NCBI Conserved Domain Search

Conserved domains on [gi|16129442|ref|NP_416000|]

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putative D,D-dipeptide ABC transporter ATP-binding subunit DdpF [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438319)

ABC transporter ATP-binding protein similar to D,D-dipeptide transport ATP-binding protein DdpF, which is part of the ABC transporter complex DdpABCDF and is responsible for energy coupling to the transport system

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

AppF super family

cl34787

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

1-307

9.09e-144

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

The actual alignment was detected with superfamily member COG4608:

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 407.97 E-value: 9.09e-144

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG4608   3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 --RSGSQ-----RIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4608  83 tgLSGRElrplrRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGC-EVRQSLAIREDGRELRCWR 306
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQVACHL 322


                .
gi 16129442 307 A 307
Cdd:COG4608 323 A 323

Name

Accession

Description

Interval

E-value

AppF

COG4608

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

1-307

9.09e-144

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 407.97 E-value: 9.09e-144

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG4608   3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 --RSGSQ-----RIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4608  83 tgLSGRElrplrRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGC-EVRQSLAIREDGRELRCWR 306
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQVACHL 322


                .
gi 16129442 307 A 307
Cdd:COG4608 323 A 323

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

1-307

3.89e-113

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 330.00 E-value: 3.89e-113

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFPARKNwLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-- 78
Cdd:PRK11308   1 SQQPLLQAIDLKKHYPVKRG-LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   79 -----------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:PRK11308  80 lkadpeaqkllRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGCEVRQSLAIREDGRELRCWRA 307
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAV 319

ABC_NikE_OppD_transporters

cd03257

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

5-225

1.85e-107

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: 311.75 E-value: 1.85e-107

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------S 78
Cdd:cd03257   1 LLEVKNLSVSFPTGGGS-------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 QRI-------MQMVFQDPLSSLNPRLPVWRIITEPLWIAKR-SSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:cd03257  74 RRLrkirrkeIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKlSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

nickel_nikE

TIGR02769

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

4-248

5.79e-63

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: 200.03 E-value: 5.79e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     4 TLLTLRDVHINFpaRKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----- 78
Cdd:TIGR02769   1 SLLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyql 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    79 --------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:TIGR02769  79 drkqrrafRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238

                         250
                  ....*....|....*....
gi 16129442   231 LTApAHPYTRLLLDS-LPA 248
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAvLPE 256

ABC_tran

pfam00005

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

32-171

1.07e-37

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: 131.23 E-value: 1.07e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ----------YIRSGSQRIMQMVFQDPlsSLNPRLPVWR 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdDERKSLRKEIGYVFQDP--QLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442   102 IITEPLWI---AKRSSEQQRRALAEELAvQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:pfam00005  79 NLRLGLLLkglSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

31-207

2.96e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 2.96e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQdplSSLNPRLP--VWRIITEPLW 108
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR---SEVPDSLPltVRDLVAMGRW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  109 ----IAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:NF040873  84 arrgLWRRLTRDDRAAVDDALE-RVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161

                        170       180
                 ....*....|....*....|...
gi 16129442  185 LVTLQENhGLTYVLISHNVSVIR 207
Cdd:NF040873 162 LAEEHAR-GATVVVVTHDLELVR 183

GguA

NF040905

sugar ABC transporter ATP-binding protein;

24-223

1.07e-17

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 1.07e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmLQPsHGQY---------------IRSGSQR----IMQM 84
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP-HGSYegeilfdgevcrfkdIRDSEALgiviIHQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   85 VFQDPLSSlnprlpvwriITEPLWIakrSSEQQRRAL---------AEELAVQVGirpeyLDRLPHAFSG----GQRQRI 151
Cdd:NF040905  87 LALIPYLS----------IAENIFL---GNERAKRGVidwnetnrrARELLAKVG-----LDESPDTLVTdigvGKQQLV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219

AAA

smart00382

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

41-219

2.64e-16

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: 74.33 E-value: 2.64e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     41 RGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQDplsslnprlpvwriiteplwiakrsseqqrra 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    121 laeelavqvgIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT-----LQENHGLT 195
Cdd:smart00382  49 ----------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSEKNLT 118

                          170       180
                   ....*....|....*....|....*....
gi 16129442    196 YVLISHNVSV-----IRHMSDRVAVMYLG 219
Cdd:smart00382 119 VILTTNDEKDlgpalLRRRFDRRIVLLLI 147

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

31-174

2.46e-11

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 2.46e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGS----QRI--MQMVFqdplsSLNPRLP 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgQPVDAGDiatrRRVgyMSQAF-----SLYGELT 355

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   99 VwRiitEPLWI-AK--RSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:NF033858 356 V-R---QNLELhARlfHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

40850658_otr

NF000106

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

29-232

3.45e-09

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 3.45e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGcgkstlAQLLMGMLqPSHGQYIRSGSQRIMQMVFQDPLSSLNPRLPVWRIIT---- 104
Cdd:NF000106  26 VKAVDGVDLDVREGTVLGVLGP*G------AA**RGAL-PAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*grr 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 ------EPLWIAKRS---SEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:NF000106  99 esfsgrENLYMIGR*ldlSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  176 SVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:NF000106 178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233

GguA

NF040905

sugar ABC transporter ATP-binding protein;

9-229

2.95e-08

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 2.95e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    9 RDVHINFPAR-----------KNWlgkTTEH-VHA----INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMlqpSHGQ 72
Cdd:NF040905 240 RDLEDRYPERtpkigevvfevKNW---TVYHpLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   73 YIrSGSqrimqmVFQD----PLSS--------------------LNPRLPVWRIITEPLW--IAKRS--SEQQRRALAEE 124
Cdd:NF040905 314 NI-SGT------VFKDgkevDVSTvsdaidaglayvtedrkgygLNLIDDIKRNITLANLgkVSRRGviDENEEIKVAEE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  125 LAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDisVQA-----QILNLLVtlqeNHGLTYVLI 199
Cdd:NF040905 387 YRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyeiyTIINELA----AEGKGVIVI 460

                        250       260       270
                 ....*....|....*....|....*....|...
gi 16129442  200 SHNVSVIRHMSDRVAVMYLGQIV-EL--GDAQQ 229
Cdd:NF040905 461 SSELPELLGMCDRIYVMNEGRITgELprEEASQ 493

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

23-174

1.01e-03

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 1.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   23 GKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG---------------MLQPSHGqyiRSGSQRIMQMvfq 87
Cdd:NF033858  12 GKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevlggdMADARHR---RAVCPRIAYM--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   88 dP--L-SSLNPRLPVwriiTEPLWIAKR---SSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:NF033858  82 -PqgLgKNLYPTLSV----FENLDFFGRlfgQDAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDP 155

                        170
                 ....*....|...
gi 16129442  162 DVIVLDEPTSALD 174
Cdd:NF033858 156 DLLILDEPTTGVD 168

Name

Accession

Description

Interval

E-value

AppF

COG4608

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

1-307

9.09e-144

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 407.97 E-value: 9.09e-144

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG4608   3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 --RSGSQ-----RIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4608  83 tgLSGRElrplrRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGC-EVRQSLAIREDGRELRCWR 306
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQVACHL 322


                .
gi 16129442 307 A 307
Cdd:COG4608 323 A 323

DppD

COG0444

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

5-307

3.15e-140

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: 398.66 E-value: 3.15e-140

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQYIR 75
Cdd:COG0444   1 LLEVRNLKVYFPTRRGV-------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitsgeilfDGEDLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  76 SGSQRIM--------QMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRP--EYLDRLPHAFSG 145
Cdd:COG0444  74 KLSEKELrkirgreiQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 226 DAQQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALrKTDLPGNRTLPQGCFFYERCPLATHGC-EVRQSLAIREDGRELRC 304
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDGRRLIPI-PGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGPGHRVAC 312


                ...
gi 16129442 305 WRA 307
Cdd:COG0444 313 HLY 315

GsiA

COG1123

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

1-250

7.27e-123

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: 361.53 E-value: 7.27e-123

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARKnwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRG------KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdl 329

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 --RSGSQ-----RIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG1123 330 tkLSRRSlrelrRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQ 409

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489

                       250       260
                ....*....|....*....|...
gi 16129442 228 QQVLTAPAHPYTRLLLDSLPAID 250
Cdd:COG1123 490 EEVFANPQHPYTRALLAAVPSLD 512

YejF

COG4172

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

3-250

1.18e-122

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: 361.69 E-value: 1.18e-122

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmLQPSHGQyIRSGSQRI- 81
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGE-IRFDGQDLd 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  82 -------------MQMVFQDPLSSLNPRLPVWRIITEPLWI-AKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4172 351 glsrralrplrrrMQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQ 430

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510

                       250       260
                ....*....|....*....|...
gi 16129442 228 QQVLTAPAHPYTRLLLDSLPAID 250
Cdd:COG4172 511 EQVFDAPQHPYTRALLAAAPLLE 533

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

1-307

3.89e-113

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 330.00 E-value: 3.89e-113

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFPARKNwLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-- 78
Cdd:PRK11308   1 SQQPLLQAIDLKKHYPVKRG-LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   79 -----------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:PRK11308  80 lkadpeaqkllRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGCEVRQSLAIREDGRELRCWRA 307
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAV 319

ABC_NikE_OppD_transporters

cd03257

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

5-225

1.85e-107

Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 311.75 E-value: 1.85e-107

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------S 78
Cdd:cd03257   1 LLEVKNLSVSFPTGGGS-------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 QRI-------MQMVFQDPLSSLNPRLPVWRIITEPLWIAKR-SSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:cd03257  74 RRLrkirrkeIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKlSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

DppF

COG1124

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

5-252

2.07e-104

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: 304.80 E-value: 2.07e-104

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ---------YIR 75
Cdd:COG1124   1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvtRRR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  76 SGSQ-RIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRralAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG1124  74 RKAFrRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230

                       250
                ....*....|....*...
gi 16129442 235 AHPYTRLLLDSLPAIDKP 252
Cdd:COG1124 231 KHPYTRELLAASLAFERA 248

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

5-287

1.41e-96

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 288.14 E-value: 1.41e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRD--VHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRS 76
Cdd:PRK15079   8 LLEVADlkVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGevawlgKDLLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   77 GSQRIM-------QMVFQDPLSSLNPRLPVWRIITEPLWIAK-RSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQR 148
Cdd:PRK15079  88 MKDDEWravrsdiQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQ 228
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442  229 QVLTAPAHPYTRLLLDSLPAIDKPLE--EEWALRKTDLPGNRTLPQGCFFYERCPLATHGC 287
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLErnKTIQLLEGELPSPINPPSGCVFRTRCPIAGPEC 308

YejF

COG4172

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

1-252

2.07e-86

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: 268.48 E-value: 2.07e-86

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFparknwlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS----------H 70
Cdd:COG4172   2 MSMPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpsgsilfD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  71 GQYIRSGSQRIMQ--------MVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIR-PEY-LDRLP 140
Cdd:COG4172  75 GQDLLGLSERELRrirgnriaMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERrLDAYP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234

                       250       260       270
                ....*....|....*....|....*....|..
gi 16129442 221 IVELGDAQQVLTAPAHPYTRLLLDSLPAIDKP 252
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPR 266

SapF

COG4167

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

4-245

2.43e-86

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 259.77 E-value: 2.43e-86

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   4 TLLTLRDVHINFPARKNWLGKttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------ 77
Cdd:COG4167   3 ALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleyg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  78 -----SQRImQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIA 152
Cdd:COG4167  81 dykyrCKHI-RMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239

                       250
                ....*....|...
gi 16129442 233 APAHPYTRLLLDS 245
Cdd:COG4167 240 NPQHEVTKRLIES 252

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

1-307

3.31e-74

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 231.15 E-value: 3.31e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFparknwlgKTTE-HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQpSHGqyIRSGSQ 79
Cdd:PRK09473   8 QADALLDVKDLRVTF--------STPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANG--RIGGSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   80 RI--------------------MQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQrrALAEEL----AVQVgirPEY 135
Cdd:PRK09473  77 TFngreilnlpekelnklraeqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAE--AFEESVrmldAVKM---PEA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  136 LDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDR 212
Cdd:PRK09473 152 RKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDK 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  213 VAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDSLPAIDkplEEEWALrkTDLPGNR----TLPQGCFFYERCPLATHGCE 288
Cdd:PRK09473 232 VLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLD---AEGESL--LTIPGNPpnllRLPKGCPFQPRCPHAMEICS 306

                        330
                 ....*....|....*....
gi 16129442  289 VRQSLAIREDGRELRCWRA 307
Cdd:PRK09473 307 SAPPLEEFGPGRLRACFKP 325

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

4-243

5.27e-73

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 233.83 E-value: 5.27e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    4 TLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQYIRSGS----- 78
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQplhnl 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   79 --------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRS-SEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQ 149
Cdd:PRK15134 353 nrrqllpvRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQ 432

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512

                        250
                 ....*....|....
gi 16129442  230 VLTAPAHPYTRLLL 243
Cdd:PRK15134 513 VFAAPQQEYTRQLL 526

GsiA

COG1123

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

3-265

2.28e-70

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: 226.71 E-value: 2.28e-70

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQY 73
Cdd:COG1123   2 TPLLEVRDLSVRYPGGD---------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisgevllDGRD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  74 IRSGSQRIMQ----MVFQDPLSSLNPrLPVWRIITEPLWIAKRSSEQqRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQ 149
Cdd:COG1123  73 LLELSEALRGrrigMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAE-ARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16129442 230 VLTAPAhpytrlLLDSLPAIDKPLEEEWALRKTDLP 265
Cdd:COG1123 230 ILAAPQ------ALAAVPRLGAARGRAAPAAAAAEP 259

PRK10261

glutathione transporter ATP-binding protein; Provisional

2-267

2.44e-68

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 223.96 E-value: 2.44e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    2 SDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRI 81
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRI 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   82 --------------MQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:PRK10261 389 dtlspgklqalrrdIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 16129442  228 QQVLTAPAHPYTRLLLDSLPAIDKPLEE-EWALRKTDLPGN 267
Cdd:PRK10261 549 RAVFENPQHPYTRKLMAAVPVADPSRQRpQRVLLSDDLPSN 589

nickel_nikE

TIGR02769

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

4-248

5.79e-63

Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 200.03 E-value: 5.79e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     4 TLLTLRDVHINFpaRKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----- 78
Cdd:TIGR02769   1 SLLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyql 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    79 --------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:TIGR02769  79 drkqrrafRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238

                         250
                  ....*....|....*....
gi 16129442   231 LTApAHPYTRLLLDS-LPA 248
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAvLPE 256

PRK15112

peptide ABC transporter ATP-binding protein SapF;

3-245

7.16e-63

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 200.02 E-value: 7.16e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    3 DTLLTLRDVHINFPARKNWLGKttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----- 77
Cdd:PRK15112   2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 ------SQRImQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRI 151
Cdd:PRK15112  80 gdysyrSQRI-RMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238

                        250
                 ....*....|....
gi 16129442  232 TAPAHPYTRLLLDS 245
Cdd:PRK15112 239 ASPLHELTKRLIAG 252

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

32-248

5.78e-62

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 197.60 E-value: 5.78e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMVFQDPLSSLNPRLP 98
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafRRDIQMVFQDSISAVNPRKT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442  179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE---LGDAQQVltapAHPYTRLLLDS-LPA 248
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLTF----SSPAGRVLQNAvLPA 257

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

31-304

1.45e-60

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 195.73 E-value: 1.45e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ-PS---------HGQYIRSGSQRIMQ--------MVFQDPLSS 92
Cdd:PRK11022  22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmaeklefNGQDLQRISEKERRnlvgaevaMIFQDPMTS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   93 LNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGI-RPEY-LDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  171 SALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDSLPaid 250
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP--- 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442  251 kpleeEWALRKTDL-------PGNRTLPQGCFFYERCPLATHGCEVRQSLAIREDGRELRC 304
Cdd:PRK11022 259 -----EFAQDKARLaslpgvvPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKC 314

SapD

COG4170

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

29-304

4.62e-59

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 192.04 E-value: 4.62e-59

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS----------HGQYI--RSGSQR--IM----QMVFQDPL 90
Cdd:COG4170  20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLlkLSPRERrkIIgreiAMIFQEPS 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  91 SSLNPRLPVWRIITE--PLWIAKRS---SEQQRRALAEELAVQVGIR--PEYLDRLPHAFSGGQRQRIAIARALSSQPDV 163
Cdd:COG4170 100 SCLDPSAKIGDQLIEaiPSWTFKGKwwqRFKWRKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 164 IVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLL 243
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 244 DSLPAIDKPLEEEWALrkTDLPGN----RTLPQGCFFYERCPLATHGCeVRQSLAIREDGRELRC 304
Cdd:COG4170 260 RSMPDFRQPLPHKSRL--NTLPGSipplQHLPIGCRLGPRCPYAQKKC-VETPRLRKIKGHEFAC 321

AbcC

COG1135

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

6-266

1.89e-56

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.67 E-value: 1.89e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-- 83
Cdd:COG1135   2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS-VLVDGVDLTAls 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 ------------MVFQDP--LSSLNprlpVWRIITEPLWIAKRSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQ 149
Cdd:COG1135  74 erelraarrkigMIFQHFnlLSSRT----VAENVALPLEIAGVPKAE-IRKRVAELLELVGLS-DKADAYPSQLSGGQKQ 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 16129442 230 VLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPG 266
Cdd:COG1135 228 VFANPQSELTRRFLPTVLNDELPEELLARLREAAGGG 264

MlaF

COG1127

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

1-240

1.05e-54

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: 177.86 E-value: 1.05e-54

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARknwlgktteHVHaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIR----- 75
Cdd:COG1127   1 MSEPMIEVRNLTKSFGDR---------VVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILvdgqd 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  76 ----SGSQRI-----MQMVFQDP--LSSLNprlpVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHAFS 144
Cdd:COG1127  69 itglSEKELYelrrrIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELS 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 145 GGQRQRIAIARALSSQPDVIVLDEPTSALD-ISVqAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222

