD-----FGIVFQSYALFPNLtvaq 96
Cdd:COG4615   351 IDLTIRRGElvFIV--GGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREayrqlFSAVFSDFHLFDRL---- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 niaFGLENQGLArdlikERVDHWLGLVDLtaqSHKYPSQ--------ISGGQQQRVALaralalspglllldepLSAL-- 166
Cdd:COG4615   422 ---LGLDGEADP-----ARARELLERLEL---DHKVSVEdgrfsttdLSQGQRKRLAL----------------LVALle 474

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267523 167 --------------DALVR----THLRSEIRAlqqrLGITTIMVTHDqEEALTMADRIVVMEGGRIVQVGTPQ 221
Cdd:COG4615   475 drpilvfdewaadqDPEFRrvfyTELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

20-214

2.63e-13

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 2.63e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNLtvaqn 97
Cdd:PRK10522  338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQL----- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  98 iafgLENQGLARDliKERVDHW---LGLVD-LTAQSHKYPS-QISGGQQQRVALARALALSPGLLLLDEPLSALDALVRT 172
Cdd:PRK10522  413 ----LGPEGKPAN--PALVEKWlerLKMAHkLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2051267523 173 HLRSEIRALQQRLGITTIMVTHDqEEALTMADRIVVMEGGRI 214
Cdd:PRK10522  487 EFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527

PLN03232

ABC transporter C family member; Provisional

10-231

3.28e-13

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 3.28e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   10 HLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSYA 87
Cdd:PLN03232  1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPV 1320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   88 LFPNlTVAQNI-AFGLEN-----QGLARDLIKERVDHwlGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PLN03232  1321 LFSG-TVRFNIdPFSEHNdadlwEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523  162 PLSAL----DALVRTHLRSEIRAlqqrlgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRF 231
Cdd:PLN03232  1398 ATASVdvrtDSLIQRTIREEFKS-------CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

6-195

6.29e-13

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 6.29e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGgrnisqlppQQRDFGIVFQS 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVKLAYVDQS 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 Y-ALFPNLTVAQNIAFGLENQGLARDLIKERVdhWLGLVDLTAQ-SHKYPSQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2051267523 164 SALDalVRThLRSEIRALQQRLGiTTIMVTHD 195
Cdd:TIGR03719 472 NDLD--VET-LRALEEALLNFAG-CAVVISHD 499

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

21-212

6.46e-13

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

Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.36 E-value: 6.46e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQLPPQQRDFGIVFQSYAL----FPNLTVA 95
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRNRYSVAYAAqkpwLLNATVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGlenQGLARDLIKERVDHWLGLVDLTAQSHKYPSQI-------SGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:cd03290    97 ENITFG---SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIgerginlSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2051267523 169 LVRTHLRSE-IRALQQRLGITTIMVTHdQEEALTMADRIVVMEGG 212
Cdd:cd03290   174 HLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

24-215

9.07e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 9.07e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNIS------------QLPPQQRDF-GIVfqsyalfP 90
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagiMLCPEDRKAeGII-------P 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  91 NLTVAQNIAFGLENQGL-ARDLIKERVDhwlglvDLTAQSH------KYPS------QISGGQQQRVALARALALSPGLL 157
Cdd:PRK11288  345 VHSVADNINISARRHHLrAGCLINNRWE------AENADRFirslniKTPSreqlimNLSGGNQQKAILGRWLSEDMKVI 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 158 LLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:PRK11288  419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

19-211

1.36e-12

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 1.36e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEF-----ICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ-QRDFgivfqsyalfpnl 92
Cdd:cd03237     8 KTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADY------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 tvaqniafglenQGLARDLIKERVDhwlglvdlTAQSHKY-------PSQI-----------SGGQQQRVALARALALSP 154
Cdd:cd03237    75 ------------EGTVRDLLSSITK--------DFYTHPYfkteiakPLQIeqildrevpelSGGELQRVAIAACLSKDA 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523 155 GLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:cd03237   135 DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

6-216

1.41e-12

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 1.41e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD---SGEIWQGG-----RNISQlppqQR 77
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGevcrfKDIRD----SE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  78 DFGIVF--QSYALFPNLTVAQNIAFGLENQ--GL---------ARDLIKErvdhwlglVDLTAQSHKYPSQISGGQQQRV 144
Cdd:NF040905   77 ALGIVIihQELALIPYLSIAENIFLGNERAkrGVidwnetnrrARELLAK--------VGLDESPDTLVTDIGVGKQQLV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQ 216
Cdd:NF040905  149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219

PLN03130

ABC transporter C family member; Provisional

21-256

1.62e-12

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 1.62e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSYALFPNlTVAQNI 98
Cdd:PLN03130  1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGIIPQAPVLFSG-TVRFNL 1333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 -AFGLEN-----QGLARDLIKERV-DHWLGlvdLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL----D 167
Cdd:PLN03130  1334 dPFNEHNdadlwESLERAHLKDVIrRNSLG---LDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtD 1410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  168 ALVRTHLRSEIRAlqqrlgITTIMVTHdQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRF---VASfVGTMN--FL 242
Cdd:PLN03130  1411 ALIQKTIREEFKS------CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFskmVQS-TGAANaqYL 1482

                          250
                   ....*....|....
gi 2051267523  243 DTLVLSPTQVRLNE 256
Cdd:PLN03130  1483 RSLVFGGDEDRLAR 1496

PRK15093

peptide ABC transporter ATP-binding protein SapD;

4-258

2.25e-12

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 2.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   4 PYLDIQHLNKQF----GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdlpdSGEIWQ--GGR------NISQ 71
Cdd:PRK15093    2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----TKDNWRvtADRmrfddiDLLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  72 LPPQQR------DFGIVFQ--SYALFPNLTVA----QNIAfGLENQGLARDLIKER------VDHWLGLVDLTAQSHKYP 133
Cdd:PRK15093   78 LSPRERrklvghNVSMIFQepQSCLDPSERVGrqlmQNIP-GWTYKGRWWQRFGWRkrraieLLHRVGIKDHKDAMRSFP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 134 SQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGR 213
Cdd:PRK15093  157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2051267523 214 IVQVGTPQEIYHQPASRFVASFVGTM-NFLDTLvlsPTQVRLNEQP 258
Cdd:PRK15093  237 TVETAPSKELVTTPHHPYTQALIRAIpDFGSAM---PHKSRLNTLP 279

ycf16

CHL00131

sulfate ABC transporter protein; Validated

1-219

2.94e-12

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 2.94e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGldLPD----SGEIWQGGRNISQLPPQQ 76
Cdd:CHL00131    3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  77 R---------------------DF-GIVFQSYALFPNLTVAQNIAFgLEnqglardLIKERVDhwlgLVDLTAQS-HKYP 133
Cdd:CHL00131   81 RahlgiflafqypieipgvsnaDFlRLAYNSKRKFQGLPELDPLEF-LE-------IINEKLK----LVGMDPSFlSRNV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 134 SQ-ISGGQQQRVALARALALSPGLLLLDEPLSALDalvrthlrseIRALQQ-RLGITTIM--------VTHDQEealtMA 203
Cdd:CHL00131  149 NEgFSGGEKKRNEILQMALLDSELAILDETDSGLD----------IDALKIiAEGINKLMtsensiilITHYQR----LL 214

                         250       260
                  ....*....|....*....|.
gi 2051267523 204 DRIV-----VMEGGRIVQVGT 219
Cdd:CHL00131  215 DYIKpdyvhVMQNGKIIKTGD 235

40850658_otr

NF000106

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

6-255

3.39e-12

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 3.39e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCG--KTTLLRAIAGldlPDSGE-IWQGGRNISQLPPQQRDFGI- 81
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrPWRF*TWCANRRALRRTIG*h 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  82 ------VFQSYALFPNLTVaqnIAFGLEnqgLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPG 155
Cdd:NF000106   91 rpvr*gRRESFSGRENLYM---IGR*LD---LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 156 LLLLDEPLSALDALVRTHLRSEIRALqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQPASRFVASF 235
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIR 243

                         250       260
                  ....*....|....*....|
gi 2051267523 236 VGTMNFLDTLVLSPTQVRLN 255
Cdd:NF000106  244 PAHAAELDRMVGAIAQAGLD 263

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

19-220

4.15e-12

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.74 E-value: 4.15e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNlTVAQ 96
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLFSG-TIRS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIafglenqglarDLIKERVDHWLglvdLTAQSHKYP-SQISGGQQQRVALARALALSPGLLLLDEPLSAL----DALVR 171
Cdd:cd03369   101 NL-----------DPFDEYSDEEI----YGALRVSEGgLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQ 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2051267523 172 THLRSEIRAlqqrlgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTP 220
Cdd:cd03369   166 KTIREEFTN-------STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207

PRK10790

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

21-223

8.25e-12

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 8.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFPNlTVAQNI 98
Cdd:PRK10790  357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLANV 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 AFGlenqglaRDLIKERVDHWLGLVDLTAQSHKYPSQI-----------SGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK10790  436 TLG-------RDISEEQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLALARVLVQTPQILILDEATANID 508

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 168 ALVRTHLRSEIRALQQRlgiTTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK10790  509 SGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

21-226

1.19e-11

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: 64.49 E-value: 1.19e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnISQLPpqqrdfgivfQSYALFPNlTVAQNIAF 100
Cdd:cd03291    53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS----------QFSWIMPG-TIKENIIF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 101 GLE-NQGLARDLIKErvdhwlglVDLTAQSHKYPSQ-----------ISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:cd03291   121 GVSyDEYRYKSVVKA--------CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 169 LVRTHLRS----EIRALQQRLGITTIMvthdqeEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:cd03291   193 FTEKEIFEscvcKLMANKTRILVTSKM------EHLKKADKILILHEGSSYFYGTFSELQSL 248

PRK13543

heme ABC exporter ATP-binding protein CcmA;

28-211

3.66e-11

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 3.66e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  28 IEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQlppQQRDFGIVFQSY--ALFPNLTVAQNIAFgleNQ 105
Cdd:PRK13543   34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHlpGLKADLSTLENLHF---LC 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 106 GLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDaLVRTHLRSEIRALQQRL 185
Cdd:PRK13543  108 GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISAHLRG 186

                         170       180
                  ....*....|....*....|....*.
gi 2051267523 186 GITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:PRK13543  187 GGAALVTTHGAYAAPPVRTRMLTLEA 212

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

1-211

4.43e-11

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 4.43e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   1 MTQPYLDIQHLNKQFGAFqalkgiSLTIEPG-----EFICFLGPSGCGKTTLLRAIAGLDLPDSGEIwQGGRNISqLPPQ 75
Cdd:COG1245   337 EEETLVEYPDLTKSYGGF------SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKIS-YKPQ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 --QRDFgivfqsyalfpNLTVAQNIafglenqglaRDLIKERVD-HW--------LGLVDLTaqsHKYPSQISGGQQQRV 144
Cdd:COG1245   409 yiSPDY-----------DGTVEEFL----------RSANTDDFGsSYykteiikpLGLEKLL---DKNVKDLSGGELQRV 464

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 145 ALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDqeeaLTM----ADRIVVMEG 211
Cdd:COG1245   465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVFEG 531