                       250
                ....*....|....*..
gi 16129442 224 LGDAQQVLTAPaHPYTR 240
Cdd:COG1127 223 EGTPEELLASD-DPWVR 238

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

1-256

3.76e-53

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 181.83 E-value: 3.76e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFpaRKnwlGKTTEHVhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPS----------- 69
Cdd:PRK15134   1 MTQPLLAIENLSVAF--RQ---QQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypsgdir 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   70 -HGQYIRSGSQRI--------MQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIR--PEYLDR 138
Cdd:PRK15134  73 fHGESLLHASEQTlrgvrgnkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 16129442  219 GQIVELGDAQQVLTAPAHPYTRLLLDSLPAIDK-PLEEE 256
Cdd:PRK15134 233 GRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPvPLPEP 271

ABC_MetN_methionine_transporter

cd03258

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

5-234

5.05e-53

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: 173.54 E-value: 5.05e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS------ 78
Cdd:cd03258   1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltlls 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 -------QRIMQMVFQ--DPLSSLNprlpVWRIITEPLWIAKrSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQ 149
Cdd:cd03258  74 gkelrkaRRRIGMIFQhfNLLSSRT----VFENVALPLEIAG-VPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQ 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227


                ....*
gi 16129442 230 VLTAP 234
Cdd:cd03258 228 VFANP 232

LolD

COG1136

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

3-223

7.07e-53

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.92 E-value: 7.07e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIM 82
Cdd:COG1136   2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG-QDIS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  83 QM---------------VFQDPlsSLNPRLPVWRIITEPLWIAKRSSEQqRRALAEELAVQVGIrPEYLDRLPHAFSGGQ 147
Cdd:COG1136  74 SLserelarlrrrhigfVFQFF--NLLPELTALENVALPLLLAGVSRKE-RRERARELLERVGL-GDRLDHRPSQLSGGQ 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIVS 224

PotA

COG3842

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

1-238

7.56e-53

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.44 E-value: 7.56e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG3842   1 MAMPALELENVSKRY-------GDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRD 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  81 I---------MQMVFQDPlsSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAvQVGIrPEYLDRLPHAFSGGQRQRI 151
Cdd:COG3842  69 VtglppekrnVGMVFQDY--ALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLE-LVGL-EGLADRYPHQLSGGQQQRV 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN----VSvirhMSDRVAVMYLGQIVELGDA 227
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTP 220

                       250
                ....*....|.
gi 16129442 228 QQVLTAPAHPY 238
Cdd:COG3842 221 EEIYERPATRF 231

ABC_Carb_Solutes_like

cd03259

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

22-225

9.57e-53

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: 171.93 E-value: 9.57e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ---------MVFQDPlsS 92
Cdd:cd03259   6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-ILIDGRDVTGvpperrnigMVFQDY--A 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  93 LNPRLPVWRIITEPLWIAKRSSEQQRRAlAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03259  83 LFPHLTVAENIAFGLKLRGVPKAEIRAR-VRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129442 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

PRK10261

glutathione transporter ATP-binding protein; Provisional

29-265

4.36e-52

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 180.82 E-value: 4.36e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRI------------------MQM 84
Cdd:PRK10261  29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmLLRRRSRQVielseqsaaqmrhvrgadMAM 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   85 VFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIrPE---YLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:PRK10261 109 IFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEaqtILSRYPHQLSGGMRQRVMIAMALSCRP 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  162 DVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRL 241
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267

                        250       260
                 ....*....|....*....|....
gi 16129442  242 LLDSLPAIDkpleeewALRKTDLP 265
Cdd:PRK10261 268 LLAAVPQLG-------AMKGLDYP 284

GlnQ

COG1126

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

5-246

1.08e-51

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 170.17 E-value: 1.08e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFparknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGS 78
Cdd:COG1126   1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtitvDGEDLTDSK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 QRIMQ------MVFQdplsSLN--PRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQR 150
Cdd:COG1126  70 KDINKlrrkvgMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQR 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223

                       250
                ....*....|....*.
gi 16129442 231 LTAPAHPYTRLLLDSL 246
Cdd:COG1126 224 FENPQHERTRAFLSKV 239

EcfA2

COG1122

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

6-234

2.77e-51

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: 168.66 E-value: 2.77e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFParknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY-----------I 74
Cdd:COG1122   1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkknL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 RSGSQRImQMVFQDP--------------LSSLNPRLPvwriiteplwiakrssEQQRRALAEELAVQVGIRpEYLDRLP 140
Cdd:COG1122  71 RELRRKV-GLVFQNPddqlfaptveedvaFGPENLGLP----------------REEIRERVEEALELVGLE-HLADRPP 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGR 211

                       250
                ....*....|....
gi 16129442 221 IVELGDAQQVLTAP 234
Cdd:COG1122 212 IVADGTPREVFSDY 225

TauB

COG1116

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

1-216

3.20e-51

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.50 E-value: 3.20e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYI 74
Cdd:COG1116   3 AAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTsgevlvDGKPV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 RSGSQRIMqMVFQDPlsSLNPRLPVWRIITEPLWIAKRSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG1116  76 TGPGPDRG-VVFQEP--ALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVS-VIRhMSDRVAVM 216
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVL 212

ABC_Org_Solvent_Resistant

cd03261

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

8-240

9.29e-50

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: 164.98 E-value: 9.29e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   8 LRDVHINFPARknwlgktteHVHaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQ-- 79
Cdd:cd03261   3 LRGLTKSFGGR---------TVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsgevliDGEDISGLSEae 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  80 -----RIMQMVFQDP--LSSLNprlpVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIA 152
Cdd:cd03261  72 lyrlrRRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVA 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226


                ....*...
gi 16129442 233 APaHPYTR 240
Cdd:cd03261 227 SD-DPLVR 233

ABC_NrtD_SsuB_transporters

cd03293

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

6-216

2.02e-49

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: 163.80 E-value: 2.02e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQ-- 83
Cdd:cd03293   1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTGpg 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 ----MVFQDPlsSLNPRLPVWRIITEPLWIaKRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSS 159
Cdd:cd03293  73 pdrgYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

1-248

4.39e-49

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 163.94 E-value: 4.39e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDvhinfparknwLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-------- 72
Cdd:PRK11701   2 MDQPLLSVRG-----------LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdg 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   73 -----YIRSGSQRIMQM------VFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPH 141
Cdd:PRK11701  71 qlrdlYALSEAERRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230

                        250       260
                 ....*....|....*....|....*...
gi 16129442  222 VELGDAQQVLTAPAHPYTRLLLDS-LPA 248
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYTQLLVSSvLQV 258

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

7-270

1.27e-48

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.36 E-value: 1.27e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    7 TLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------- 77
Cdd:PRK11153   3 ELKNISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsek 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 ----SQRIMQMVFQ--DPLSSLNprlpVWRIITEPLWIAKRSSEQQRRALAEELAVqVGIRpEYLDRLPHAFSGGQRQRI 151
Cdd:PRK11153  76 elrkARRQIGMIFQhfNLLSSRT----VFDNVALPLELAGTPKAEIKARVTELLEL-VGLS-DKADRYPAQLSGGQKQRV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 16129442  232 TAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTL 270
Cdd:PRK11153 230 SHPKHPLTREFIQSTLHLDLPEDYLARLQAEPTTGSGPL 268

ABC_MJ0796_LolCDE_FtsE

cd03255

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

18-221

4.02e-48

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: 160.35 E-value: 4.02e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  18 RKNWlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM------------- 84
Cdd:cd03255   7 SKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDISKLsekelaafrrrhi 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 --VFQDPlsSLNPRLPVWRIITEPLWIAKRSSEQqRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPD 162
Cdd:cd03255  85 gfVFQSF--NLLPDLTALENVELPLLLAGVPKKE-RRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442 163 VIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218

CcmA

COG1131

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

22-231

6.72e-47

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 6.72e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY------IRSGSQRIMQM---VFQDPlsS 92
Cdd:COG1131   6 LTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRRigyVPQEP--A 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  93 LNPRLPVWRIITeplWIAK--RSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:COG1131  84 LYPDLTVRENLR---FFARlyGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442 171 SALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:COG1131 160 SGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219

ABC_PotA_N

cd03300

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

24-235

2.31e-46

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: 156.24 E-value: 2.31e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMVFQDplSSLNP 95
Cdd:cd03300   8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphKRPVNTVFQN--YALFP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  96 RLPVWRIITEPLWIAKRSSEQQRRALAEELA-VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03300  86 HLTVFENIAFGLRLKKLPKAEIKERVAEALDlVQLE---GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442 175 ISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA 235
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223

ABC_cobalt_CbiO_domain1

cd03225

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

31-220

8.15e-46

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: 154.16 E-value: 8.15e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----SQRIMQ------MVFQDPLSSL-NPRlpv 99
Cdd:cd03225  16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltKLSLKElrrkvgLVFQNPDDQFfGPT--- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 wriITEPLWIAKRS---SEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03225  93 ---VEEEVAFGLENlglPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16129442 177 VQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd03225 169 GRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211

PRK15093

peptide ABC transporter ATP-binding protein SapD;

5-287

6.36e-45

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 155.35 E-value: 6.36e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG-------------------M 65
Cdd:PRK15093   3 LLDIRNLTIEFKTSDGW-------VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   66 LQPSHGQYiRSGSQRIMQMVFQDPLSSLNPRLPVWRIITE--PLWIAK-----RSSEQQRRALaeELAVQVGIRPEY--L 136
Cdd:PRK15093  76 LRLSPRER-RKLVGHNVSMIFQEPQSCLDPSERVGRQLMQniPGWTYKgrwwqRFGWRKRRAI--ELLHRVGIKDHKdaM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  137 DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  217 YLGQIVELGDAQQVLTAPAHPYTRLLLDSLPAIDKPLEEEwaLRKTDLPGN----RTLPQGCFFYERCPLATHGC 287
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHK--SRLNTLPGAipllEHLPIGCRLGPRCPYAQREC 305

ABC_Class3

cd03229

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

24-220

6.70e-45

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: 150.42 E-value: 6.70e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------------YIRSGSQRIMQMVFQDPls 91
Cdd:cd03229   8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdleDELPPLRRRIGMVFQDF-- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  92 SLNPRLPVWRIITEPLwiakrsseqqrralaeelavqvgirpeyldrlphafSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:cd03229  86 ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129442 172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178

ABC_PstB_phosphate_transporter

cd03260

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

30-230

9.77e-45

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: 151.95 E-value: 9.77e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-----QPSHGQYIRSGS------------QRIMQMVFQDPlss 92
Cdd:cd03260  14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelRRRVGMVFQKP--- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  93 lNP-RLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRL-PHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:cd03260  91 -NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPT 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 171 SALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:cd03260 170 SALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

ABC_Pro_Gly_Betaine

cd03294

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

17-240

1.96e-44

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: 152.41 E-value: 1.96e-44

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  17 ARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YI-------------RSGSQRIM 82
Cdd:cd03294  25 KSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvLIdgqdiaamsrkelRELRRKKI 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  83 QMVFQDplSSLNPRLPVWRIITEPLWIAKRSsEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPD 162
Cdd:cd03294 105 SMVFQS--FALLPHRTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPD 180

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 163 VIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTR 240
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258

ZnuC

COG1121

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

1-235

1.13e-43

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 1.13e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFparknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYI 74
Cdd:COG1121   2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrlfgKPP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 RSGSQRI---MQMvfqdplSSLNPRLP--VWRIITEPLW----IAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSG 145
Cdd:COG1121  71 RRARRRIgyvPQR------AEVDWDFPitVRDVVLMGRYgrrgLFRRPSRADREAVDEALE-RVGLE-DLADRPIGELSG 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMyLGQIVELG 225
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHG 220

                       250
                ....*....|
gi 16129442 226 DAQQVLTAPA 235
Cdd:COG1121 221 PPEEVLTPEN 230

ECF_ATPase_2

TIGR04521

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

24-232

1.67e-43

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: 149.91 E-value: 1.67e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ--------------MVFQDP 89
Cdd:TIGR04521  13 GTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT-VTIDGRDITAkkkkklkdlrkkvgLVFQFP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    90 LSSL-----------NPR-LPVwriiteplwiakrsSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:TIGR04521  92 EHQLfeetvykdiafGPKnLGL--------------SEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442   158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232

FepC

COG1120

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

5-233

2.19e-42

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: 146.34 E-value: 2.19e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   5 LLTLRDVHINFPARknwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM 84
Cdd:COG1120   1 MLEAENLSVGYGGR-----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE-VLLDGRDLASL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 -----------VFQDPLSSLN------------PRLPVWRiiteplwiakRSSEQQRRALAEELAvQVGIRpEYLDRLPH 141
Cdd:COG1120  69 srrelarriayVPQEPPAPFGltvrelvalgryPHLGLFG----------RPSAEDREAVEEALE-RTGLE-HLADRPVD 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216

                       250
                ....*....|..
gi 16129442 222 VELGDAQQVLTA 233
Cdd:COG1120 217 VAQGPPEEVLTP 228

CysA

COG1118

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

1-239

2.91e-42

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 148.76 E-value: 2.91e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSdtlLTLRDVHINFPARknwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-------- 72
Cdd:COG1118   1 MS---IEVRNISKRFGSF-----------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRivlngrdl 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  73 YIRSGSQ-RIMQMVFQDPLssLNPRLPVWRIITEPLWIAKRsSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRI 151
Cdd:COG1118  67 FTNLPPReRRVGFVFQHYA--LFPHMTVAENIAFGLRVRPP-SKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRV 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222


                ....*...
gi 16129442 232 TAPAHPYT 239
Cdd:COG1118 223 DRPATPFV 230

MalK

COG3839

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

1-236

3.11e-42

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 148.68 E-value: 3.11e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDtlLTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG3839   1 MAS--LELENVSKSY-------GG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-ILIGGRD 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  81 I---------MQMVFQDPlsSLNPRLPVWRIITEPLWIAKRSsEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRI 151
Cdd:COG3839  67 VtdlppkdrnIAMVFQSY--ALYPHMTVYENIAFPLKLRKVP-KAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRV 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN----VSvirhMSDRVAVMYLGQIVELGDA 227
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTP 218


                ....*....
gi 16129442 228 QQVLTAPAH 236
Cdd:COG3839 219 EELYDRPAN 227

PstB

COG1117

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

2-240

3.49e-42

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.95 E-value: 3.49e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   2 SDTLLTLRDVHInfparknWLGKTtehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPS---------H 70
Cdd:COG1117   8 LEPKIEVRNLNV-------YYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvegeillD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  71 GQYIRSGS-------QRIMqMVFQDPlsslNPrLP--VWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRL-- 139
Cdd:COG1117  77 GEDIYDPDvdvvelrRRVG-MVFQKP----NP-FPksIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLkk 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 140 -PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD-ISVqAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:COG1117 151 sALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFY 227

                       250       260
                ....*....|....*....|...
gi 16129442 218 LGQIVELGDAQQVLTAPAHPYTR 240
Cdd:COG1117 228 LGELVEFGPTEQIFTNPKDKRTE 250

ABC_HisP_GlnQ

cd03262

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

30-221

5.25e-42

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: 144.21 E-value: 5.25e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQRIMQ------MVFQDplSSLNPRL 97
Cdd:cd03262  14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtiiiDGLKLTDDKKNINElrqkvgMVFQQ--FNLFPHL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  98 PVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:cd03262  92 TVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16129442 178 QAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03262 171 VGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213

ABC_OpuCA_Osmoprotection

cd03295

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

24-245

2.13e-41

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: 143.60 E-value: 2.13e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  24 KTTEHVH-AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQmvfQDPLS----------- 91
Cdd:cd03295   8 KRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGE-IFIDGEDIRE---QDPVElrrkigyviqq 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  92 -SLNPRLPVWRIITEPLWIAKRSsEQQRRALAEELAVQVGIRP-EYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:cd03295  84 iGLFPHMTVEENIALVPKLLKWP-KEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442 170 TSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDS 245
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238

ThiQ

COG3840

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

35-243

2.47e-41

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 2.47e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNPRLPVWRIITEP 106
Cdd:COG3840  18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppAERPVSMLFQE--NNLFPHLTVAQNIGLG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 107 LWIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:COG3840  96 LRPGLKLTAEQRAQVEQALE-RVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 187 TLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLL 243
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230

ABCC_MRP_Like

cd03228

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

6-220

6.06e-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: 140.21 E-value: 6.06e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM- 84
Cdd:cd03228   1 IEFKNVSFSYPGRPKP---------VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-ILIDGVDLRDLd 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 ----------VFQDPlsslnprlpvwriiteplWIAKRSseqqrraLAEELavqvgirpeyldrlphaFSGGQRQRIAIA 154
Cdd:cd03228  71 leslrkniayVPQDP------------------FLFSGT-------IRENI-----------------LSGGQRQRIAIA 108

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQ 220
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171

SunT

COG2274

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

6-241

1.16e-40

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: 149.98 E-value: 1.16e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-- 83
Cdd:COG2274 474 IELENVSFRYPGDSPP---------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGIDLRQid 543

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 ---------MVFQDPL---SSL--NprlpvwriITepLWIAKRSSEQQRRALAeelavQVGIRpEYLDRLPH-------- 141
Cdd:COG2274 544 paslrrqigVVLQDVFlfsGTIreN--------IT--LGDPDATDEEIIEAAR-----LAGLH-DFIEALPMgydtvvge 607

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 142 ---AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHmSDRVAVMYL 218
Cdd:COG2274 608 ggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTIRL-ADRIIVLDK 684

                       250       260
                ....*....|....*....|...
gi 16129442 219 GQIVELGDAQQVLTAPAHpYTRL 241
Cdd:COG2274 685 GRIVEDGTHEELLARKGL-YAEL 706

FetA

COG4619

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

6-221

1.29e-40

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.34 E-value: 1.29e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehvhaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIrsgsqrimqmv 85
Cdd:COG4619   1 LELEGLSFRVGGKPIL-----------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY----------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  86 FQD-PLSSLNPrlPVWR-----IITEPLWIAKR-----------SSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQR 148
Cdd:COG4619  59 LDGkPLSAMPP--PEWRrqvayVPQEPALWGGTvrdnlpfpfqlRERKFDRERALELLERLGLPPDILDKPVERLSGGER 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442 149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209

PRK11264

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

32-244

1.51e-40

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.81 E-value: 1.51e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI-------------------MQMVFQDplSS 92
Cdd:PRK11264  19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT-IRVGDITIdtarslsqqkglirqlrqhVGFVFQN--FN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   93 LNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK11264  96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  173 LDISVQAQILNLLVTLQENHgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLD 244
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245

CydD

COG4988

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

6-231

4.84e-40

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

Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 146.83 E-value: 4.84e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqyirsgsqRIMqmV 85
Cdd:COG4988 337 IELEDVSFSYPGGRP----------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG--------SIL--I 396

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  86 FQDPLSSLNPRlPVWRIITeplWIAKR-------------------SSEQQRRALAeelavQVGIRpEYLDRLPH----- 141
Cdd:COG4988 397 NGVDLSDLDPA-SWRRQIA---WVPQNpylfagtirenlrlgrpdaSDEELEAALE-----AAGLD-EFVAALPDgldtp 466

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 142 ------AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAV 215
Cdd:COG4988 467 lgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQA-DRILV 543

                       250
                ....*....|....*.
gi 16129442 216 MYLGQIVELGDAQQVL 231
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559

PhnC

COG3638

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

4-222

7.18e-40

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.81 E-value: 7.18e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   4 TLLTLRDVHINFPARKnwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ 83
Cdd:COG3638   1 PMLELRNLSKRYPGGT----------PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGE-ILVDGQDVTA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 --------------MVFQDPlsSLNPRLPV--------------WRIITePLWiakrSSEQQRRALaEELAvQVGIrPEY 135
Cdd:COG3638  70 lrgralrrlrrrigMIFQQF--NLVPRLSVltnvlagrlgrtstWRSLL-GLF----PPEDRERAL-EALE-RVGL-ADK 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 136 LDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:COG3638 140 AYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219


                ....*..
gi 16129442 216 MYLGQIV 222
Cdd:COG3638 220 LRDGRVV 226

ABC_MalK_N

cd03301

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

24-225

1.56e-39

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: 137.77 E-value: 1.56e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNP 95
Cdd:cd03301   8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppKDRDIAMVFQN--YALYP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  96 RLPVWRIITEPLWIAKRSSE---QQRRALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03301  86 HMTVYDNIAFGLKLRKVPKDeidERVREVAELLQIE-----HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129442 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213

ABC_DR_subfamily_A

cd03230

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

30-221

2.40e-39

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: 135.99 E-value: 2.40e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQRIMQM---VFQDPlsSLNPRLPVW 100
Cdd:cd03230  14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsgeikvLGKDIKKEPEEVKRRigyLPEEP--SLYENLTVR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 101 riiteplwiakrsseqqrralaeelavqvgirpEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:cd03230  92 ---------------------------------ENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16129442 181 ILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03230 134 FWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173

ABC_Mj1267_LivG_branched

cd03219

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

6-235

2.57e-39

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: 137.95 E-value: 2.57e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM- 84
Cdd:cd03219   1 LEVRGLTKRF-------GG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLp 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 -----------VFQDP--LSSL----NPRLPVWRIITEPLWIAK-RSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGG 146
Cdd:cd03219  69 pheiarlgigrTFQIPrlFPELtvleNVMVAAQARTGSGLLLARaRREEREARERAEELLERVGLA-DLADRPAGELSYG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGD 226
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226


                ....*....
gi 16129442 227 AQQVLTAPA 235
Cdd:cd03219 227 PDEVRNNPR 235

ABC_ATPase

cd00267

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

22-220

5.89e-39

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: 134.68 E-value: 5.89e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmvfqdplsslnprlpvwr 101
Cdd:cd00267   5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD---------------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 102 iiteplwIAKRSSEQQRRalaeelavQVGIRPEyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:cd00267  63 -------IAKLPLEELRR--------RIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16129442 182 LNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd00267 120 LELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157

NatA

COG4555

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

22-231

5.96e-39

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: 137.30 E-value: 5.96e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRIMQ---MVFQDPlsS 92
Cdd:COG4555   7 LSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgeDVRKEPREARRqigVLPDER--G 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  93 LNPRLPVWRII--TEPLWiakRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:COG4555  85 LYDRLTVRENIryFAELY---GLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442 171 SALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:COG4555 161 NGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220

LivG

COG0411

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

2-235

8.07e-39

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: 137.09 E-value: 8.07e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   2 SDTLLTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI 81
Cdd:COG0411   1 SDPLLEVRGLTKRF-------GG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDI 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  82 MQM------------VFQDP-----LSSL-NPRLPVWRIITEPLWIAK------RSSEQQRRALAEELAVQVGIRpEYLD 137
Cdd:COG0411  69 TGLpphriarlgiarTFQNPrlfpeLTVLeNVLVAAHARLGRGLLAALlrlpraRREEREARERAEELLERVGLA-DRAD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 138 RLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227

                       250
                ....*....|....*...
gi 16129442 218 LGQIVELGDAQQVLTAPA 235
Cdd:COG0411 228 FGRVIAEGTPAEVRADPR 245

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

36-232

1.10e-38

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 136.25 E-value: 1.10e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNPRLPVWRIITEPL 107
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppSRRPVSMLFQE--NNLFSHLTVAQNIGLGL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  108 WIAKRSSEQQRRALaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT 187
Cdd:PRK10771  97 NPGLKLNAAQREKL-HAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16129442  188 LQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219

ABC_Carb_Monos_I

cd03216

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

6-222

1.60e-38

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: 133.71 E-value: 1.60e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmv 85
Cdd:cd03216   1 LELRGITKRFGG-----------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-ILVDGK------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  86 fqdPLSSLNPRLpvwriiteplwiakrsseqqrralaeelAVQVGIRpeyldrLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:cd03216  63 ---EVSFASPRD----------------------------ARRAGIA------MVYQLSVGERQMVEIARALARNARLLI 105

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 166 LDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161

FtsE

COG2884

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

29-223

1.82e-38

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 1.82e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-----------------YIRsgsqRIMQMVFQDplS 91
Cdd:COG2884  15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkrreipYLR----RRIGVVFQD--F 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  92 SLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:COG2884  89 RLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLD-LVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129442 172 ALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:COG2884 167 NLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217

CydC

COG4987

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

6-242

5.01e-38

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

Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 141.44 E-value: 5.01e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY------IRSGSQ 79
Cdd:COG4987 334 LELEDVSFRYPGAGRP---------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdLRDLDE 404

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  80 ----RIMQMVFQDP---LSSL--NPRLpvwriiteplwiAKR--SSEQQRRALAeelavQVGIRPeYLDRLPH------- 141
Cdd:COG4987 405 ddlrRRIAVVPQRPhlfDTTLreNLRL------------ARPdaTDEELWAALE-----RVGLGD-WLAALPDgldtwlg 466

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 142 ----AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLtyVLISHNVSVIRHMsDRVAVMY 217
Cdd:COG4987 467 eggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLE 543

                       250       260
                ....*....|....*....|....*
gi 16129442 218 LGQIVELGDAQQVLTAPAHpYTRLL 242
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGR-YRQLY 567

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

1-239

6.67e-38

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.77 E-value: 6.67e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVhinfpaRKNWLGKTtehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--- 77
Cdd:PRK09452  10 SLSPLVELRGI------SKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdi 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 -----SQRIMQMVFQDplSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELA-VQVgirPEYLDRLPHAFSGGQRQRI 151
Cdd:PRK09452  79 thvpaENRHVNTVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRmVQL---EEFAQRKPHQLSGGQQQRV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233


                 ....*...
gi 16129442  232 TAPAHPYT 239
Cdd:PRK09452 234 EEPKNLFV 241

ABC_tran

pfam00005

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

32-171

1.07e-37

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 131.23 E-value: 1.07e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ----------YIRSGSQRIMQMVFQDPlsSLNPRLPVWR 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdDERKSLRKEIGYVFQDP--QLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442   102 IITEPLWI---AKRSSEQQRRALAEELAvQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:pfam00005  79 NLRLGLLLkglSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_ModC_like

cd03299

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

34-234

1.26e-37

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: 133.62 E-value: 1.26e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMVFQDplSSLNPRLPVWRIITE 105
Cdd:cd03299  17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppeKRDISYVPQN--YALFPHMTVYKNIAY 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 106 PLWIAKRS-SEQQRRALaeELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:cd03299  95 GLKKRKVDkKEIERKVL--EIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129442 185 LVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

32-245

1.44e-37

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 134.06 E-value: 1.44e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQP----SHGQYIRSGSQ--------RIMQMVFQDPLSSLNPRLPV 99
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPvapcalrgRKIATIMQNPRSAFNPLHTM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 WRIITEPLWIAKRSSEQQRRALAEElAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:PRK10418  99 HTHARETCLALGKPADDATLTAALE-AVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDS 245
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243

potA

TIGR01187

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

47-238

1.45e-37

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: 136.08 E-value: 1.45e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    47 IVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------RIMQMVFQDplSSLNPRLPVWRIITEPLWIAKRSSEQQR 118
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvtnvpphlRHINMVFQS--YALFPHMTVEENVAFGLKMRKVPRAEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   119 RALAEELA-VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYV 197
Cdd:TIGR01187  79 PRVLEALRlVQLE---EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 16129442   198 LISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPY 238
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

32-225

1.66e-37

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: 131.40 E-value: 1.66e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrIMqmVFQDPLSSLNPRlpvwriiteplWIAK 111
Cdd:cd03214  15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--------IL--LDGKDLASLSPK-----------ELAR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 112 RsseqqrRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEN 191
Cdd:cd03214  74 K------IAYVPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE 146

                       170       180       190
                ....*....|....*....|....*....|....
gi 16129442 192 HGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03214 147 RGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180

ABC_CysA_sulfate_importer

cd03296

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

31-238

2.75e-37

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: 132.85 E-value: 2.75e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNPRLPVWRI 102
Cdd:cd03296  17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvQERNVGFVFQH--YALFRHMTVFDN 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 103 ITEPLWIAKRS---SEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:cd03296  95 VAFGLRVKPRSerpPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPY 238
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232

ArtP

COG4161

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

31-227

4.27e-37

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.44 E-value: 4.27e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------------RIMQMVFQDplSSLN 94
Cdd:COG4161  17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairllrQKVGMVFQQ--YNLW 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  95 PRLPVWRIITE-PLWIAKRSsEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:COG4161  95 PHLTVMENLIEaPCKVLGLS-KEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16129442 174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDA 227
Cdd:COG4161 173 DPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

31-235

4.87e-37

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 4.87e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI---------------MQMVFQDPLSSLNP 95
Cdd:PRK13634  22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT-VTIGERVItagkknkklkplrkkVGIVFQFPEHQLFE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   96 RLPVWRIITEPLWIAkrSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13634 101 ETVEKDICFGPMNFG--VSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  176 SVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA 235
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238

ABC_phnC

TIGR02315

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

29-230

1.94e-36

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: 130.88 E-value: 1.94e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------------SQRIMQMVFQD-----PL 90
Cdd:TIGR02315  15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrkLRRRIGMIFQHynlieRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    91 SS----LNPRL---PVWRIITEPLwiakrSSEQQRRALaeELAVQVGIRPEYLDRLpHAFSGGQRQRIAIARALSSQPDV 163
Cdd:TIGR02315  95 TVlenvLHGRLgykPTWRSLLGRF-----SEEDKERAL--SALERVGLADKAYQRA-DQLSGGQQQRVAIARALAQQPDL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442   164 IVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:TIGR02315 167 ILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

22-241

2.33e-36

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.81 E-value: 2.33e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMVFQDplSSL 93
Cdd:PRK11607  25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyQRPINMMFQS--YAL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   94 NPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGL-VHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  174 DISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLtapAHPYTRL 241
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTRY 245

ntrCD

TIGR01184

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

32-224

2.91e-36

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: 129.89 E-value: 2.91e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ-------RIMqmVFQDplSSLNPrlpvWRIIT 104
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitepgpdRMV--VFQN--YSLLP----WLTVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   105 EPLWIAKRS-----SEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:TIGR01184  73 ENIALAVDRvlpdlSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16129442   180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM------YLGQIVEL 224
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

1-231

2.93e-36

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 131.51 E-value: 2.93e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFParknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--- 77
Cdd:PRK13636   1 MEDYILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpi 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 ---SQRIMQ------MVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRAlaEELAVQVGIRPeYLDRLPHAFSGGQR 148
Cdd:PRK13636  71 dysRKGLMKlresvgMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV--DNALKRTGIEH-LKDKPTHCLSFGQK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQ 228
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227


                 ...
gi 16129442  229 QVL 231
Cdd:PRK13636 228 EVF 230

MdlB

COG1132

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

31-241

4.33e-36

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.06 E-value: 4.33e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MVFQDPL---SSL--N 94
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR-ILIDGVDIRDltleslrrqigVVPQDTFlfsGTIreN 433

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  95 prlpvwriITepLWIAKRSSEQQRRALAeelAVQVGirpEYLDRLPH-----------AFSGGQRQRIAIARALSSQPDV 163
Cdd:COG1132 434 --------IR--YGRPDATDEEVEEAAK---AAQAH---EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPI 497

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 164 IVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELGDAQQVLTAPAHpYTRL 241
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEELLARGGL-YARL 571

LolD_lipo_ex

TIGR02211

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...

32-223

5.06e-36

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

Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 129.01 E-value: 5.06e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQ--------RIMQMVFQdpLSSLNPRL 97
Cdd:TIGR02211  21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTsgevlfNGQSLSKLSSneraklrnKKLGFIYQ--FHHLLPDF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    98 PVWRIITEPLWIAKRS-SEQQRRALAEELAVQVGIRpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:TIGR02211  99 TALENVAMPLLIGKKSvKEAKERAYEMLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNN 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 16129442   177 VQAQILNLLVTLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:TIGR02211 176 NAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221

YbbA

COG4181

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

1-228

7.86e-36

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: 128.71 E-value: 7.86e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPARknwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG4181   4 SSAPIIELRGLTKTVGTG-------AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-VRLAGQD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  81 IMQM---------------VFQDplSSLNPRLPVWRIITEPLWIAkrsSEQQRRALAEELAVQVGIRpEYLDRLPHAFSG 145
Cdd:COG4181  76 LFALdedararlrarhvgfVFQS--FQLLPTLTALENVMLPLELA---GRRDARARARALLERVGLG-HRLDHYPAQLSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228


                ...
gi 16129442 226 DAQ 228
Cdd:COG4181 229 AAT 231

TauB

COG4525

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

4-223

1.99e-35

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 128.44 E-value: 1.99e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   4 TLLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ 83
Cdd:COG4525   2 SMLTVRHVSVRYPGGG-------QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 ------MVFQDplSSLNPRLPVWRIITEPLWIAKRSsEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:COG4525  74 pgadrgVVFQK--DALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARAL 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM--YLGQIVE 223
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217

ABC_ThiQ_thiamine_transporter

cd03298

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

36-225

3.63e-35

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: 126.45 E-value: 3.63e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNPRLPVWRIITEPL 107
Cdd:cd03298  18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappADRPVSMLFQE--NNLFAHLTVEQNVGLGL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 108 WIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT 187
Cdd:cd03298  96 SPGLKLTAEDRQAIEVALA-RVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16129442 188 LQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211

ABC_ModC_molybdenum_transporter

cd03297

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

35-225

4.19e-35

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: 126.26 E-value: 4.19e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  35 IDLQIRrGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------------QRIMQMVFQDplSSLNPRLPVW 100
Cdd:cd03297  17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqQRKIGLVFQQ--YALFPHLNVR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 101 RIITeplWIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:cd03297  94 ENLA---FGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16129442 181 ILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

35-228

4.55e-35

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 4.55e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------------RIMQMVFQDplSSLNPRLP 98
Cdd:PRK11124  21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkairelrRNVGMVFQQ--YNLWPHLT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITE-PLWIAKRSsEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK11124  99 VQQNLIEaPCRVLGLS-KDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129442  178 QAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQ 228
Cdd:PRK11124 177 TAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226

ABC_PhnC_transporter

cd03256

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

22-230

5.79e-35

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: 126.91 E-value: 5.79e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEH-VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ-------------RIMQMVFQ 87
Cdd:cd03256   6 LSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrRQIGMIFQ 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  88 DPlsSLNPRLPVW------RIITEPLW--IAKRSSEQQRRALAEELAvQVGIRPEYLDRLpHAFSGGQRQRIAIARALSS 159
Cdd:cd03256  86 QF--NLIERLSVLenvlsgRLGRRSTWrsLFGLFPKEEKQRALAALE-RVGLLDKAYQRA-DQLSGGQQQRVAIARALMQ 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTyVLIS-HNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGIT-VIVSlHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

ModC

COG4148

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

35-268

3.05e-34

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: 127.91 E-value: 3.05e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS---------------QRIMQMVFQDPlsSLNPRLPV 99
Cdd:COG4148  18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG-RIRLGGevlqdsargiflpphRRRIGYVFQEA--RLFPHLSV 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 WRIItepLWIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:COG4148  95 RGNL---LYGRKRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHpyTRLLLDS-----LPAIDKPLE 254
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDL--LPLAGGEeagsvLEATVAAHD 248