PRK11147

ABC transporter ATPase component; Reviewed

26-215

4.78e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 4.78e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  26 LTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQL---PPQQRDfGIVFqSYalfpnltvaqnIAFG 101
Cdd:PRK11147   24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARLqqdPPRNVE-GTVY-DF-----------VAEG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 102 LENQG--------LARDL--------------IKERVDH---W---------LGLVDLTAqsHKYPSQISGGQQQRVALA 147
Cdd:PRK11147   91 IEEQAeylkryhdISHLVetdpseknlnelakLQEQLDHhnlWqlenrinevLAQLGLDP--DAALSSLSGGWLRKAALG 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 148 RALALSPGLLLLDEPLSALDalVRThlrseIRALQQRL----GiTTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:PRK11147  169 RALVSNPDVLLLDEPTNHLD--IET-----IEWLEGFLktfqG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

21-223

5.16e-11

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: 62.56 E-value: 5.16e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPPQQ--RDFGIVFQSYALFPNlTVAQNi 98
Cdd:cd03289    20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-TFRKN- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  99 afgLENQGLARDLIKERVDHWLGLVDLTAQshkYPSQ-----------ISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:cd03289    97 ---LDPYGKWSDEEIWKVAEEVGLKSVIEQ---FPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 168 ALVRTHLRseiRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:cd03289   171 PITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

21-223

5.89e-11

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: 64.16 E-value: 5.89e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnISQLPpqqrdfgivfQSYALFPNlTVAQNIAF 100
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP----------QTSWIMPG-TIKDNIIF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  101 GLE-NQGLARDLIKErvdhwlglVDLTAQSHKYPSQ-----------ISGGQQQRVALARALALSPGLLLLDEPLSALDA 168
Cdd:TIGR01271  510 GLSyDEYRYTSVIKA--------CQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523  169 LVRTHLRSeiRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR01271  582 VTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634

PRK15056

manganese/iron ABC transporter ATP-binding protein;

20-211

7.98e-11

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 7.98e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQlPPQQRDFGIVFQSYAL---FPNLT--- 93
Cdd:PRK15056   22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQSEEVdwsFPVLVedv 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 --VAQNIAFGLENQGLARDliKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:PRK15056  101 vmMGRYGHMGWLRRAKKRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2051267523 172 THLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:PRK15056  179 ARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKG 217

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

19-195

4.73e-10

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 4.73e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-QGGRNISQLP--PQqrdfgivfqsyaLFPNLTVA 95
Cdd:PRK11819   21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpAPGIKVGYLPqePQ------------LDPEKTVR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNI--AFGLENQGLAR----------------DLIKE------RVDHWlGLVDLTAQ------SHKYP------SQISGG 139
Cdd:PRK11819   89 ENVeeGVAEVKAALDRfneiyaayaepdadfdALAAEqgelqeIIDAA-DAWDLDSQleiamdALRCPpwdakvTKLSGG 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 140 QQQRVALARALALSPGLLLLDEPLSALDAlvrthlrsEIRA-LQQRL----GiTTIMVTHD 195
Cdd:PRK11819  168 ERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAwLEQFLhdypG-TVVAVTHD 219

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

20-239

7.25e-10

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 7.25e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI-SQLPPQQRDFGIVFQSYALFPNLTVAQNI 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 AFGLENQGLARDLIkERVDHW-LGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSE 177
Cdd:TIGR01257 2034 YLYARLRGVPAEEI-EKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267523  178 IRALqQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIyhqpASRFVASFVGTM 239
Cdd:TIGR01257 2113 IVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYIVTM 2169

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

8-223

9.55e-10

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 9.55e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   8 IQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIW-----------------------Q 64
Cdd:NF033858    4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhrravcpriaympQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  65 G-GRNisqlppqqrdfgivfqsyaLFPNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQR 143
Cdd:NF033858   84 GlGKN-------------------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 144 VALARALALSPGLLLLDEPLSALDALVRTH---LRSEIRAlqQRLGITTIMVTHDQEEALTMaDRIVVMEGGRIVQVGTP 220
Cdd:NF033858  145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221


                  ...
gi 2051267523 221 QEI 223
Cdd:NF033858  222 AEL 224

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

24-214

9.68e-10

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 9.68e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD--SGEIWQGGRNISQLPPQQR-DFGIVF-----QSYALFPNLTVA 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGkfEGNVFINGKPVDIRNPAQAiRAGIAMvpedrKRHGIVPILGVG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIAFGLENQGLARDLIKER-----VDHWLGLVDLTAQSHKYP-SQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAaelqiIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2051267523 170 VRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

11-215

2.10e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 2.10e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNI---SQLPPQQRDFGIVFQSYA 87
Cdd:PRK10982    4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  88 LFPNLTVAQNIAFG--------LENQGLARDLIKERVDhwlglVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLL 159
Cdd:PRK10982   84 LVLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFDE-----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523 160 DEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIV 215
Cdd:PRK10982  159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213

PRK15064

ABC transporter ATP-binding protein; Provisional

6-63

2.87e-09

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.87e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI-W 63
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW 378

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

11-211

3.16e-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: 55.66 E-value: 3.16e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFQalkgisLTIEPGEF-----ICFLGPSGCGKTTLLRAIAGLDLPDSGEI-WQGGRNISQlpPQQRDfgivfq 84
Cdd:cd03222     6 CVKRYGVFF------LLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDNDeWDGITPVYK--PQYID------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  85 syalfpnltvaqniafglenqglardlikervdhwlglvdltaqshkypsqISGGQQQRVALARALALSPGLLLLDEPLS 164
Cdd:cd03222    72 ---------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSA 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 165 ALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:cd03222   101 YLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147

PRK13549

xylose transporter ATP-binding subunit; Provisional

24-214

5.25e-09

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 5.25e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPD--SGEIWQGGRNISQLPPQQR-DFGIVF-----QSYALFPNLTVA 95
Cdd:PRK13549  281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGA-YPGrwEGEIFIDGKPVKIRNPQQAiAQGIAMvpedrKRDGIVPVMGVG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  96 QNIA---------FGLENQGLARDLIKERVDHwlgLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:PRK13549  360 KNITlaaldrftgGSRIDDAAELKTILESIQR---LKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2051267523 167 DALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PRK13549  437 DVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

2-223

6.77e-09

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 6.77e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523    2 TQPYLDIQHLNKQF--GAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLdLPDSGEIWQGGRNISQLPPQQ--R 77
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTwrK 1292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   78 DFGIVFQSYALFPNlTVAQNiafgLENQGLARDLIKERVDHWLGLVDLTAQshkYPSQ-----------ISGGQQQRVAL 146
Cdd:TIGR01271 1293 AFGVIPQKVFIFSG-TFRKN----LDPYEQWSDEEIWKVAEEVGLKSVIEQ---FPDKldfvlvdggyvLSNGHKQLMCL 1364

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523  147 ARALALSPGLLLLDEPLSALDALVRTHLRseiRALQQRLGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

11-211

7.65e-09

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 7.65e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  11 LNKQFGAFqalkgiSLTIEPG-----EFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRnISqLPPQ--QRDFgivf 83
Cdd:PRK13409  346 LTKKLGDF------SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-IS-YKPQyiKPDY---- 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  84 qsyalfpNLTVAQNiafgLENQG--LARDLIKERVDHWLGLVDLTaqsHKYPSQISGGQQQRVALARALALSPGLLLLDE 161
Cdd:PRK13409  414 -------DGTVEDL----LRSITddLGSSYYKSEIIKPLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 162 PLSALDALVRTHLRSEIRALQQRLGITTIMVTHDqeeaLTM----ADRIVVMEG 211
Cdd:PRK13409  480 PSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVFEG 529

TOBE_2

pfam08402

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...

273-359

7.80e-09

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: 51.85 E-value: 7.80e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 273 VAIRPEAITLSApselslGQHGIEATIDQVEFLGAAQRLICTADtylGPQQILVERPTHELPRHEQGGwrsgmRCSLHWP 352
Cdd:pfam08402   1 LAIRPEKIRLAA------AANGLSGTVTDVEYLGDHTRYHVELA---GGEELVVRVPNAHARPPAPGD-----RVGLGWD 66


                  ....*..
gi 2051267523 353 AGAMQLF 359
Cdd:pfam08402  67 PEDAHVL 73

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

6-195

1.86e-08

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.86e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGgrnisqlppQQRDFGIVFQS 85
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG---------ETVKLAYVDQS 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  86 Y-ALFPNLTVAQNIAFGLenqglarDLIKervdhwLGLVDLTAQSH------------KYPSQISGGQQQRVALARALAL 152
Cdd:PRK11819  396 RdALDPNKTVWEEISGGL-------DIIK------VGNREIPSRAYvgrfnfkggdqqKKVGVLSGGERNRLHLAKTLKQ 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2051267523 153 SPGLLLLDEPLSALDalVRThLRSEIRALQQRLGiTTIMVTHD 195
Cdd:PRK11819  463 GGNVLLLDEPTNDLD--VET-LRALEEALLEFPG-CAVVISHD 501

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

25-226

2.56e-08

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 2.56e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  25 SLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGE----------------------IWQGgRNISQLPPQQRDFGiv 82
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrlsfeqlqklvsdEWQR-NNTDMLSPGEDDTG-- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  83 fqsyalfpnLTVAQNIAFGLENQGLARDLIKErvdhwLGLVDLTAQSHKYpsqISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:PRK10938  100 ---------RTTAEIIQDEVKDPARCEQLAQQ-----FGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 163 LSALDALVRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:PRK10938  163 FDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225

PTZ00265

multidrug resistance protein (mdr1); Provisional

58-223

2.63e-08

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.63e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   58 DSGEIWQGGRNIS--QLPPQQRDFGIVFQSYALFpNLTVAQNIAFGLENQglARDLIKeRVDHWLGLVD-LTAQSHKYPS 134
Cdd:PTZ00265  1275 NSGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDA--TREDVK-RACKFAAIDEfIESLPNKYDT 1350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  135 QI-------SGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHdQEEALTMADRIV 207
Cdd:PTZ00265  1351 NVgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIV 1429

                          170       180
                   ....*....|....*....|.
gi 2051267523  208 VMEG----GRIVQV-GTPQEI 223
Cdd:PTZ00265  1430 VFNNpdrtGSFVQAhGTHEEL 1450

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

30-206

1.56e-07

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 1.56e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   30 PGEFICFLGPSGCGKTTLLRAIAGldlpdsgeiwqggrnisQLPPQQRDFGIVfqsyalfpnltvaqNIAFGLENQGLAR 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-----------------ELGPPGGGVIYI--------------DGEDILEEVLDQL 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  110 DLIKERVDHWLGlvdltaqshkypsqiSGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRA-----LQQR 184
Cdd:smart00382  50 LLIIVGGKKASG---------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114

                          170       180
                   ....*....|....*....|..
gi 2051267523  185 LGITTIMVTHDQEEALTMADRI 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136