                       250
                ....*....|....
gi 16129442 255 EEWALRKTDLPGNR 268
Cdd:COG4148 249 PDYGLTRLALGGGR 262

ABC_Metallic_Cations

cd03235

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

28-216

7.56e-34

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: 123.03 E-value: 7.56e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMVFQdpLSSLNPRLP--VW 100
Cdd:cd03235  11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekERKRIGYVPQ--RRSIDRDFPisVR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 101 RIITEPLW----IAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03235  89 DVVLMGLYghkgLFRRLSKADKAKVDEALE-RVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16129442 177 VQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03235 167 TQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

29-231

9.46e-34

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 129.15 E-value: 9.46e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSG----------------SQRIMQMVFQDplS 91
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvNVRVGdewvdmtkpgpdgrgrAKRYIGILHQE--Y 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    92 SLNPRLPVWRIITEPLWIAKRSSEQQRRALAeeLAVQVGIRPEY----LDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILD 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442   168 EPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516

ABC_DrrA

cd03265

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

31-225

3.28e-33

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: 121.71 E-value: 3.28e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS---------QRIMQMVFQDPlsSLNPRLPVWr 101
Cdd:cd03265  15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvreprevRRRIGIVFQDL--SVDDELTGW- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 102 iitEPLWIAKR---SSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:cd03265  92 ---ENLYIHARlygVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16129442 179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214

modC_ABC

TIGR02142

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

35-238

3.79e-33

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: 124.84 E-value: 3.79e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------------QRIMQMVFQDplSSLNPRLPVW 100
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppeKRRIGYVFQE--ARLFPHLSVR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   101 RIITEPLWiakRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:TIGR02142  94 GNLRYGMK---RARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442   181 ILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPY 238
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227

MglA

COG1129

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

2-230

6.45e-33

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 6.45e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   2 SDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG---- 77
Cdd:COG1129   1 AEPLLEMRGISKSFGG-----------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvr 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  78 ------SQR--ImQMVFQDPlsSLNPRLPVW------RIITEPLWIAKRSSEQQRRALAEELavQVGIRPeylDRLPHAF 143
Cdd:COG1129  70 frsprdAQAagI-AIIHQEL--NLVPNLSVAeniflgREPRRGGLIDWRAMRRRARELLARL--GLDIDP---DTPVGDL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220


                ....*..
gi 16129442 224 LGDAQQV 230
Cdd:COG1129 221 TGPVAEL 227

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

20-221

6.77e-33

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 121.71 E-value: 6.77e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   20 NWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS------QRIMQMVFQDPlssl 93
Cdd:PRK11247  16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeaREDTRLMFQDA---- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   94 npRLPVWRIITEPLWIAKRSS--EQQRRALAEelavqVGIRPEYLDrLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK11247  91 --RLLPWKKVIDNVGLGLKGQwrDAALQALAA-----VGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129442  172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212

PRK13633

energy-coupling factor transporter ATPase;

23-230

8.08e-33

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 122.12 E-value: 8.08e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   23 GKTTEHVhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------RIMQ---MVFQDPLS 91
Cdd:PRK13633  18 EESTEKL-ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwDIRNkagMVFQNPDN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   92 SLnprlpVWRIITE------------PLWIAKRSSEQQRRalaeelavqVGIRpEYLDRLPHAFSGGQRQRIAIARALSS 159
Cdd:PRK13633  97 QI-----VATIVEEdvafgpenlgipPEEIRERVDESLKK---------VGMY-EYRRHAPHLLSGGQKQRVAIAGILAM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHnvsvirHM-----SDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH------YMeeaveADRIIVMDSGKVVMEGTPKEI 231

ABC_MTABC3_MDL1_MDL2

cd03249

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

7-231

1.04e-32

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: 120.72 E-value: 1.04e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   7 TLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmvf 86
Cdd:cd03249   2 EFKNVSFRYPSRPD--------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG--------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  87 qDPLSSLNPRLpvWR-----IITEPLWIA------------KRSSEQQRRAlaeelAVQVGIRpEYLDRLPHAF------ 143
Cdd:cd03249  65 -VDIRDLNLRW--LRsqiglVSQEPVLFDgtiaenirygkpDATDEEVEEA-----AKKANIH-DFIMSLPDGYdtlvge 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 144 -----SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYL 218
Cdd:cd03249 136 rgsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQN 212

                       250
                ....*....|...
gi 16129442 219 GQIVELGDAQQVL 231
Cdd:cd03249 213 GQVVEQGTHDELM 225

ABC_subfamily_A

cd03263

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

29-229

1.07e-32

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: 120.30 E-value: 1.07e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRIMQMV---FQDplSSLNPRLPV 99
Cdd:cd03263  15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingySIRTDRKAARQSLgycPQF--DALFDELTV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 WriitEPLWI---AKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03263  93 R----EHLRFyarLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129442 177 VQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:cd03263 168 SRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218

ABC_cobalt_CbiO_domain2

cd03226

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

32-222

1.68e-32

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: 119.28 E-value: 1.68e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------QRIMQMVFQDPLSSLNpRLPVWRIIT 104
Cdd:cd03226  16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerRKSIGYVMQDVDYQLF-TDSVREELL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 105 EPLWIAKRSSEQQRRALAE-ELAvqvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILN 183
Cdd:cd03226  95 LGLKELDAGNEQAETVLKDlDLY-------ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16129442 184 LLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03226 168 LIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

13-241

2.09e-32

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 2.09e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   13 INFPARKNWLGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI---------RSGSQRIMQ 83
Cdd:PRK09493   2 IEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvndpKVDERLIRQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   84 ---MVFQDplSSLNPRLPVWR-IITEPLWIaKRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSS 159
Cdd:PRK09493  78 eagMVFQQ--FYLFPHLTALEnVMFGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPahPYT 239
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP--PSQ 230


                 ..
gi 16129442  240 RL 241
Cdd:PRK09493 231 RL 232

thiQ

TIGR01277

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

36-226

2.10e-32

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: 119.20 E-value: 2.10e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMVFQDplSSLNPRLPVWRIITEPL 107
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapYQRPVSMLFQE--NNLFAHLTVRQNIGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   108 WIA-KRSSEQQRRAlaEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:TIGR01277  96 HPGlKLNAEQQEKV--VDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 16129442   187 TLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGD 226
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

27-231

1.13e-31

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 117.71 E-value: 1.13e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  27 EHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMvfqdPLSSLNPRLPVwrIITEP 106
Cdd:cd03254  14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ-ILIDGIDIRDI----SRKSLRSMIGV--VLQDT 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 107 LWIA-------KRSSEQQRRALAEELAVQVGIRpEYLDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:cd03254  87 FLFSgtimeniRLGRPNATDEEVIEAAKEAGAH-DFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDE 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442 169 PTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVL 231
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

5-234

1.24e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 1.24e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRDVHINFParknwlgKTTEhvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS------ 78
Cdd:PRK13639   1 ILETRDLKYSYP-------DGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydk 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   79 ------QRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIA 152
Cdd:PRK13639  71 ksllevRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRV--KEALKAVGME-GFENKPPHHLSGGQKKRVA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226


                 ..
gi 16129442  233 AP 234
Cdd:PRK13639 227 DI 228

cbiO

PRK13646

energy-coupling factor transporter ATPase;

23-223

2.40e-31

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 2.40e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   23 GKTTEHVhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG---------------QYIRSGSQRImQMVFQ 87
Cdd:PRK13646  15 GTPYEHQ-AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdditithktkdKYIRPVRKRI-GMVFQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   88 DPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALaeELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13646  93 FPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAH--RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  168 EPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

25-232

2.56e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 2.56e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   25 TTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--------------YIRSGsqriMQMVFQDPL 90
Cdd:PRK13632  18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEikidgitiskenlkEIRKK----IGIIFQNPD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   91 SSLnprlpvwrI-ITEPLWIA-----KRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVI 164
Cdd:PRK13632  94 NQF--------IgATVEDDIAfglenKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEII 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442  165 VLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVS-VIrhMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAI--LADKVIVFSEGKLIAQGKPKEILN 231

cbiO

PRK13637

energy-coupling factor transporter ATPase;

31-230

4.24e-31

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.84 E-value: 4.24e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----SQRI--------MQMVFQDPLSSLNPRLP 98
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVklsdirkkVGLVFQYPEYQLFEETI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITEPLWIAKRSSEQQRRAL-AEELavqVGIRPE-YLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKrAMNI---VGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129442  177 VQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

1-235

5.23e-31

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.05 E-value: 5.23e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YI----- 74
Cdd:PRK11432   2 TQKNFVVLKNITKRF-------GSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIdgedv 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   75 --RSGSQRIMQMVFQDplSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAV--QVGIRPEYLDRLphafSGGQRQR 150
Cdd:PRK11432  71 thRSIQQRDICMVFQS--YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELvdLAGFEDRYVDQI----SGGQQQR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224


                 ....*
gi 16129442  231 LTAPA 235
Cdd:PRK11432 225 YRQPA 229

ABC_TM1139_LivF_branched

cd03224

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

29-231

6.31e-31

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: 115.61 E-value: 6.31e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQM----VFQDPlsSLNPRL 97
Cdd:cd03224  13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglpPHERARAgigyVPEGR--RIFPEL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  98 PVwriiTEPLWIAkrSSEQQRRALAEELAVQVGIRP---EYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03224  91 TV----EENLLLG--AYARRRAKRKARLERVYELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 175 ISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:cd03224 165 PKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220

ABCC_Protease_Secretion

cd03246

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

6-221

7.97e-31

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: 113.85 E-value: 7.97e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWLgkttehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmv 85
Cdd:cd03246   1 LEVENVSFRYPGAEPPV---------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR-VRLDGA------ 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  86 fqdPLSSLNPrlpvwriiteplwiakrsseqqrralaEELAVQVGIRPEYLDRLP-----HAFSGGQRQRIAIARALSSQ 160
Cdd:cd03246  65 ---DISQWDP---------------------------NELGDHVGYLPQDDELFSgsiaeNILSGGQRQRLGLARALYGN 114

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442 161 PDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRhMSDRVAVMYLGQI 221
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173

cbiO

PRK13644

energy-coupling factor transporter ATPase;

31-282

8.15e-31

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.01 E-value: 8.15e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-----------QRIMQMVFQDPLSSLnprlpV 99
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgiRKLVGIVFQNPETQF-----V 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 WRIITE------------PLWIAKRSSeqqrRALAEelavqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13644  92 GRTVEEdlafgpenlclpPIEIRKRVD----RALAE-----IGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  168 EPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIrHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDSLp 247
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSL- 238

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 16129442  248 aIDkpLEEEWALRKTDLPGNRTLPQGCFFYERCPL 282
Cdd:PRK13644 239 -IE--LAENLKMHGVVIPWENTSSPSSFAEEICRL 270

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

6-225

1.01e-30

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: 113.95 E-value: 1.01e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimQMV 85
Cdd:cd03247   1 LSINNVSFSYPEQEQQ---------VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP---VSD 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  86 FQDPLSSLNPRLPvwriiteplwiakrsseQQRRALAEELAVQVGIRpeyldrlphaFSGGQRQRIAIARALSSQPDVIV 165
Cdd:cd03247  69 LEKALSSLISVLN-----------------QRPYLFDTTLRNNLGRR----------FSGGERQRLALARILLQDAPIVL 121

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 166 LDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178

PRK14239

phosphate transporter ATP-binding protein; Provisional

1-239

5.62e-30

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 5.62e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS--------- 69
Cdd:PRK14239   1 MTEPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivy 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   70 HGQYIRSGSQRIMQ------MVFQDPlsslNP-RLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLpH- 141
Cdd:PRK14239  70 NGHNIYSPRTDTVDlrkeigMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-Hd 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  142 ---AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:PRK14239 145 salGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLD 222

                        250       260
                 ....*....|....*....|.
gi 16129442  219 GQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKET 243

PRK10070

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

37-240

1.24e-29

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.29 E-value: 1.24e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   37 LQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------------SQRIMQMVFQDplSSLNPRLPVWRI 102
Cdd:PRK10070  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevRRKKIAMVFQS--FALMPHMTVLDN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  103 ITEPLWIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALR-QVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  183 NLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTR 240
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

31-230

1.37e-29

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 1.37e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQ-----------RIMQMVFQDPLSSL------ 93
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-ITVGGMvlseetvwdvrRQVGMVFQNPDNQFvgatvq 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   94 --------NPRLPvwriiteplwiakrSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:PRK13635 101 ddvafgleNIGVP--------------REEMVERV--DQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  166 LDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

6-241

1.55e-29

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: 117.88 E-value: 1.55e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     6 LTLRDVHINFPARKNWLgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS------- 78
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldp 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    79 ---QRIMQMVFQDPL----SSL-NPRLPVWRIITEPLWIAKRSSEQQR--RALAEELAVQVGIRPEYLdrlphafSGGQR 148
Cdd:TIGR02204 410 aelRARMALVPQDPVlfaaSVMeNIRYGRPDATDEEVEAAARAAHAHEfiSALPEGYDTYLGERGVTL-------SGGQR 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGdAQ 228
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQG-TH 558

                         250
                  ....*....|...
gi 16129442   229 QVLTAPAHPYTRL 241
Cdd:TIGR02204 559 AELIAKGGLYARL 571

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

31-231

1.72e-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: 112.32 E-value: 1.72e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMVFQDP-LSSLNprlpv 99
Cdd:cd03251  17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslRRQIGLVSQDVfLFNDT----- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 wriITEPLWIAKR--SSEQQRRALAEELAVqvgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVL 166
Cdd:cd03251  92 ---VAENIAYGRPgaTREEVEEAARAANAH------EFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILIL 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 167 DEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVL 231
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

32-233

1.86e-29

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.56 E-value: 1.86e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmVFQDPLSSLNPR--------LP----- 98
Cdd:PRK13548  18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE-VR---------LNGRPLADWSPAelarrravLPqhssl 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 --------VWRIITEPLwiakRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARAL------SSQPDVI 164
Cdd:PRK13548  88 sfpftveeVVAMGRAPH----GLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442  165 VLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

29-256

2.13e-29

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.97 E-value: 2.13e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMVFQDPLSSLNPRLP 98
Cdd:PRK13652  17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenirevrKFVGLVFQNPDDQIFSPTV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITEPLWIAKRSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK13652  97 EQDIAFGPINLGLDEETVAHRV--SSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442  179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP-AHPYTRLLLDSLPAIDKPLEEE 256
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPdLLARVHLDLPSLPKLIRSLQAQ 252

PRK10619

histidine ABC transporter ATP-binding protein HisP;

1-237

2.89e-29

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 112.37 E-value: 2.89e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFparknwlgktTEHvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYI 74
Cdd:PRK10619   1 MSENKLNVIDLHKRY----------GEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngQTI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   75 RSGSQRIMQMVFQDP--LSSLNPRLP-------VWRIIT-------EPLWIAKRSsEQQRRALAEELAVQVGIRPEYLDR 138
Cdd:PRK10619  70 NLVRDKDGQLKVADKnqLRLLRTRLTmvfqhfnLWSHMTvlenvmeAPIQVLGLS-KQEARERAVKYLAKVGIDERAQGK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:PRK10619 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQ 227

                        250
                 ....*....|....*....
gi 16129442  219 GQIVELGDAQQVLTAPAHP 237
Cdd:PRK10619 228 GKIEEEGAPEQLFGNPQSP 246

CcmA

COG4133

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

34-201

3.49e-29

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: 110.65 E-value: 3.49e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQRIM------QMVFQDPLSSLNPRLPVWRIITep 106
Cdd:COG4133  20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvLWNGEPIRDAredyrrRLAYLGHADGLKPELTVRENLR-- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 107 lWIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:COG4133  98 -FWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175

                       170
                ....*....|....*
gi 16129442 187 TLQENHGLTyVLISH 201
Cdd:COG4133 176 AHLARGGAV-LLTTH 189

YnjD

COG4136

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

6-229

9.43e-29

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.49 E-value: 9.43e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHInfparknwlgkTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQYIRS 76
Cdd:COG4136   2 LSLENLTI-----------TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsasgevllNGRRLTA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  77 GS--QRIMQMVFQDPLssLNPRLPVWRIItePLWIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG4136  71 LPaeQRRIGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALL 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVsvirhmSDRVAVmylGQIVELGDAQQ 229
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE------EDAPAA---GRVLDLGNWQH 211

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

3-233

1.04e-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: 110.56 E-value: 1.04e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI-----RSG 77
Cdd:COG1119   1 DPLLELRNVTVRRGGKT-----------ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgeRRG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  78 S-------QRI------MQMVFQdplsslnPRLPVWRII------TEPLWiaKRSSEQQRRaLAEELAVQVGIRpEYLDR 138
Cdd:COG1119  70 GedvwelrKRIglvspaLQLRFP-------RDETVLDVVlsgffdSIGLY--REPTDEQRE-RARELLELLGLA-HLADR 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218

                       250
                ....*....|....*
gi 16129442 219 GQIVELGDAQQVLTA 233
Cdd:COG1119 219 GRVVAAGPKEEVLTS 233

ABC_FtsE

cd03292

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

29-221

1.09e-28

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: 109.42 E-value: 1.09e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMVFQDplSSLNP 95
Cdd:cd03292  14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylRRKIGVVFQD--FRLLP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  96 RLPVWRIITEPLWIAKRSSEQQRRALAEELAvQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:cd03292  92 DRNVYENVAFALEVTGVPPREIRKRVPAALE-LVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16129442 176 SVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03292 170 DTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214