PTZ00243

ABC transporter; Provisional

21-231

3.23e-07

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 3.23e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQ--LPPQQRDFGIVFQSYALFPNlTVAQNI 98
Cdd:PTZ00243  1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 AFGLENQG----LARDLI--KERVDHWLGLVDLTAQSHKypSQISGGQQQRVALARALALSPGL-LLLDEPLS----ALD 167
Cdd:PTZ00243  1405 DPFLEASSaevwAALELVglRERVASESEGIDSRVLEGG--SNYSVGQRQLMCMARALLKKGSGfILMDEATAnidpALD 1482

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267523  168 ALVRTHLRSEIRALqqrlgiTTIMVTHDQEealTMA--DRIVVMEGGRIVQVGTPQEIYHQPASRF 231
Cdd:PTZ00243  1483 RQIQATVMSAFSAY------TVITIAHRLH---TVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

24-185

3.76e-07

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 3.76e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLppQQRDFGIVFQSYALFPNLTVAQNIAFGLE 103
Cdd:PRK13541   19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKFWSE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 104 NQGLArDLIKERVdHWLGLVDLTAqshKYPSQISGGQQQRVALARALALSPGLLLLDEplsaldalVRTHLRSEIRALQQ 183
Cdd:PRK13541   97 IYNSA-ETLYAAI-HYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDE--------VETNLSKENRDLLN 163


                  ..
gi 2051267523 184 RL 185
Cdd:PRK13541  164 NL 165

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

3-199

4.00e-07

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 4.00e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   3 QPYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGlDLPD--------------SGE-IWQGGR 67
Cdd:PRK10938  258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGEtIWDIKK 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  68 NI----SQLPPQQRdfgivfqsyalfPNLTVAQNIAFG-LENQGLAR---DLIKERVDHWLGLVDLTAQSHKYPSQ-ISG 138
Cdd:PRK10938  337 HIgyvsSSLHLDYR------------VSTSVRNVILSGfFDSIGIYQavsDRQQKLAQQWLDILGIDKRTADAPFHsLSW 404

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 139 GQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTHDQEEA 199
Cdd:PRK10938  405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

10-223

8.44e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 8.44e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  10 HLNKqfgAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGrnisqlppqqrDFGIVFQSYALF 89
Cdd:PRK13546   32 HKNK---TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  90 PNLTVAQNIAFGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:PRK13546   98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 170 VRTHLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEGGRIVQVGTPQEI 223
Cdd:PRK13546  178 FAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230

PRK11147

ABC transporter ATPase component; Reviewed

7-197

1.09e-06

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 1.09e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   7 DIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDfgivfqsy 86
Cdd:PRK11147  321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRA-------- 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  87 ALFPNLTVAQNIAFG---LENQGLARdlikervdHWLGLVdltaQSHKYPSQ--------ISGGQQQRVALARALALSPG 155
Cdd:PRK11147  393 ELDPEKTVMDNLAEGkqeVMVNGRPR--------HVLGYL----QDFLFHPKramtpvkaLSGGERNRLLLARLFLKPSN 460

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2051267523 156 LLLLDEPLSALDalVRT-HLRSEIRALQQrlGiTTIMVTHDQE 197
Cdd:PRK11147  461 LLILDEPTNDLD--VETlELLEELLDSYQ--G-TVLLVSHDRQ 498

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

21-218

1.61e-06

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: 48.41 E-value: 1.61e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLL---------------------RAIAGLDLPDSgeiwqggRNISQLPP----Q 75
Cdd:cd03270    11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDV-------DSIEGLSPaiaiD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  76 QRDF--------GIVFQSYALFPNLtvaqniafglenqgLARDLIKERVDHW--LGLVDLTAqSHKYPSqISGGQQQRVA 145
Cdd:cd03270    84 QKTTsrnprstvGTVTEIYDYLRLL--------------FARVGIRERLGFLvdVGLGYLTL-SRSAPT-LSGGEAQRIR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 146 LARALALSPGLLL--LDEPLSALDALVRTHLRSEIRALQQrLGITTIMVTHDqEEALTMADRIVVM------EGGRIVQV 217
Cdd:cd03270   148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHD-EDTIRAADHVIDIgpgagvHGGEIVAQ 225


                  .
gi 2051267523 218 G 218
Cdd:cd03270   226 G 226

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

42-229

1.92e-06

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: 49.63 E-value: 1.92e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  42 CGKTTLLRA-----IAGLDLPDsgeiwqggrnISQLPpqqrdfgiVFQSYALFPNLTVaqniafGLENQGLARDLIKERV 116
Cdd:TIGR00630 411 CGGTRLKPEalavtVGGKSIAD----------VSELS--------IREAHEFFNQLTL------TPEEKKIAEEVLKEIR 466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 117 DHWLGLVDLtAQSHKYPSQ----ISGGQQQRVALAR--ALALSPGLLLLDEPLSAL-----DALVRT--HLRSeiralqq 183
Cdd:TIGR00630 467 ERLGFLIDV-GLDYLSLSRaagtLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLhqrdnRRLINTlkRLRD------- 538

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 184 rLGITTIMVTHDqEEALTMADRIVVM------EGGRIVQVGTPQEIYHQPAS 229
Cdd:TIGR00630 539 -LGNTLIVVEHD-EDTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDS 588

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

21-226

2.28e-06

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 2.28e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDF--GIVFQSYALFPNlTVAQNI 98
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFkiTIIPQDPVLFSG-SLRMNL 1380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 ----AFGLENQGLARDLikervDHWLGLVD-----LTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDAL 169
Cdd:TIGR00957 1381 dpfsQYSDEEVWWALEL-----AHLKTFVSalpdkLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523  170 VRTHLRSEIRAlqQRLGITTIMVTHDQEealTMAD--RIVVMEGGRIVQVGTPQEIYHQ 226
Cdd:TIGR00957 1456 TDNLIQSTIRT--QFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNLLQQ 1509

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

6-218

2.65e-06

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 2.65e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   6 LDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLD--LPDSGEIWQGGRNISQLPPQQR---DFG 80
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  81 IVFQSYALFPN------LTVAQNIAFGLENQ-GLAR----DLIKERVDHWLGLVDLTAQSHKYpsQISGGQQQRVALARA 149
Cdd:PRK09580   82 MAFQYPVEIPGvsnqffLQTALNAVRSYRGQePLDRfdfqDLMEEKIALLKMPEDLLTRSVNV--GFSGGEKKRNDILQM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 150 LALSPGLLLLDEPLSAL--DAL------VRThLRSEIRALqqrlgittIMVTHDQE-EALTMADRIVVMEGGRIVQVG 218
Cdd:PRK09580  160 AVLEPELCILDESDSGLdiDALkivadgVNS-LRDGKRSF--------IIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

19-107

2.73e-06

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: 47.24 E-value: 2.73e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLL-----RAIAGLdlpDSGEIWQGGRnisQLPPQ-QRDFGIVFQSYALFPNL 92
Cdd:cd03232    21 QLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGV---ITGEILINGR---PLDKNfQRSTGYVEQQDVHSPNL 94

                          90
                  ....*....|....*
gi 2051267523  93 TVAQNIAFGLENQGL 107
Cdd:cd03232    95 TVREALRFSALLRGL 109

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

20-218

3.04e-06

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: 46.93 E-value: 3.04e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIagldLPDSGEiwqgGRNISQLPPQQRDFGIVFQSYALFpnltvaqnIA 99
Cdd:cd03238    10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGK----ARLISFLPKFSRNKLIFIDQLQFL--------ID 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 100 FGLENQGLARDLikervdhwlglvdltaqshkypSQISGGQQQRVALAR--ALALSPGLLLLDEPLSALDALVRTHLRSE 177
Cdd:cd03238    74 VGLGYLTLGQKL----------------------STLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEV 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2051267523 178 IRALQQrLGITTIMVTHDqEEALTMADRIVVM------EGGRIVQVG 218
Cdd:cd03238   132 IKGLID-LGNTVILIEHN-LDVLSSADWIIDFgpgsgkSGGKVVFSG 176

PTZ00265

multidrug resistance protein (mdr1); Provisional

22-194

7.79e-06

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 7.79e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   22 KGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGE-IWQGGRNIS--QLPPQQRDFGIVFQSYALFPNlTVAQNI 98
Cdd:PTZ00265   402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiIINDSHNLKdiNLKWWRSKIGVVSQDPLLFSN-SIKNNI 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   99 AFGL---------ENQ-----------------------GLARDLIKERVDHWL-------------GLVDLT------- 126
Cdd:PTZ00265   481 KYSLyslkdlealSNYynedgndsqenknkrnscrakcaGDLNDMSNTTDSNELiemrknyqtikdsEVVDVSkkvlihd 560

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523  127 ---AQSHKY-------PSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRLGITTIMVTH 194
Cdd:PTZ00265   561 fvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

20-232

1.03e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 1.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQ---QRDFGIVFQ---SYALFPNLT 93
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeaiNHGFALVTEerrSTGIYAYLD 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  94 VA-----QNIAFGLENQGLARDLIKERVDHWLglvdLTAQSHKYPSQ------ISGGQQQRVALARALALSPGLLLLDEP 162
Cdd:PRK10982  343 IGfnsliSNIRNYKNKVGLLDNSRMKSDTQWV----IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEP 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267523 163 LSALDALVRTHLRSEIRALQQR-LGIttIMVTHDQEEALTMADRIVVMEGGR---IVQVG-TPQEIYHQPASRFV 232
Cdd:PRK10982  419 TRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLvagIVDTKtTTQNEILRLASLHL 491

PLN03140

ABC transporter G family member; Provisional

21-222

1.10e-05

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 1.10e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   21 LKGISLTIEPGEFICFLGPSGCGKTTLLRAIAG-LD--LPDSGEIWQGGRNISQLPPQQRDFGIVfQSYALFPNLTVAQN 97
Cdd:PLN03140   181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDpsLKVSGEITYNGYRLNEFVPRKTSAYIS-QNDVHVGVMTVKET 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   98 IAFGLENQGLAR--DLIKERV--------------------------------DHWLGLVDL-----TAQSHKYPSQISG 138
Cdd:PLN03140   260 LDFSARCQGVGTryDLLSELArrekdagifpeaevdlfmkatamegvksslitDYTLKILGLdickdTIVGDEMIRGISG 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  139 GQQQRVALARALALSPGLLLLDEPLSALDALVRTHLrseIRALQQRLGIT--TIMVTHDQ--EEALTMADRIVVMEGGRI 214
Cdd:PLN03140   340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI---VKCLQQIVHLTeaTVLMSLLQpaPETFDLFDDIILLSEGQI 416


                   ....*...
gi 2051267523  215 VQVGtPQE 222
Cdd:PLN03140   417 VYQG-PRD 423

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

21-238

1.59e-05

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: 45.67 E-value: 1.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  21 LKGISLTIEPGEFICFLGPSGCGKTTLlrAIAGLDLPD--SGEIWQGGRNISQLPPQ--QRDFGIVFQSYALFpnltvAQ 96
Cdd:cd03288    37 LKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRLSIILQDPILF-----SG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NIAFGLENQGLARDlikERVDHWLGLVDLTAQSHKYP-----------SQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:cd03288   110 SIRFNLDPECKCTD---DRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267523 166 LDALVRTHLRSEI-RALQQRlgiTTIMVTHDQEEALTmADRIVVMEGGRIVQVGTPQEIYHQPASRFvASFVGT 238
Cdd:cd03288   187 IDMATENILQKVVmTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLVRT 255