ABCC_bacteriocin_exporters

cd03245

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

6-222

1.33e-28

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: 109.60 E-value: 1.33e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM- 84
Cdd:cd03245   3 IEFRNVSFSYPNQEI---------PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIRQLd 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 ----------VFQDPlsslnpRLpVWRIITEPLWIAKRSSEQQRRALAEELAvqvGIRpEYLDRLPHAF----------- 143
Cdd:cd03245  73 padlrrnigyVPQDV------TL-FYGTLRDNITLGAPLADDERILRAAELA---GVT-DFVNKHPNGLdlqigergrgl 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRhMSDRVAVMYLGQIV 222
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217

NupO

COG3845

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

1-222

1.36e-28

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 1.36e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQ 79
Cdd:COG3845   1 MMPPALELRGITKRFGG-----------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEiLIDGKPV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  80 RIMQ----------MVFQDPlsSLNPRLPVWR-II--TEPLW---IAKRSSEQQRRALAEELAVQVGirpeyLDRLPHAF 143
Cdd:COG3845  70 RIRSprdaialgigMVHQHF--MLVPNLTVAEnIVlgLEPTKggrLDRKAARARIRELSERYGLDVD-----PDAKVEDL 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219


                .
gi 16129442 222 V 222
Cdd:COG3845 220 V 220

HisP

COG4598

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

34-234

1.52e-28

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 110.28 E-value: 1.52e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  34 GIDLQIRRGETLGIVGESGCGKSTLAQLlMGML-QPSHGQYI-----------RSGS---------QRI---MQMVFQdp 89
Cdd:COG4598  26 GVSLTARKGDVISIIGSSGSGKSTFLRC-INLLeTPDSGEIRvggeeirlkpdRDGElvpadrrqlQRIrtrLGMVFQ-- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  90 lsSLN--PRLPVWRIITE-PLWIAKRSsEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:COG4598 103 --SFNlwSHMTVLENVIEaPVHVLGRP-KAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 167 DEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

31-230

1.52e-28

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 1.52e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MVFQDPLSSLnprlpV 99
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDdnfeklrkhigIVFQNPDNQF-----V 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 WRIITEPLWIAKR----SSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13648  98 GSIVKYDVAFGLEnhavPYDEMHRRVSEALK-QVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  176 SVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

31-233

1.93e-28

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: 109.50 E-value: 1.93e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMVFQ----------DPL 90
Cdd:cd03252  17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlRRQVGVVLQenvlfnrsirDNI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  91 SSLNPRLPVWRIIteplwiakrssEQQRRALAEELAVQVgirPEYLDRL----PHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:cd03252  97 ALADPGMSMERVI-----------EAAKLAGAHDFISEL---PEGYDTIvgeqGAGLSGGQRQRIAIARALIHNPRILIF 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 167 DEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226

ABC_BcrA_bacitracin_resist

cd03268

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

22-223

1.98e-28

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: 108.46 E-value: 1.98e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyirSGSQRIMQMVFQDPLSSLNpRLPVwr 101
Cdd:cd03268   6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD------SGEITFDGKSYQKNIEALR-RIGA-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 102 IITEPLWIAKRSSEQQRRALA----------EELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:cd03268  77 LIEAPGFYPNLTARENLRLLArllgirkkriDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129442 172 ALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

27-231

1.99e-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: 109.24 E-value: 1.99e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  27 EHVH--------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVfqdpLSSLNPRLP 98
Cdd:cd03253   4 ENVTfaydpgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-ILIDGQDIREVT----LDSLRRAIG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  99 VWRIITePLW-------IA----KRSSEQQRRA------------LAEELAVQVGIRPEYLdrlphafSGGQRQRIAIAR 155
Cdd:cd03253  79 VVPQDT-VLFndtigynIRygrpDATDEEVIEAakaaqihdkimrFPDGYDTIVGERGLKL-------SGGEKQRVAIAR 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442 156 ALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVL 231
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223

LivF

COG0410

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

3-235

3.45e-28

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: 108.53 E-value: 3.45e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIM 82
Cdd:COG0410   1 MPMLEVENLHAGYGG-----------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS-IRFDGEDIT 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  83 QM------------------VFqdplsslnPRLPVWriitEPLWIA---KRSSEQQRRALAE------ELAvqvgirpEY 135
Cdd:COG0410  69 GLpphriarlgigyvpegrrIF--------PSLTVE----ENLLLGayaRRDRAEVRADLERvyelfpRLK-------ER 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 136 LDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:COG0410 130 RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYV 208

                       250       260
                ....*....|....*....|
gi 16129442 216 MYLGQIVELGDAQQVLTAPA 235
Cdd:COG0410 209 LERGRIVLEGTAAELLADPE 228

cbiO

PRK13649

energy-coupling factor transporter ATPase;

31-230

4.53e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.45 E-value: 4.53e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGSQR--IMQ------MVFQDPLSSLNPR 96
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddTLITSTSKNkdIKQirkkvgLVFQFPESQLFEE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   97 LPVWRIITEP--LWIAKRSSEQqrraLAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:PRK13649 102 TVLKDVAFGPqnFGVSQEEAEA----LAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  175 ISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

32-239

5.04e-28

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.98 E-value: 5.04e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ------PSHGQYIRSGS----------QRIMQMVFQDPlsSLNP 95
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKdifqidaiklRKEVGMVFQQP--NPFP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   96 RLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  173 LDIsVQAQILNLLVTLQENHgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248

ABC_NatA_sodium_exporter

cd03266

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

28-225

6.78e-28

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: 107.45 E-value: 6.78e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmVFQDPLS------------SLNP 95
Cdd:cd03266  17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-----VVKEPAEarrrlgfvsdstGLYD 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  96 RLPVWRIIT--EPLWIAKRSSEQQRralAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:cd03266  92 RLTARENLEyfAGLYGLKGDELTAR---LEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129442 174 DISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03266 168 DVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

24-235

9.52e-28

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.55 E-value: 9.52e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG-----------------QYIRSGSQRI----- 81
Cdd:PRK13631  34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnheLITNPYSKKIknfke 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   82 ----MQMVFQDPLSSLNPRLPVWRIITEPlwIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:PRK13631 114 lrrrVSMVFQFPEYQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA 235
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268

type_I_sec_HlyB

TIGR01846

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...

32-241

1.07e-27

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

Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.91 E-value: 1.07e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMVFQDplsslnpRLPVWR 101
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdlaiadpawlRRQMGVVLQE-------NVLFSR 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   102 IITEPLWIAKRSSEQQRRALAEELAVQVgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:TIGR01846 546 SIRDNIALCNPGAPFEHVIHAAKLAGAH----DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFDEAT 621

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442   171 SALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGdAQQVLTAPAHPYTRL 241
Cdd:TIGR01846 622 SALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG-RHEELLALQGLYARL 688

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

30-239

1.13e-27

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.13e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH-----------GQYIRSGS------QRIMQMVFQDPlsS 92
Cdd:PRK14267  18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDvdpievRREVGMVFQYP--N 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   93 LNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQ-VGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK14267  96 PFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKkAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442  169 PTSALDISVQAQILNLLVTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244

cbiO

PRK13643

energy-coupling factor transporter ATPase;

31-231

1.55e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 1.55e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS---------------QRIMQMVFQDPLSSLNP 95
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK-VTVGDivvsstskqkeikpvRKKVGVVFQFPESQLFE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   96 RLPVWRIITEP--LWIAKRSSEQqrraLAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13643 100 ETVLKDVAFGPqnFGIPKEKAEK----IAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK13643 176 DPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232

type_I_sec_LssB

TIGR03375

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

8-233

1.84e-27

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: 112.27 E-value: 1.84e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     8 LRDVHINFPARKNwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG----------QYIRSG 77
Cdd:TIGR03375 466 FRNVSFAYPGQET---------PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdirQIDPAD 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    78 SQRIMQMVFQDPlsslnpRLpVWRIITEPLWIAKRSSEQQRRALAEELAvqvGIRpEYLDRLPHAF-----------SGG 146
Cdd:TIGR03375 537 LRRNIGYVPQDP------RL-FYGTLRDNIALGAPYADDEEILRAAELA---GVT-EFVRRHPDGLdmqigergrslSGG 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVtlQENHGLTYVLISHNVSVIRhMSDRVAVMYLGQIVELGD 226
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLK--RWLAGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGP 682


                  ....*..
gi 16129442   227 AQQVLTA 233
Cdd:TIGR03375 683 KDQVLEA 689

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

1-233

2.03e-27

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.09 E-value: 2.03e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   1 MSDtLLTLRDVHINFPAR-------KNWL----GKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS 69
Cdd:COG1134   1 MSS-MIEVENVSKSYRLYhepsrslKELLlrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  70 HGQYIRSGsqRImqmvfqdplSSL-------NPRLPVW-------RIIteplwiaKRSSEQQRRALAE--ELAvQVGirp 133
Cdd:COG1134  80 SGRVEVNG--RV---------SALlelgagfHPELTGReniylngRLL-------GLSRKEIDEKFDEivEFA-ELG--- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 134 EYLDrLP-HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGlTYVLISHNVSVIRHMSDR 212
Cdd:COG1134 138 DFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDR 215

                       250       260
                ....*....|....*....|.
gi 16129442 213 VAVMYLGQIVELGDAQQVLTA 233
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236

ugpC

PRK11650

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

6-235

2.86e-27

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.78 E-value: 2.86e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    6 LTLRDVhinfpaRKNWLGKTtehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-- 83
Cdd:PRK11650   4 LKLQAV------RKSYDGKT----QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNEle 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   84 -------MVFQDplSSLNPRLPVWRIITEPLWIAKrSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARA 156
Cdd:PRK11650  73 padrdiaMVFQN--YALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442  157 LSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA 235
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

8-224

3.95e-27

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 3.95e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   8 LRDVHINFPARKnwLgkttehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRI---MQM 84
Cdd:COG0488   1 LENLSKSFGGRP--L---------LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIgylPQE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 VFQDP--------LSSLNPRLPVWRII-------TEPLWIAKRSSEQQRR----------ALAEELAVQVGIRPEYLDRL 139
Cdd:COG0488  70 PPLDDdltvldtvLDGDAELRALEAELeeleaklAEPDEDLERLAELQEEfealggweaeARAEEILSGLGFPEEDLDRP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 140 PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQ--AQILNllvtlqeNHGLTYVLISHNvsviRHMSDRVAvm 216
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFLK-------NYPGTVLVVSHD----RYFLDRVA-- 216


                ....*...
gi 16129442 217 ylGQIVEL 224
Cdd:COG0488 217 --TRILEL 222

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

7-225

4.24e-27

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.58 E-value: 4.24e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    7 TLRDVhinfparknwlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIrsGSQRI---- 81
Cdd:PRK11000   5 TLRNV-----------TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlFI--GEKRMndvp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   82 -----MQMVFQDplSSLNPRLPVWRIITEPLWIAK-RSSEQQRR--ALAEELavQVGirpEYLDRLPHAFSGGQRQRIAI 153
Cdd:PRK11000  72 paergVGMVFQS--YALYPHLSVAENMSFGLKLAGaKKEEINQRvnQVAEVL--QLA---HLLDRKPKALSGGQRQRVAI 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

6-202

6.31e-27

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: 110.14 E-value: 6.31e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     6 LTLRDVHINFPARKNwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmv 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPP----------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV------- 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    86 fqdPLSSLNPRLPVWRI-------------ITEPLWIAKR--SSEQQRRALAeelAVQVGirpEYLDRLPH--------- 141
Cdd:TIGR02868 398 ---PVSSLDQDEVRRRVsvcaqdahlfdttVRENLRLARPdaTDEELWAALE---RVGLA---DWLRALPDgldtvlgeg 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442   142 --AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHN 202
Cdd:TIGR02868 469 gaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529

ABC_drug_resistance_like

cd03264

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

22-225

8.35e-27

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: 104.58 E-value: 8.35e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQIRRGeTLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-SQRIMQMVFQDPLSSL------N 94
Cdd:cd03264   6 LTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLRRRIGYLpqefgvY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  95 PRLPVWRIITEPLWIAKRSSEQQRRALAEEL-AVQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:cd03264  85 PNFTVREFLDYIAWLKGIPSKEVKARVDEVLeLVNLG---DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129442 174 DISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03264 162 DPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211

COG4559

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

32-234

1.14e-26

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 1.14e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmVFQDPLSSLNPR--------------- 96
Cdd:COG4559  17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGE-VR---------LNGRPLAAWSPWelarrravlpqhssl 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  97 ---LPVWRIITEPLwIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARAL-------SSQPDVIVL 166
Cdd:COG4559  87 afpFTVEEVVALGR-APHGSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFL 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 167 DEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

29-239

1.28e-26

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 1.28e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPS---HGQYIRSGS----------QRIMQMVFQDPlsSL 93
Cdd:PRK14247  16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQdifkmdvielRRRVQMVFQIP--NP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   94 NPRLPVWRIITEPL---WIAKRSSE-QQRRALAEELAvqvGIRPEYLDRL--PHA-FSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK14247  94 IPNLSIFENVALGLklnRLVKSKKElQERVRWALEKA---QLWDEVKDRLdaPAGkLSGGQQQRLCIARALAFQPEVLLA 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442  167 DEPTSALDISVQAQILNLLVTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

31-231

2.33e-26

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: 109.06 E-value: 2.33e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVFQDPLSSLN--PRLPVW---RIITE 105
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSLKDIDRHTLRQFINylPQEPYIfsgSILEN 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   106 PLWIAKRSSEQQRRALAEELAvqvGIRPEyLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01193 568 LLLGAKENVSQDEIWAACEIA---EIKDD-IENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNLD 643

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442   175 ISVQAQILNLLVTLQENhglTYVLISHNVSVIRhMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELL 696

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

5-241

3.11e-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: 108.27 E-value: 3.11e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     5 LLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------- 77
Cdd:TIGR02203 330 DVEFRNVTFRYPGRD---------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladyt 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    78 -----------SQRIMqmVFQDPLSSlNprlpvwriiteplwIAKRSSEQQRRALAEElAVQVGIRPEYLDRLPHAF--- 143
Cdd:TIGR02203 401 laslrrqvalvSQDVV--LFNDTIAN-N--------------IAYGRTEQADRAEIER-ALAAAYAQDFVDKLPLGLdtp 462

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   144 --------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAV 215
Cdd:TIGR02203 463 igengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVV 539

                         250       260
                  ....*....|....*....|....*.
gi 16129442   216 MYLGQIVELGDAQQVLTAPAHpYTRL 241
Cdd:TIGR02203 540 MDDGRIVERGTHNELLARNGL-YAQL 564

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

32-227

3.30e-26

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.61 E-value: 3.30e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY-IRSGS-----QRIMQM------------VFQDPlssl 93
Cdd:COG0396  16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-----HPKYeVTSGSilldgEDILELspderaragiflAFQYP---- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  94 nPRLP------VWRIITEplwiAKRSSEQQRRA---LAEELAVQVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSQPDV 163
Cdd:COG0396  87 -VEIPgvsvsnFLRTALN----ARRGEELSAREflkLLKEKMKELGLDEDFLDRyVNEGFSGGEKKRNEILQMLLLEPKL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 164 IVLDEPTSALDI-SVQ--AQILNLLvtLQENHGLtyVLISHNVSVIRHMS-DRVAVMYLGQIVELGDA 227
Cdd:COG0396 162 AILDETDSGLDIdALRivAEGVNKL--RSPDRGI--LIITHYQRILDYIKpDFVHVLVDGRIVKSGGK 225

ABC_Carb_Monos_II

cd03215

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

31-221

4.30e-26

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: 101.74 E-value: 4.30e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmvfqdPLSSLNPRLpvwriiteplWIA 110
Cdd:cd03215  15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK----------PVTRRSPRD----------AIR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 111 KR----SSEQQRRALAEELAVQVGIRpeyldrLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:cd03215  75 AGiayvPEDRKREGLVLDLSVAENIA------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148

                       170       180       190
                ....*....|....*....|....*....|....*
gi 16129442 187 TLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03215 149 ELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182

cbiO

PRK13650

energy-coupling factor transporter ATPase;

32-261

5.95e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 5.95e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMVFQDPLSSLnprlpVWR 101
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirHKIGMVFQNPDNQF-----VGA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 IITEPLWIA---KRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK13650  98 TVEDDVAFGlenKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  179 AQILNLLVTLQENHGLTYVLISHNVSVIRhMSDRVAVMYLGQIVELGDAQQVLTAPAH--------PYTRLLLDSLPAID 250
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQSLRQNG 255

                        250
                 ....*....|.
gi 16129442  251 KPLEEEWALRK 261
Cdd:PRK13650 256 YDLPEGYLTEK 266

PRK13651

cobalt transporter ATP-binding subunit; Provisional

24-231

6.05e-26

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.40 E-value: 6.05e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ---YIRSGSQRIMQMVFQDPLSSLNPRLPVW 100
Cdd:PRK13651  15 KLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEKVLEKLVIQKTRF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEPLWIAKRS------SEQQ-------------------RRALAEELAVQ----VGIRPEYLDRLPHAFSGGQRQRI 151
Cdd:PRK13651  95 KKIKKIKEIRRRVgvvfqfAEYQlfeqtiekdiifgpvsmgvSKEEAKKRAAKyielVGLDESYLQRSPFELSGGQKRRV 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253

MglA

COG1129

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

9-222

8.87e-26

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 8.87e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   9 RDVHINFPARKNWLGKT---TEHV---HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--------YI 74
Cdd:COG1129 239 RELEDLFPKRAAAPGEVvleVEGLsvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEirldgkpvRI 318

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  75 RSGSQRIMQ-MVFqdpLS------SLNPRLPVWRIITEPlWIAKRS-----SEQQRRALAEELAVQVGIRPEYLDRLPHA 142
Cdd:COG1129 319 RSPRDAIRAgIAY---VPedrkgeGLVLDLSIRENITLA-SLDRLSrggllDRRRERALAEEYIKRLRIKTPSPEQPVGN 394

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473

NupO

COG3845

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

3-230

1.61e-25

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 1.61e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHInfparknwlgKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-------YIR 75
Cdd:COG3845 255 EVVLEVENLSV----------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSirldgedITG 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  76 SGSQRIMQM----VFQDPLSS-LNPRLPVW------RIITEPL----WIAKRsseqQRRALAEELAVQVGIRPEYLDRLP 140
Cdd:COG3845 325 LSPRERRRLgvayIPEDRLGRgLVPDMSVAenlilgRYRRPPFsrggFLDRK----AIRAFAEELIEEFDVRTPGPDTPA 400

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGR 479

                       250
                ....*....|
gi 16129442 221 IVELGDAQQV 230
Cdd:COG3845 480 IVGEVPAAEA 489

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

27-203

2.00e-25

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.39 E-value: 2.00e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   27 EHVHAI-NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQM---------------VFQDPL 90
Cdd:PRK10584  20 EHELSIlTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG-QPLHQMdeearaklrakhvgfVFQSFM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   91 ssLNPRLPVWRIITEPLwIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK10584  99 --LIPTLNALENVELPA-LLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174

                        170       180       190
                 ....*....|....*....|....*....|...
gi 16129442  171 SALDISVQAQILNLLVTLQENHGLTYVLISHNV 203
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

9-228

2.11e-25

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 2.11e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   9 RDVHINFPARKNwLGK---TTEHVHA-------INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS 78
Cdd:COG0488 299 KTVEIRFPPPER-LGKkvlELEGLSKsygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGE 376

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 QriMQMVF--QDpLSSLNPRLPVWRIITEplwIAKRSSEQQRRALAEELavqvGIRPEYLDRLPHAFSGGQRQRIAIARA 156
Cdd:COG0488 377 T--VKIGYfdQH-QEELDPDKTVLDELRD---GAPGGTEQEVRGYLGRF----LFSGDDAFKPVGVLSGGEKARLALAKL 446

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442 157 LSSQPDVIVLDEPTSALDI-SVQAqilnLLVTLQENHGlTYVLISHNvsviRHMSDRVAvmylGQIVELGDAQ 228
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHD----RYFLDRVA----TRILEFEDGG 506

cbiO

PRK13645

energy-coupling factor transporter ATPase;

24-232

2.79e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 2.79e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------RSGSQRIMQ---------MVFQD 88
Cdd:PRK13645  19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaiPANLKKIKEvkrlrkeigLVFQF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   89 PLSSLNPRLPVWRIITEPLWIAKRSSEQQRRAlaEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK13645  99 PEYQLFQETIEKDIAFGPVNLGENKQEAYKKV--PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442  169 PTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

31-225

4.45e-25

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 4.45e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI----------RSGSQRIMQMVFQDPLSsLNprlpvw 100
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvtRASLRRNIAVVFQDAGL-FN------ 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEPLWIAKR--SSEQQRRALAEELAVqvgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13657 423 RSIEDNIRVGRPdaTDEEMRAAAERAQAH------DFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILD 496

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  168 EPTSALDISVQAQILNLLVTLQenHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551

ArpD

COG4618

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

32-231

7.06e-25

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: 104.44 E-value: 7.06e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmvfqdPLSSLNPR--------LPvwrii 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS-VRLDGA---------DLSQWDREelgrhigyLP----- 412

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 104 teplwiakrsseqQRRAL-----AE--------------ELAVQVGIRpEYLDRLP-----------HAFSGGQRQRIAI 153
Cdd:COG4618 413 -------------QDVELfdgtiAEniarfgdadpekvvAAAKLAGVH-EMILRLPdgydtrigeggARLSGGQRQRIGL 478

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGDAQQVL 231
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVL 554

cbiO

PRK13640

energy-coupling factor transporter ATPase;

1-225

9.98e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 9.98e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQP---SHGQYIRSG 77
Cdd:PRK13640   1 MKDNIVEFKHVSFTYPDSK---------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 ---SQRIM-------QMVFQDPLSSL--------------N---PRLPVWRIIteplwiakrsseqqRRALAeelavQVG 130
Cdd:PRK13640  72 itlTAKTVwdirekvGIVFQNPDNQFvgatvgddvafgleNravPRPEMIKIV--------------RDVLA-----DVG 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  131 IRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIrHMS 210
Cdd:PRK13640 133 ML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMA 210

                        250
                 ....*....|....*
gi 16129442  211 DRVAVMYLGQIVELG 225
Cdd:PRK13640 211 DQVLVLDDGKLLAQG 225

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

32-242

1.58e-24

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]

Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 103.48 E-value: 1.58e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQR--IMQMVFQDPLSSLNPRL-----PVWRIIT 104
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPReeIPREVLANSVAMVDQDIflfegTVRDNLT 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   105 epLWIAKRSSEQQRRALAE-ELAVQVGIRP-EYLDRLPHA---FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:TIGR03796 575 --LWDPTIPDADLVRACKDaAIHDVITSRPgGYDAELAEGganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442   180 QIL-NLlvtlqENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTAPAhPYTRLL 242
Cdd:TIGR03796 653 IIDdNL-----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVGG-AYARLI 709

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

26-222

1.69e-24

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

Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 1.69e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  26 TEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY----IRSGSQRI-----MQMVFQDPlSSLNPR 96
Cdd:cd03267  31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKkflrrIGVVFGQK-TQLWWD 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  97 LPV---WRIITEPLWIAKRSSEQQRRALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:cd03267 110 LPVidsFYLLAAIYDLPPARFKKRLDELSELLDLE-----ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129442 174 DISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233

urea_trans_UrtE

TIGR03410

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

30-226

1.86e-24

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: 98.75 E-value: 1.86e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIM------------------QMVFqdpls 91
Cdd:TIGR03410  14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGS-IRLDGEDITklppheraragiayvpqgREIF----- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    92 slnPRLPVWRIITEPLWIAKRSSeqqrRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:TIGR03410  88 ---PRLTVEENLLTGLAALPRRS----RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442   172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGD 226
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215

PRK11160

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

5-232

2.21e-24

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.98 E-value: 2.21e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRDVHINFPARknwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------- 77
Cdd:PRK11160 338 SLTLNNVSFTYPDQ---------PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadys 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 -----------SQRIMqmVFQDPLSslnprlpvwriitEPLWIAK-RSSEQQrraLAEELAvQVGIR-----PEYLD--- 137
Cdd:PRK11160 409 eaalrqaisvvSQRVH--LFSATLR-------------DNLLLAApNASDEA---LIEVLQ-QVGLEklledDKGLNawl 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  138 ----RlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRV 213
Cdd:PRK11160 470 geggR---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRI 543

                        250
                 ....*....|....*....
gi 16129442  214 AVMYLGQIVELGDAQQVLT 232
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLA 562

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

31-216

2.78e-24

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: 102.36 E-value: 2.78e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmvfqdPLSSLNPRlpVWR--------- 101
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGV---------PLADADAD--SWRdqiawvpqh 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   102 ------IITEPLWIAKR--SSEQQRRAL-AEELAVQVGIRPEYLDRL----PHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:TIGR02857 405 pflfagTIAENIRLARPdaSDAEIREALeRAGLDEFVAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDE 484

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 16129442   169 PTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVM 216
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALA-DRIVVL 529

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

31-207

2.96e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 2.96e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQdplSSLNPRLP--VWRIITEPLW 108
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR---SEVPDSLPltVRDLVAMGRW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  109 ----IAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:NF040873  84 arrgLWRRLTRDDRAAVDDALE-RVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161

                        170       180
                 ....*....|....*....|...
gi 16129442  185 LVTLQENhGLTYVLISHNVSVIR 207
Cdd:NF040873 162 LAEEHAR-GATVVVVTHDLELVR 183

NHLM_micro_ABC2

TIGR03797

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...

33-234

4.13e-24

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

Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 102.34 E-value: 4.13e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    33 NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrimqmVFQD--PLSSLNPR---------LPVWR 101
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGS------------VFYDgqDLAGLDVQavrrqlgvvLQNGR 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   102 IITEPLWIAKRSSEQQRRALAEELAVQVGIRpEYLDRLP---H--------AFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:TIGR03797 538 LMSGSIFENIAGGAPLTLDEAWEAARMAGLA-EDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEAT 616

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442   171 SALDISVQAQILNLLVTLQenhgLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:TIGR03797 617 SALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

32-233

6.58e-24

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: 101.27 E-value: 6.58e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVFQDplssLNPR---LPvWRIITEPLW 108
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS-VRLDGADLKQWDRET----FGKHigyLP-QDVELFPGT 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   109 IAKRSSEQQRRALAE---ELAVQVGIRpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01842 408 VAENIARFGENADPEkiiEAAKLAGVH-ELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   175 ISVQAQILNLLVTLQEnHGLTYVLISHNVSVIrHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:TIGR01842 487 EEGEQALANAIKALKA-RGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

31-225

6.62e-24

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: 96.79 E-value: 6.62e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI-----------MQMVFQDPL-------SS 92
Cdd:cd03244  19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-ILIDGVDIskiglhdlrsrISIIPQDPVlfsgtirSN 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  93 LNPrlpvwriiteplwIAKRSSEQQRRALAeelavQVGIRpEYLDRLPHA-----------FSGGQRQRIAIARALSSQP 161
Cdd:cd03244  98 LDP-------------FGEYSDEELWQALE-----RVGLK-EFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKS 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 162 DVIVLDEPTSALDISVQAQILNllvTLQEN-HGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:cd03244 159 KILVLDEATASVDPETDALIQK---TIREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219

cbiO

PRK13641

energy-coupling factor transporter ATPase;

35-234

7.58e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.36 E-value: 7.58e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------------RIMQMVFQDPLSSLNPRLPVW 100
Cdd:PRK13641  26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlkklrKKVSLVFQFPEAQLFENTVLK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEPLWIAkrSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:PRK13641 106 DVEFGPKNFG--FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129442  181 ILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:PRK13641 184 MMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

20-246

8.81e-24

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 8.81e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   20 NWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGSQRIMQM---------VFQDpl 90
Cdd:PRK10851   6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG-HIRFHGTDVSRLhardrkvgfVFQH-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   91 SSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELA-----VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:PRK10851  83 YALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTqllemVQLA---HLADRYPAQLSGGQKQRVALARALAVEPQILL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  166 LDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAhpyTRLLLDS 245
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA---TRFVLEF 236


                 .
gi 16129442  246 L 246
Cdd:PRK10851 237 M 237

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

31-203

9.57e-24

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 9.57e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ------MVFQDplSSLNPRLPVWRIIT 104
Cdd:PRK11248  16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGKPVEGpgaergVVFQN--EGLLPWRNVQDNVA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 EPLWIAKRSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:PRK11248  93 FGLQLAGVEKMQ-RLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170

                        170
                 ....*....|....*....
gi 16129442  185 LVTLQENHGLTYVLISHNV 203
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDI 189

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

4-216

9.68e-24

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: 96.73 E-value: 9.68e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   4 TLLTLRDVHINFparknwlgktTEH------VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRS 76
Cdd:COG4778   3 TLLEVENLSKTF----------TLHlqggkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSiLVRH 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  77 GSQRImQMVFQDP-----------------LSSLnPRLPVWRIITEPLwIAKRSSEQQRRALAEELAVQVGIrPEYLDRL 139
Cdd:COG4778  73 DGGWV-DLAQASPreilalrrrtigyvsqfLRVI-PRVSALDVVAEPL-LERGVDREEARARARELLARLNL-PERLWDL 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442 140 PHA-FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:COG4778 149 PPAtFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225

3a01208

TIGR00958

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

5-234

9.82e-24

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.34 E-value: 9.82e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     5 LLTLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQ- 83
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPD--------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VPLVQy 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    84 ----------MVFQDPLSSlnpRLPVWRIITEPLwiaKRSSEQQRRALAEELAVQvgirpEYLDRLPHAF---------- 143
Cdd:TIGR00958 549 dhhylhrqvaLVGQEPVLF---SGSVRENIAYGL---TDTPDEEIMAAAKAANAH-----DFIMEFPNGYdtevgekgsq 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   144 -SGGQRQRIAIARALSSQPDVIVLDEPTSALDisvqAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIV 222
Cdd:TIGR00958 618 lSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692

                         250
                  ....*....|..
gi 16129442   223 ELGDAQQVLTAP 234
Cdd:TIGR00958 693 EMGTHKQLMEDQ 704

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

6-234

1.88e-23

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 1.88e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    6 LTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI----------- 74
Cdd:PRK09536   4 IDVSDLSVEF-------GDTT----VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsa 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   75 RSGSQRIMQmVFQDplSSLNPRLPVWRII----TEPLWIAKRSSEQQRRALAEELAvQVGIrPEYLDRLPHAFSGGQRQR 150
Cdd:PRK09536  73 RAASRRVAS-VPQD--TSLSFEFDVRQVVemgrTPHRSRFDTWTETDRAAVERAME-RTGV-AQFADRPVTSLSGGERQR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226


                 ....
gi 16129442  231 LTAP 234
Cdd:PRK09536 227 LTAD 230

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

28-213

1.92e-23

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.04 E-value: 1.92e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ------------RIMQMVFQDPLSSLNP 95
Cdd:PRK11629  21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaakaelRNQKLGFIYQFHHLLP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   96 RLPVWRIITEPLWIA-KRSSEQQRRALaeELAVQVGIRPEYLDRlPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:PRK11629 101 DFTALENVAMPLLIGkKKPAEINSRAL--EMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16129442  175 ISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRV 213
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216

PhnK

COG1101

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

6-222

3.62e-23

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 3.62e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPArknwlGKTTEhVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM- 84
Cdd:COG1101   2 LELKNLSKTFNP-----GTVNE-KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS-ILIDGKDVTKLp 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  85 ----------VFQDPLSSLNPRLpvwrIITEPLWIA---------KRSSEQQRRALAEELAVQVGIRPEylDRLpHA--- 142
Cdd:COG1101  75 eykrakyigrVFQDPMMGTAPSM----TIEENLALAyrrgkrrglRRGLTKKRRELFRELLATLGLGLE--NRL-DTkvg 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 143 -FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNvsvIRH---MSDRVAVMYL 218
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQaldYGNRLIMMHE 224


                ....
gi 16129442 219 GQIV 222
Cdd:COG1101 225 GRII 228

PRK10908

cell division ATP-binding protein FtsE;

30-222

6.89e-23

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.17 E-value: 6.89e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMVFQDplSSLNPR 96
Cdd:PRK10908  16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflRRQIGMIFQD--HHLLMD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   97 LPVWRIITEPLWIAKRSSEQQRRALAEELAvQVGIrpeyLDR---LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK10908  94 RTVYDNVAIPLIIAGASGDDIRRRVSAALD-KVGL----LDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16129442  174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK10908 169 DDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

27-225

9.92e-23

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: 93.75 E-value: 9.92e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  27 EHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqRIMQMVfqDPLSSLNPRLPVWR--IIT 104
Cdd:cd03220  33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSLL--GLGGGFNPELTGREniYLN 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 105 EPLWIAKRSSEQQRRALAEELAvQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:cd03220 109 GRLLGLSRKEIDEKIDEIIEFS-ELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16129442 185 LVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03220 185 LRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

3-208

1.37e-22

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 1.37e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   3 DTLLTLRDVHINFPArknwlGKTTehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIM 82
Cdd:COG4178 360 DGALALEDLTLRTPD-----GRPL-----LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL 429

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  83 qMVFQDP---LSSLnpRlpvwRIITEPLWIAKRSSEQQRRALAeelavQVGIrPEYLDRL------PHAFSGGQRQRIAI 153
Cdd:COG4178 430 -FLPQRPylpLGTL--R----EALLYPATAEAFSDAELREALE-----AVGL-GHLAERLdeeadwDQVLSLGEQQRLAF 496

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRH 208
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAF 549

oligo_HPY

pfam08352

Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ...

222-287

1.55e-22

Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.

Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 88.61 E-value: 1.55e-22

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442   222 VELGDAQQVLTAPAHPYTRLLLDSLPAIDKPLeEEWALRKTDLPGNRTLPQGCFFYERCPLATHGC 287
Cdd:pfam08352   1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPK-RPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

30-247

1.91e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 1.91e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MVFQDP----LSSln 94
Cdd:PRK13647  19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMGREVNAenekwvrskvgLVFQDPddqvFSS-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   95 prlPVWRIIT-EPLWIAKRSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13647  96 ---TVWDDVAfGPVNMGLDKDEVERRV--EEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  174 DISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGD----------AQQVLTAPA-----HPY 238
Cdd:PRK13647 170 DPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDkslltdedivEQAGLRLPLvaqifEDL 248


                 ....*....
gi 16129442  239 TRLLLDSLP 247
Cdd:PRK13647 249 PELGQSKLP 257

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

32-214

2.19e-22

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: 90.59 E-value: 2.19e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmvfqdplsslnprlpvwriiteplwiak 111
Cdd:cd03221  16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------------------------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 112 rsseqqrralaeelavqvGIRPEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQAqilnLLVTLQE 190
Cdd:cd03221  62 ------------------TVKIGYFEQL----SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALKE 115

                       170       180
                ....*....|....*....|....
gi 16129442 191 NHGlTYVLISHNvsviRHMSDRVA 214
Cdd:cd03221 116 YPG-TVILVSHD----RYFLDQVA 134

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

21-216

2.32e-22

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 92.15 E-value: 2.32e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  21 WLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQR--IMQMVFQDplssl 93
Cdd:cd03250  10 WDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvSQEpwIQNGTIRE----- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  94 NprlpvwrII-TEPLwiakrssEQQR-----RALAeelavqvgIRPEyLDRLPH-----------AFSGGQRQRIAIARA 156
Cdd:cd03250  85 N-------ILfGKPF-------DEERyekviKACA--------LEPD-LEILPDgdlteigekgiNLSGGQKQRISLARA 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 157 LSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVM 216
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

22-230

9.27e-22

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 9.27e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----------SQRIMQMVFQ--- 87
Cdd:PRK09700  11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaAQLGIGIIYQels 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   88 --DPLSSLNpRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEyLDRLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:PRK09700  91 viDELTVLE-NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVII 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  166 LDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:PRK09700 169 MDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232

COG4586

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

19-226

1.14e-21

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 1.14e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  19 KNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-----YI----RSGSQRIMQMVF-QD 88
Cdd:COG4586  25 KGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEvrvlgYVpfkrRKEFARRIGVVFgQR 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  89 plSSLNPRLPVWriitEPLWIAK---RSSEQQRRALAEELAVQVGIRpEYLDR----LphafSGGQRQRIAIARALSSQP 161
Cdd:COG4586 105 --SQLWWDLPAI----DSFRLLKaiyRIPDAEYKKRLDELVELLDLG-ELLDTpvrqL----SLGQRMRCELAAALLHRP 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 162 DVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGD 226
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238

ABC_YhbG

cd03218

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

30-235

1.14e-21

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: 91.07 E-value: 1.14e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVF------------QDPlsSLNPRL 97
Cdd:cd03218  14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK-ILLDGQDITKLPMhkrarlgigylpQEA--SIFRKL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  98 PVWRIITEPLWIAKRSSEQQRR---ALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03218  91 TVEENILAVLEIRGLSKKEREEkleELLEEFHIT-----HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442 175 -ISVQaQILNLLVTLQENhGLTyVLIS-HNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA 235
Cdd:cd03218 166 pIAVQ-DIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225

cbiO

PRK13642

energy-coupling factor transporter ATPase;

29-223

1.19e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 1.19e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMVFQDPLSSLnprlp 98
Cdd:PRK13642  20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrRKIGMVFQNPDNQF----- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITEPLWIAKRSS-----EQQRRALAEELAVQVgirPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13642  95 VGATVEDDVAFGMENQgipreEMIKRVDEALLAVNM---LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129442  174 DISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVE 223
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

5-222

1.58e-21

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.79 E-value: 1.58e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYiRSGSQRIMQM 84
Cdd:PRK10535   4 LLELKDIRRSYPSGE-------EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY-RVAGQDVATL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   85 VfQDPLSSLN--------------PRLPVWRIITEPLWIAKrSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQR 150
Cdd:PRK10535  76 D-ADALAQLRrehfgfifqryhllSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHmSDRVAVMYLGQIV 222
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222

PRK11176

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

31-231

2.81e-21

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 2.81e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------------------SQRIMqmVFQDPLSS 92
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnqvalvSQNVH--LFNDTIAN 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   93 lNprlpvwriiteplwIAKRSSEQQRRALAEElAVQVGIRPEYLDRLPHAF-----------SGGQRQRIAIARALSSQP 161
Cdd:PRK11176 436 -N--------------IAYARTEQYSREQIEE-AARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDS 499

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  162 DVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566

CP_lyasePhnL

TIGR02324

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...

22-213

2.88e-21

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL 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 C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.

Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 89.76 E-value: 2.88e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    22 LGKT-TEHVH------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSG---------SQRIMQM 84
Cdd:TIGR02324   7 LSKTfTLHQQggvrlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRiLVRHEgawvdlaqaSPREVLE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    85 VFQDPLSSLN------PRLPVWRIITEPLwIAKRSSEQQRRALAEELAVQVGIrPEYLDRLPHA-FSGGQRQRIAIARAL 157
Cdd:TIGR02324  87 VRRKTIGYVSqflrviPRVSALEVVAEPL-LERGVPREAARARARELLARLNI-PERLWHLPPAtFSGGEQQRVNIARGF 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442   158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRV 213
Cdd:TIGR02324 165 IADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219

ABC_putative_ATPase

cd03269

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

29-225

2.99e-21

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: 89.65 E-value: 2.99e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQriMQMVFQDPLSSLnPR----LPVWRIIT 104
Cdd:cd03269  13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP--LDIAARNRIGYL-PEerglYPKMKVID 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 105 EPLWIA--KRSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:cd03269  90 QLVYLAqlKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16129442 183 NLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03269 169 DVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

47-239

4.98e-21

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 4.98e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   47 IVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS-----------------QRIMQMVFQDPlsslNP-RLPVWRIITEPLW 108
Cdd:PRK14271  52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDvllggrsifnyrdvlefRRRVGMLFQRP----NPfPMSIMDNVLAGVR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  109 IAKRSSEQQRRALAEELAVQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:PRK14271 127 AHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129442  186 VTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14271 207 RSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

38-215

5.17e-21

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 5.17e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------------QYIRSGSqrimQMVFQDPLSSLNPRL---PVWRI 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelkisykpQYIKPDY----DGTVEDLLRSITDDLgssYYKSE 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  103 ITEPLWIakrsseqqrralaEELavqvgirpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK13409 437 IIKPLQL-------------ERL----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493

                        170       180       190
                 ....*....|....*....|....*....|...
gi 16129442  183 NLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526

PRK11174

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

35-249

6.13e-21

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 6.13e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQyIRSGSQRIMQMVFQDPLSSL-----NPRLPVWRIITEPLWI 109
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGS-LKINGIELRELDPESWRKHLswvgqNPQLPHGTLRDNVLLG 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  110 AKRSSEQQRRALAEELAVQvgirpEYLDRLPH-----------AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK11174 447 NPDASDEQLQQALENAWVS-----EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442  179 AQILNLLvtLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGDAQQVLTAPAhPYTRLLLDSLPAI 249
Cdd:PRK11174 522 QLVMQAL--NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQEEI 588

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

32-240

6.54e-21

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 6.54e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS---------HGQYIRSGS------QRIMQMVFQDP----- 89
Cdd:PRK14258  23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvegrvefFNQNIYERRvnlnrlRRQVSMVHPKPnlfpm 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   90 -----------LSSLNPRLPVWRIITEPLWIAKRSSEQQRRalaeelavqvgIRPEYLDrlphaFSGGQRQRIAIARALS 158
Cdd:PRK14258 103 svydnvaygvkIVGWRPKLEIDDIVESALKDADLWDEIKHK-----------IHKSALD-----LSGGQQQRLCIARALA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  159 SQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMY-----LGQIVELGDAQQVLTA 233
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNS 246


                 ....*..
gi 16129442  234 PAHPYTR 240
Cdd:PRK14258 247 PHDSRTR 253

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

27-231

8.05e-21

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

Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 92.58 E-value: 8.05e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  27 EHVH--------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQ----RIMQMVFQD 88
Cdd:COG5265 361 ENVSfgydperpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTsgriliDGQDIRDVTQaslrAAIGIVPQD 440

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  89 PL---SSL--NprlpvwriiteplwIA---KRSSEQQRRALAEelAVQVGirpEYLDRLPHAF-----------SGGQRQ 149
Cdd:COG5265 441 TVlfnDTIayN--------------IAygrPDASEEEVEAAAR--AAQIH---DFIESLPDGYdtrvgerglklSGGEKQ 501

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQ 229
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAE 578


                ..
gi 16129442 230 VL 231
Cdd:COG5265 579 LL 580

PRK13549

xylose transporter ATP-binding subunit; Provisional

1-235

8.42e-21

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 8.42e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-------------Q 67
Cdd:PRK13549   1 MMEYLLEMKNITKTFGG-----------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgtyegeiifegE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   68 PSHGQYIRSGSQRIMQMVFQDplSSLNPRLPVWRII---TEPLwIAKRSSEQQRRALAEELAVQVGirpeyLDRLPHA-- 142
Cdd:PRK13549  70 ELQASNIRDTERAGIAIIHQE--LALVKELSVLENIflgNEIT-PGGIMDYDAMYLRAQKLLAQLK-----LDINPATpv 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  143 --FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVmylgq 220
Cdd:PRK13549 142 gnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICV----- 215

                        250
                 ....*....|....*
gi 16129442  221 iveLGDAQQVLTAPA 235
Cdd:PRK13549 216 ---IRDGRHIGTRPA 227

PRK09984

phosphonate ABC transporter ATP-binding protein;

22-229

1.57e-20

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 1.57e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ-----PSHGQYIRSGSQRIMQM------------ 84
Cdd:PRK09984  10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLardirksrantg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   85 -VFQDplSSLNPRLPVWRII------TEPLW---IAKRSSEQQRRALaeELAVQVGIRPEYLDRLPhAFSGGQRQRIAIA 154
Cdd:PRK09984  90 yIFQQ--FNLVNRLSVLENVligalgSTPFWrtcFSWFTREQKQRAL--QALTRVGMVHFAHQRVS-TLSGGQQQRVAIA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQ 229
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

35-221

3.21e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 3.21e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI--------RSGSQRIMQMVFQDP----LSSLNPRLPV-WR 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinaLSTAQRLARGLVYLPedrqSSGLYLDAPLaWN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 II-----TEPLWIakrsSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK15439 362 VCalthnRRGFWI----KPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16129442  177 VQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK15439 438 ARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481

fecE

PRK11231

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

32-233

4.77e-20

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 4.77e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmvfqdPLSSLNPR--------LPVWRII 103
Cdd:PRK11231  18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGT-VFLGDK---------PISMLSSRqlarrlalLPQHHLT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  104 TE----------------PLWiAKRSSEQQRRAlaeELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK11231  88 PEgitvrelvaygrspwlSLW-GRLSAEDNARV---NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  168 EPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228

LptB

COG1137

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

32-231

5.71e-20

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 5.71e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM------------------VFQdplssl 93
Cdd:COG1137  19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGR-IFLDGEDITHLpmhkrarlgigylpqeasIFR------ 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  94 npRLPVW---RIITEplwIAKRSSEQQRR---ALAEELAVQvGIRpeylDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:COG1137  92 --KLTVEdniLAVLE---LRKLSKKEREErleELLEEFGIT-HLR----KSKAYSLSGGERRRVEIARALATNPKFILLD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 168 EPTSALD-ISVqAQILNLLVTLQEnHGLTyVLIS-HNV----SVIrhmsDRVAVMYLGQIVELGDAQQVL 231
Cdd:COG1137 162 EPFAGVDpIAV-ADIQKIIRHLKE-RGIG-VLITdHNVretlGIC----DRAYIISEGKVLAEGTPEEIL 224

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

39-215

6.48e-20

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: 86.69 E-value: 6.48e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  39 IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG-------------QYIRSGSqrimQMVFQDPLSSLNPRL---PVWRI 102
Cdd:cd03237  22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldtvsykpQYIKADY----EGTVRDLLSSITKDFythPYFKT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 103 -ITEPLWIakrsseqqrralaEELavqvgirpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:cd03237  98 eIAKPLQI-------------EQI----------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 16129442 182 LNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

24-228

1.09e-19

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: 89.11 E-value: 1.09e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-------------QPSHGQYIRSGSQRIMQMVFQDpl 90
Cdd:TIGR02633   9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRDTERAGIVIIHQE-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    91 SSLNPRLPVWRII------TEPLWIAKRSSEQQRralAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVI 164
Cdd:TIGR02633  87 LTLVPELSVAENIflgneiTLPGGRMAYNAMYLR---AKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442   165 VLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQ 228
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMS 226

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

32-225

1.12e-19

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: 85.79 E-value: 1.12e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqpsHGQYIRSG-------------SQRIMQMVFQDplSSLNPRLP 98
Cdd:cd03234  23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGqilfngqprkpdqFQKCVAYVRQD--DILLPGLT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  99 VWRIIT--EPLWIAKRSSEQQRRALAEelavQVGIRPEYLDRLPHAF----SGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03234  98 VRETLTytAILRLPRKSSDAIRKKRVE----DVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSG 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129442 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

32-231

1.36e-19

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 1.36e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIM-------QMVFQDPLSSLnprlpV 99
Cdd:PRK13638  17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldySKRGLlalrqqvATVFQDPEQQI-----F 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 WRIITEPLWIAKRS-----SEQQRRA-LAEELAVQVGIRPEYLDRLPHafsgGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13638  92 YTDIDSDIAFSLRNlgvpeAEITRRVdEALTLVDAQHFRHQPIQCLSH----GQKKRVAIAGALVLQARYLLLDEPTAGL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  174 DISVQAQILNLL--VTLQENHgltYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK13638 168 DPAGRTQMIAIIrrIVAQGNH---VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

35-238

1.72e-19

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.24 E-value: 1.72e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQI-RRGETlGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS---------------QRIMQMVFQDPlsslnpRL- 97
Cdd:PRK11144  17 VNLTLpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKG-RIVLNGrvlfdaekgiclppeKRRIGYVFQDA------RLf 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   98 PVWRIITEPLWIAKRSSEQQRRALAEELavqvGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK11144  89 PHYKVRGNLRYGMAKSMVAQFDKIVALL----GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  178 QAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPA-HPY 238
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225

YhaQ

COG4152

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

29-270

1.88e-19

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 1.88e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmVFQDPLSS--------------LN 94
Cdd:COG4152  14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VL---------WDGEPLDPedrrrigylpeergLY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  95 PRLPVWRIItepLWIAKR---SSEQQRRAlAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:COG4152  84 PKMKVGEQL---VYLARLkglSKAEAKRR-ADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 172 ALD-ISVQAqILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTapAHPYTRLLLDSLPAID 250
Cdd:COG4152 159 GLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFGRNTLRLEADGDAG 234

                       250       260
                ....*....|....*....|
gi 16129442 251 KpLEEEWALRKTDLPGNRTL 270
Cdd:COG4152 235 W-LRALPGVTVVEEDGDGAE 253

PRK14243

phosphate transporter ATP-binding protein; Provisional

31-240

1.88e-19

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 1.88e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS---------HGQYIRSGS------QRIMQMVFQDPlssl 93
Cdd:PRK14243  25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvegkvtfHGKNLYAPDvdpvevRRRIGMVFQKP---- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   94 NPrLPvwRIITEPLWIAKRSSEQQ--RRALAEELAVQVGIRPEYLDRLPH---AFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK14243 101 NP-FP--KSIYDNIAYGARINGYKgdMDELVERSLRQAALWDEVKDKLKQsglSLSGGQQQRLCIARAIAVQPEVILMDE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  169 PTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVM---------YLGQIVELGDAQQVLTAPAHPYT 239
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255


                 .
gi 16129442  240 R 240
Cdd:PRK14243 256 R 256

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

9-221

1.95e-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: 1.95e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   9 RDVHINFPARKnwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS---------- 78
Cdd:cd03248  15 QNVTFAYPTRP--------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkyl 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  79 QRIMQMVFQDP-LSSlnprlpvwRIITEPLWIAKRSSEQQRralAEELAVQVGIRpEYLDRLPHAF-----------SGG 146
Cdd:cd03248  87 HSKVSLVGQEPvLFA--------RSLQDNIAYGLQSCSFEC---VKEAAQKAHAH-SFISELASGYdtevgekgsqlSGG 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQI 221
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226

livG

PRK11300

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

31-234

5.54e-19

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.27 E-value: 5.54e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQM----VFQdplsslNPRLPV 99
Cdd:PRK11300  20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhieglpGHQIARMgvvrTFQ------HVRLFR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 WRIITEPLWIAK------------------RSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:PRK11300  94 EMTVIENLLVAQhqqlktglfsgllktpafRRAESEALDRAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQP 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442  162 DVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

38-215

9.10e-19

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: 86.38 E-value: 9.10e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------------QYIRSGSQrimqMVFQDPLSSLNPRlpvwrIITE 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlkisykpQYISPDYD----GTVEEFLRSANTD-----DFGS 432

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 106 PLWIakrsseqqrralaEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:COG1245 433 SYYK-------------TEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498

                       170       180       190
                ....*....|....*....|....*....|
gi 16129442 186 VTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISDRLMV 528

sufC

TIGR01978

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...