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

24-194

2.32e-05

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: 46.28 E-value: 2.32e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  24 ISLTIEPGEFICFLGPSGCGKTTLLRAIagldlpdsGEIW--QGGRniSQLPPQQRDFGIVFQSY---------ALFPNl 92
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWpvYGGR--LTKPAKGKLFYVPQRPYmtlgtlrdqIIYPD- 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  93 TVAQNIAFGLENQGLARDLIKERVDHWL---GLVDLTAQshkYPSQISGGQQQRVALARALALSPGLLLLDEPLSAldal 169
Cdd:TIGR00954 540 SSEDMKRRGLSDKDLEQILDNVQLTHILereGGWSAVQD---WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA---- 612

                         170       180
                  ....*....|....*....|....*
gi 2051267523 170 VRTHLRSEIRALQQRLGITTIMVTH 194
Cdd:TIGR00954 613 VSVDVEGYMYRLCREFGITLFSVSH 637

PLN03140

ABC transporter G family member; Provisional

19-168

5.65e-05

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 5.65e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGldlPDSGEIWQGGRNISQLPPQQRDF----GIVFQSYALFPNLTV 94
Cdd:PLN03140   894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTV 970

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   95 AQNIAFGLENQgLARDLIKER----VDHWLGLVDLTAQSHK---YP--SQISGGQQQRVALARALALSPGLLLLDEPLSA 165
Cdd:PLN03140   971 RESLIYSAFLR-LPKEVSKEEkmmfVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049


                   ...
gi 2051267523  166 LDA 168
Cdd:PLN03140  1050 LDA 1052

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

27-211

1.96e-04

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: 43.23 E-value: 1.96e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  27 TIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIwqggrnisQLPPQQRD----F-GIVFQSYalFPNLtVAQNIAFG 101
Cdd:COG1245    95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEvlkrFrGTELQDY--FKKL-ANGEIKVA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 102 LENQ----------GLARDLIK---ER--VDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSAL 166
Cdd:COG1245   164 HKPQyvdlipkvfkGTVRELLEkvdERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051267523 167 DalVRTHLRSE--IRALQQRlGITTIMVTHDqeeaLT----MADRIVVMEG 211
Cdd:COG1245   244 D--IYQRLNVArlIRELAEE-GKYVLVVEHD----LAildyLADYVHILYG 287

UvrA

COG0178

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

178-229

2.03e-04

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

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 2.03e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 178 IRALQQ-R-LGITTIMVTHDqEEALTMADRIVVM------EGGRIVQVGTPQEIYHQPAS 229
Cdd:COG0178   527 IETLKRlRdLGNTVIVVEHD-EDTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNPDS 585

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

29-211

5.68e-04

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: 41.20 E-value: 5.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  29 EPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIwqggrnisQLPPQQRDF-----GIVFQSY---ALFPNLTVAQNIAF 100
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEIldefrGSELQNYftkLLEGDVKVIVKPQY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 101 --GLENQ--GLARDLIK-----ERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALDALVR 171
Cdd:cd03236    96 vdLIPKAvkGKVGELLKkkderGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2051267523 172 THLRSEIRALQQRlGITTIMVTHDQEEALTMADRIVVMEG 211
Cdd:cd03236   176 LNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYG 214

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

20-167

6.24e-04

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 6.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  20 ALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNisqlppqqrdfGIVFQSYALFPNLTVAQNIA 99
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIE 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267523 100 FGLENQGLARDLIKERVDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPLSALD 167
Cdd:PRK13545  108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175

AAA

cd00009

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...

34-52

6.57e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.

Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.82 E-value: 6.57e-04

                          10
                  ....*....|....*....
gi 2051267523  34 ICFLGPSGCGKTTLLRAIA 52
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIA 40

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

27-211

7.22e-04

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 7.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  27 TIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEiwqggrniSQLPPQ-----QRDFGIVFQSYalFPNL-----TVAQ 96
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--------YEEEPSwdevlKRFRGTELQNY--FKKLyngeiKVVH 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  97 NI--------AFglenQGLARDLIK---ER--VDHWLGLVDLTAQSHKYPSQISGGQQQRVALARALALSPGLLLLDEPL 163
Cdd:PRK13409  165 KPqyvdlipkVF----KGKVRELLKkvdERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051267523 164 SALDALVRTHLRSEIRALQQrlGITTIMVTHDqeeaLT----MADRIVVMEG 211
Cdd:PRK13409  241 SYLDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIAYG 286

uvrA

PRK00349

excinuclease ABC subunit UvrA;

160-229

9.03e-04

excinuclease ABC subunit UvrA;

Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 9.03e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 160 DEPLSAL-----DALVRT--HLRSeiralqqrLGITTIMVTHDqEEALTMADRIVVM------EGGRIVQVGTPQEIYHQ 226
Cdd:PRK00349  516 DEPSIGLhqrdnDRLIETlkHLRD--------LGNTLIVVEHD-EDTIRAADYIVDIgpgagvHGGEVVASGTPEEIMKN 586


                  ...
gi 2051267523 227 PAS 229
Cdd:PRK00349  587 PNS 589

RecA-like_NVL_r1-like

cd19518

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...

25-57

1.02e-03

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.

Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 39.31 E-value: 1.02e-03

                          10        20        30
                  ....*....|....*....|....*....|....
gi 2051267523  25 SLTIEPGEFICFLGPSGCGKTTLLRAIAG-LDLP 57
Cdd:cd19518    28 HLGVEPPRGVLLHGPPGCGKTMLANAIAGeLKVP 61

COG1223

Predicted ATPase, AAA+ superfamily [General function prediction only];

34-57

1.03e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];

Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 1.03e-03

                          10        20
                  ....*....|....*....|....*
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAG-LDLP 57
Cdd:COG1223    38 ILFYGPPGTGKTMLAEALAGeLKLP 62

PLN03073

ABC transporter F family; Provisional

34-214

1.51e-03

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAGLDLPDSGEIWQGGRNISQLPPQQRDFGIVFQSYAL------FPnltvaqniafGLENQGL 107
Cdd:PLN03073  538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLlymmrcFP----------GVPEQKL 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523 108 ARDLIKervdhwLGLVDLTAQSHKYpsQISGGQQQRVALARALALSPGLLLLDEPLSALDAlvrthlrSEIRALQQRLGI 187
Cdd:PLN03073  608 RAHLGS------FGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL-------DAVEALIQGLVL 672

                         170       180       190
                  ....*....|....*....|....*....|
gi 2051267523 188 ---TTIMVTHDQEEALTMADRIVVMEGGRI 214
Cdd:PLN03073  673 fqgGVLMVSHDEHLISGSVDELWVVSEGKV 702

SpoVK

COG0464

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...

34-57

1.93e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];

Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 39.89 E-value: 1.93e-03

                          10        20
                  ....*....|....*....|....*
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAG-LDLP 57
Cdd:COG0464   194 LLLYGPPGTGKTLLARALAGeLGLP 218

PRK10636

putative ABC transporter ATP-binding protein; Provisional

4-62

2.31e-03

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 2.31e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267523   4 PYLDIQHLNKQFGAFQALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEI 62
Cdd:PRK10636  311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

13-97

2.40e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 2.40e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523   13 KQFGAFQALKGISLTIEPGEFiCFLGPSGCGKTTLLRAIAGL---DLPDSGEIWQGGRNISQLPPQQR----DFGIVFQS 85
Cdd:TIGR00618    9 KNFGSYKGTHTIDFTALGPIF-LICGKTGAGKTTLLDAITYAlygKLPRRSEVIRSLNSLYAAPSEAAfaelEFSLGTKI 87

                           90
                   ....*....|..
gi 2051267523   86 YALFPNLTVAQN 97
Cdd:TIGR00618   88 YRVHRTLRCTRS 99

PRK00635

excinuclease ABC subunit A; Provisional

120-222

2.65e-03

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 2.65e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267523  120 LGLVDLTAQshKYPSQISGGQQQRVALAR--ALALSPGLLLLDEPLSALDALVRTHLRSEIRALQQRlGITTIMVTHDqE 197
Cdd:PRK00635   463 LGLPYLTPE--RALATLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-E 538

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2051267523  198 EALTMADRIVVME------GGRIVQVGTPQE 222
Cdd:PRK00635   539 QMISLADRIIDIGpgagifGGEVLFNGSPRE 569

RecA-like_protease

cd19481

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...

34-57

2.79e-03

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.

Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 38.03 E-value: 2.79e-03

                          10        20
                  ....*....|....*....|....*
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAG-LDLP 57
Cdd:cd19481    29 ILLYGPPGTGKTLLAKALAGeLGLP 53

EutP

COG4917

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...

34-57

2.82e-03

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];

Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 2.82e-03

                          10        20
                  ....*....|....*....|....
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAGLDLP 57
Cdd:COG4917     4 IMLIGRSGAGKTTLTQALNGEELE 27

AAA

pfam00004

ATPase family associated with various cellular activities (AAA); AAA family proteins often ...

34-65

2.97e-03

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.

Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 37.57 E-value: 2.97e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAG--------LDLPDSGEIWQG 65
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKelgapfieISGSELVSKYVG 40

PduV-EutP

pfam10662

Ethanolamine utilization - propanediol utilization; Members of this family function in ...

34-56

3.49e-03

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.

Pssm-ID: 402341 [Multi-domain] Cd Length: 137 Bit Score: 37.26 E-value: 3.49e-03

                          10        20
                  ....*....|....*....|...
gi 2051267523  34 ICFLGPSGCGKTTLLRAIAGLDL 56
Cdd:pfam10662   4 IMLIGPTGCGKTTLCQALSGEEL 26

Rad17

pfam03215

Rad17 P-loop domain;

19-89

3.90e-03

Rad17 P-loop domain;

Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 38.02 E-value: 3.90e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267523  19 QALKGISLTIEPGEFICFLGPSGCGKTTLLRAIAGLDLPDSGEiWQGGRNISQLPPQQRDFGIVFQSYALF 89
Cdd:pfam03215  33 EWLDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGPKYRE-WSNPTSFRSPPNQVTDFRGDCIVNSRF 102

CMPK

cd02020

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...

38-91

4.42e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.

Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.08 E-value: 4.42e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267523  38 GPSGCGKTTLLRAIA---GLDLPDSG-----EIWQGGRNISQLPP-------QQRDF----GIVFQS----YALFPN 91
Cdd:cd02020     6 GPAGSGKSTVAKLLAkklGLPYLDTGgirteEVGKLASEVAAIPEvrkaldeRQRELakkpGIVLEGrdigTVVFPD 82

AAA_28

pfam13521

AAA domain;

33-52

4.72e-03

AAA domain;

Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 37.24 E-value: 4.72e-03

                          10        20
                  ....*....|....*....|
gi 2051267523  33 FICFLGPSGCGKTTLLRAIA 52
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALA 20

AAA_23

pfam13476

AAA domain;

18-51

5.26e-03

AAA domain;

Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 5.26e-03

                          10        20        30
                  ....*....|....*....|....*....|....
gi 2051267523  18 FQALKGISLTIEPGeFICFLGPSGCGKTTLLRAI 51
Cdd:pfam13476   6 FRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38

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