6-241

9.93e-19

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 83.46 E-value: 9.93e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     6 LTLRDVHINfparknwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY------IRSGSQ 79
Cdd:TIGR01978   1 LKIKDLHVS-----------VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-----HPSYevtsgtILFKGQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    80 RIMQM------------VFQDPLSSlnPRLPVWRIITEPLwIAKRSSEQQ--------RRALAEELAVqVGIRPEYLDR- 138
Cdd:TIGR01978  65 DLLELepderaraglflAFQYPEEI--PGVSNLEFLRSAL-NARRSARGEepldlldfEKLLKEKLAL-LDMDEEFLNRs 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGlTYVLISHNVSVIRHMS-DRVAVMY 217
Cdd:TIGR01978 141 VNEGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKpDYVHVLL 219

                         250       260
                  ....*....|....*....|....
gi 16129442   218 LGQIVELGDAQQVLTAPAHPYTRL 241
Cdd:TIGR01978 220 DGRIVKSGDVELAKELEAKGYDWV 243

PRK10575

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

2-234

1.61e-18

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 1.61e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    2 SDTLLTLRDVHINFParknwlGKTTEHvhainGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRI 81
Cdd:PRK10575   8 SDTTFALRNVSFRVP------GRTLLH-----PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   82 MQM---VFQDPLSSLNPRLPVWRIIT--EPLWIAK--------RSSEQQRRALAEELAVqVGIRPeYLDRLPHAFSGGQR 148
Cdd:PRK10575  76 ESWsskAFARKVAYLPQQLPAAEGMTvrELVAIGRypwhgalgRFGAADREKVEEAISL-VGLKP-LAHRLVDSLSGGER 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQ 228
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233


                 ....*.
gi 16129442  229 QVLTAP 234
Cdd:PRK10575 234 ELMRGE 239

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

32-227

2.18e-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: 81.42 E-value: 2.18e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQyIRSGSQRIMQ------------MVFQDPlsslnPRL 97
Cdd:cd03217  16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGE-ILFKGEDITDlppeerarlgifLAFQYP-----PEI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  98 PvwriiteplwiakrsseqqrralaeelavqvGIR-PEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03217  90 P-------------------------------GVKnADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129442 177 VQAQILNLLVTLQENhGLTYVLISHNVSVIRHM-SDRVAVMYLGQIVELGDA 227
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

32-216

5.26e-18

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: 80.84 E-value: 5.26e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQDPLSSlnpRLPVWRIITEPlWIAK 111
Cdd:cd03290  17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN---RYSVAYAAQKP-WLLN 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 112 RSSE-----------QQRRALAEELAVQVGIrpeylDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:cd03290  93 ATVEenitfgspfnkQRYKAVTDACSLQPDI-----DLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDP 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129442 170 TSALDISVQAQILN--LLVTLQENHgLTYVLISHNVSVIRHmSDRVAVM 216
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAM 214

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

22-231

7.47e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 7.47e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI-----------RSGSQRIMQMVFQDPl 90
Cdd:PRK10895   9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplHARARRGIGYLPQEA- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   91 sSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIrpEYL-DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:PRK10895  88 -SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLrDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442  170 TSALD-ISVqAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK10895 165 FAGVDpISV-IDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225

GguA

NF040905

sugar ABC transporter ATP-binding protein;

24-223

1.07e-17

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 1.07e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmLQPsHGQY---------------IRSGSQR----IMQM 84
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP-HGSYegeilfdgevcrfkdIRDSEALgiviIHQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   85 VFQDPLSSlnprlpvwriITEPLWIakrSSEQQRRAL---------AEELAVQVGirpeyLDRLPHAFSG----GQRQRI 151
Cdd:NF040905  87 LALIPYLS----------IAENIFL---GNERAKRGVidwnetnrrARELLAKVG-----LDESPDTLVTdigvGKQQLV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129442  152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

2-211

1.18e-17

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 1.18e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    2 SDTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--- 78
Cdd:PRK10247   4 NSPLLQLQNVGYLAGDAK-----------ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdis 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   79 ----QRIMQMV---FQDPlsSL-------NPRLPvWRIiteplwiakRSSEQQRRALAEELAvQVGIRPEYLDRLPHAFS 144
Cdd:PRK10247  73 tlkpEIYRQQVsycAQTP--TLfgdtvydNLIFP-WQI---------RNQQPDPAIFLDDLE-RFALPDTILTKNIAELS 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  145 GGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSD 211
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADK 206

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

35-244

1.31e-17

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 1.31e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------------SQRIMQMVFQDplSSLNPRLPVWR 101
Cdd:PRK11831  26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytVRKRMSMLFQS--GALFTDMNVFD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 IITEPLWIAKRSSEQQRRALAEELAVQVGIRPEyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442  182 LNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQvLTAPAHPYTRLLLD 244
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRVRQFLD 244

oligo_HPY

TIGR01727

oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ...

220-305

1.69e-17

oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 75.86 E-value: 1.69e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   220 QIVELGDAQQVLTAPAHPYTRLLLDSLPAIDKPLEeewalRKTDLPGN----RTLPQGCFFYERCPLATHGCEVRQSLAI 295
Cdd:TIGR01727   1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDR-----KLISIPGEvpslINLPSGCRFYPRCPYAQDECRKEPPALV 75

                          90
                  ....*....|.
gi 16129442   296 R-EDGRELRCW 305
Cdd:TIGR01727  76 EiAEGHRVACH 86

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

32-231

1.71e-17

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

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 83.07 E-value: 1.71e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIM--QMVFQDplSSLNPRLPVWRIITEPLWi 109
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVpqQAWIQN--DSLRENILFGKALNEKYY- 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    110 akRSSEQQRRALAEELAVQVGIRPEYLDRLPHaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL-NLLVTL 188
Cdd:TIGR00957  731 --QQVLEACALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPE 807

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 16129442    189 QENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGDAQQVL 231
Cdd:TIGR00957  808 GVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

35-201

1.99e-17

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).

Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.96 E-value: 1.99e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMqMVFQDPLsslnprLPVWRiiteplwiakrss 114
Cdd:cd03223  20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL-FLPQRPY------LPLGT------------- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 115 eqqrraLAEELavqvgIRPEYldrlpHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtlqENHGL 194
Cdd:cd03223  80 ------LREQL-----IYPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGI 139


                ....*..
gi 16129442 195 TYVLISH 201
Cdd:cd03223 140 TVISVGH 146

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

22-217

2.15e-17

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: 80.10 E-value: 2.15e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  22 LGKTTEHVHAINGIDLQ----IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrimqmvFQDPlsslnprl 97
Cdd:cd03236   2 LEDEPVHRYGPNSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-------------FDDP-------- 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  98 PVWRIITEplwiAKRSSEQQR--RALAEElAVQVGIRPEYLDRLPHAF-------------------------------- 143
Cdd:cd03236  61 PDWDEILD----EFRGSELQNyfTKLLEG-DVKVIVKPQYVDLIPKAVkgkvgellkkkdergkldelvdqlelrhvldr 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 144 -----SGGQRQRIAIARALSSQPDVIVLDEPTSALDISvqaQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03236 136 nidqlSGGELQRVAIAAALARDADFYFFDEPSSYLDIK---QRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCL 212


                .
gi 16129442 217 Y 217
Cdd:cd03236 213 Y 213

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

4-213

2.73e-17

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 2.73e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    4 TLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQ 83
Cdd:PRK09544   3 SLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI-G 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   84 MVFQDplSSLNPRLPvwriITEPLWIAKRSSEQQRRALAEELAVQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDV 163
Cdd:PRK09544  71 YVPQK--LYLDTTLP----LTVNRFLRLRPGTKKEDILPALKRVQAG---HLIDAPMQKLSGGETQRVLLARALLNRPQL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129442  164 IVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRV 213
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191

PRK10790

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

35-233

3.20e-17

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 3.20e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIR-------SGSQRIMQ----MVFQDPL---SSLNPRLPVW 100
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE-IRldgrplsSLSHSVLRqgvaMVQQDPVvlaDTFLANVTLG 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEP-LWIAKRSSE--QQRRALAEELAVQVGirpEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK10790 439 RDISEEqVWQALETVQlaELARSLPDGLYTPLG---EQGNNL----SVGQKQLLALARVLVQTPQILILDEATANIDSGT 511

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  178 QAQILNLLVTLQENhgLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK10790 512 EQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564

anch_rpt_ABC

TIGR03771

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...

37-233

4.51e-17

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

Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 78.35 E-value: 4.51e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    37 LQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRiMQMVFQDPLSS----LNPRlpv 99
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAspgkgwrhigyvpQR-HEFAWDFPISVahtvMSGR--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   100 wriiTEPLWIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:TIGR03771  77 ----TGHIGWLRRPCVADFAAVRDALR-RVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16129442   180 QILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVaVMYLGQIVELGDAQQVLTA 233
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDP 202

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

35-233

4.53e-17

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 4.53e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMVFQDPLS----SLNPRLPVW 100
Cdd:PRK10253  26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevaRRIGLLAQNATTpgdiTVQELVARG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTL----SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129442  181 ILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

31-225

6.07e-17

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: 77.84 E-value: 6.07e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMvfqdPLSSLNPRLPVwrIITEPLWIA 110
Cdd:cd03369  23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGK-IEIDGIDISTI----PLEDLRSSLTI--IPQDPTLFS 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 111 K--RSS-----EQQRRALAEELAVQVGirpeyldrlPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILN 183
Cdd:cd03369  96 GtiRSNldpfdEYSDEEIYGALRVSEG---------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16129442 184 llVTLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:cd03369 167 --TIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205

BtuD

COG4138

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

34-233

8.75e-17

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 8.75e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQYIRSGsqrimqmvfqDPLSSLNPR----------------- 96
Cdd:COG4138  14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNG----------RPLSDWSAAelarhraylsqqqsppf 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  97 -LPVWRIITepLWIAKRSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARAL-------SSQPDVIVLDE 168
Cdd:COG4138  83 aMPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 169 PTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP 223

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

12-225

1.48e-16

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: 76.44 E-value: 1.48e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  12 HINFPARKNWLGKTTEHVHAINGIdlqIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH--GQYIRSGSQ-------RIM 82
Cdd:cd03213   8 NLTVTVKSSPSKSGKQLLKNVSGK---AKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPldkrsfrKII 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  83 QMVFQDplSSLNPRLPVWriitEPLWIAkrsseqqrralaeelAVQVGIrpeyldrlphafSGGQRQRIAIARALSSQPD 162
Cdd:cd03213  85 GYVPQD--DILHPTLTVR----ETLMFA---------------AKLRGL------------SGGERKRVSIALELVSNPS 131

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442 163 VIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVS-VIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

23-223

1.84e-16

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.84e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   23 GKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimQMVFQDPLSSLN-------- 94
Cdd:PRK11288  11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQ---EMRFASTTAALAagvaiiyq 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   95 -----PRLPVwriiTEPLWIAK---RSSEQQRRALAEELAvqvgirpEYLDRL-----PHA----FSGGQRQRIAIARAL 157
Cdd:PRK11288  87 elhlvPEMTV----AENLYLGQlphKGGIVNRRLLNYEAR-------EQLEHLgvdidPDTplkyLSIGQRQMVEIAKAL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  158 SSQPDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLTYVliSHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYV--SHRMEEIFALCDAITVFKDGRYVA 220

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

22-230

2.17e-16

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.46 E-value: 2.17e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQYI-----------------------RS 76
Cdd:TIGR03269   6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpVC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    77 GSQRIMQMV-FQDPLSSLNPRLPVWRII----TEPLWIAKRSSEQQRRALAE-----ELAVQVGIrpEYLD------RLP 140
Cdd:TIGR03269  86 GGTLEPEEVdFWNLSDKLRRRIRKRIAImlqrTFALYGDDTVLDNVLEALEEigyegKEAVGRAV--DLIEmvqlshRIT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   141 HA---FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:TIGR03269 164 HIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243

                         250
                  ....*....|...
gi 16129442   218 LGQIVELGDAQQV 230
Cdd:TIGR03269 244 NGEIKEEGTPDEV 256

AAA

smart00382

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

41-219

2.64e-16

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 74.33 E-value: 2.64e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     41 RGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQDplsslnprlpvwriiteplwiakrsseqqrra 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    121 laeelavqvgIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT-----LQENHGLT 195
Cdd:smart00382  49 ----------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSEKNLT 118

                          170       180
                   ....*....|....*....|....*....
gi 16129442    196 YVLISHNVSV-----IRHMSDRVAVMYLG 219
Cdd:smart00382 119 VILTTNDEKDlgpalLRRRFDRRIVLLLI 147

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

36-231

3.05e-16

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.90 E-value: 3.05e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYiRSGSQRIMQMVFQ---------------DPLSSL--NPRLP 98
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-QSQFSHITRLSFEqlqklvsdewqrnntDMLSPGedDTGRT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   99 VWRIITEplwiakrssEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK10938 102 TAEIIQD---------EVKDPARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129442  179 AQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK10938 172 QQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223

PRK10762

D-ribose transporter ATP binding protein; Provisional

32-221

1.53e-15

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.53e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ----------------------YI---RSGSQRIMQMVF 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYvtldghevvtrspqdglangivYIsedRKRDGLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   87 QDPLSslnprLPVWRIITEPLWIAKRSSEQQrraLAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK10762 348 KENMS-----LTALRYFSRAGGSLKHADEQQ---AVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  167 DEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473

PRK15056

manganese/iron ABC transporter ATP-binding protein;

31-233

2.03e-15

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 2.03e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVFQDPLSSLNPRLPV-WR--IITEPL 107
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK-ISILGQPTRQALQKNLVAYVPQSEEVdWSfpVLVEDV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  108 ----------WIaKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK15056 101 vmmgryghmgWL-RRAKKRDRQIVTAALA-RVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442  178 QAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDrVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK15056 178 EARIISLLRELRD-EGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231

PRK10789

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

31-234

6.40e-15

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 6.40e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmvFQD-PLSSLnpRLPVWR-------- 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IR----------FHDiPLTKL--QLDSWRsrlavvsq 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 -------IITEPLWIAKRSSEQQRralAEELAVQVGIRPEYLdRLPHAF-----------SGGQRQRIAIARALSSQPDV 163
Cdd:PRK10789 397 tpflfsdTVANNIALGRPDATQQE---IEHVARLASVHDDIL-RLPQGYdtevgergvmlSGGQKQRISIARALLLNAEI 472

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129442  164 IVLDEPTSALDISVQAQILNLLVtlQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

34-185

8.12e-15

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: 71.62 E-value: 8.12e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------QRIMQMVFQDPLSSLNPRLPVWriitEP 106
Cdd:TIGR01189  18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdEPHENILYLGHLPGLKPELSAL----EN 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   107 LWIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:TIGR01189  94 LHFWAAIHGGAQRTIEDALA-AVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

25-221

8.15e-15

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.48 E-value: 8.15e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    25 TTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG---------MLQPSHGQYIRSGSQRIMQ---MVFQD-PLS 91
Cdd:TIGR02633 269 INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnVFINGKPVDIRNPAQAIRAgiaMVPEDrKRH 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    92 SLNPRLPVWRIITepLWIAKRSSEQQR-RALAEELAVQVGIRPEYLdRLPHAF------SGGQRQRIAIARALSSQPDVI 164
Cdd:TIGR02633 349 GIVPILGVGKNIT--LSVLKSFCFKMRiDAAAELQIIGSAIQRLKV-KTASPFlpigrlSGGNQQKAVLAKMLLTNPRVL 425

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442   165 VLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481

livF

PRK11614

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

29-233

8.68e-15

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 8.68e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQMvfqdplsslnprlPVWRIITEPLW 108
Cdd:PRK11614  18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-KDITDW-------------QTAKIMREAVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  109 IAKRSSEQQRRALAEELAVQVGI---RPEYLDRLPHAF-----------------SGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK11614  84 IVPEGRRVFSRMTVEENLAMGGFfaeRDQFQERIKWVYelfprlherriqragtmSGGEQQMLAIGRALMSQPRLLLLDE 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  169 PTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVeLGDAQQVLTA 233
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV-LEDTGDALLA 226

PLN03211

ABC transporter G-25; Provisional

24-231

1.00e-14

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 1.00e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH--GQYI---RSGSQRIMQ---MVFQDPLssLNP 95
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILannRKPTKQILKrtgFVTQDDI--LYP 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   96 RLPVWR--IITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAF----SGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:PLN03211 154 HLTVREtlVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEP 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442  170 TSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSV-IRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAM 295

PRK13549

xylose transporter ATP-binding subunit; Provisional

28-221

1.02e-14

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQpshGQY------------IRSGSQRIMQ---MVFQD-PLS 91
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRWegeifidgkpvkIRNPQQAIAQgiaMVPEDrKRD 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   92 SLNPRLPVWRIITepLWIAKRSSEQQRRALAEELAVqvgIRpEYLDRL----PHAF------SGGQRQRIAIARALSSQP 161
Cdd:PRK13549 351 GIVPVMGVGKNIT--LAALDRFTGGSRIDDAAELKT---IL-ESIQRLkvktASPElaiarlSGGNQQKAVLAKCLLLNP 424

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  162 DVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

32-233

1.07e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 1.07e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGSQRIMQMVFQDP-LSSLNPRLPVwriiT 104
Cdd:PRK13537  23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgEPVPSRARHARQRVGVVPqFDNLDPDFTV----R 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 EPLWIAKRS---SEQQRRALAEELaVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:PRK13537  99 ENLLVFGRYfglSAAAARALVPPL-LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16129442  182 LNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTA 233
Cdd:PRK13537 178 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228

CeuD

COG4604

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

32-234

1.49e-14

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.04 E-value: 1.49e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQ-----------RIMQMVFQDPlsSLNPRLPV- 99
Cdd:COG4604  17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGE-VLVDGLdvattpsrelaKRLAILRQEN--HINSRLTVr 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 -------------------WRIITEplwiakrsseqqrrALAE-ELAvqvGIRPEYLDRLphafSGGQRQRIAIARALSS 159
Cdd:COG4604  94 elvafgrfpyskgrltaedREIIDE--------------AIAYlDLE---DLADRYLDEL----SGGQRQRAFIAMVLAQ 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129442 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227

ycf16

CHL00131

sulfate ABC transporter protein; Validated

1-227

2.06e-14

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 2.06e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    1 MSDTLLTLRDVHINFparknwlgKTTEhvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY-IRSG-- 77
Cdd:CHL00131   3 KNKPILEIKNLHASV--------NENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-----HPAYkILEGdi 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 ---------------SQRIMQMVFQDP------------------------LSSLNPrLPVWRIITEPLWIakrsseqqr 118
Cdd:CHL00131  67 lfkgesildlepeerAHLGIFLAFQYPieipgvsnadflrlaynskrkfqgLPELDP-LEFLEIINEKLKL--------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  119 ralaeelavqVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI---LNLLVTLQEnhgl 194
Cdd:CHL00131 137 ----------VGMDPSFLSRnVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSEN---- 202

                        250       260       270
                 ....*....|....*....|....*....|....
gi 16129442  195 TYVLISHNVSVIRHMS-DRVAVMYLGQIVELGDA 227
Cdd:CHL00131 203 SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

21-232

2.73e-14

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.00 E-value: 2.73e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   21 WLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVfqdplSSLNPRLPVW 100
Cdd:PRK13545  29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS-----SGLNGQLTGI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  101 RIITEPLWIAKRSSEQQRRALAE--ELAvQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIKEIIPEiiEFA-DIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129442  179 AQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK13545 180 KKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

13-217

4.31e-14

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 4.31e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   13 INFPARknwLGKTTEHVHAINGIDL----QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY---------IR--SG 77
Cdd:PRK13409  69 VNLPEE---LEEEPVHRYGVNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevLKrfRG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   78 SQriMQMVFQDpLSSLNPR----------LP------VWRIIteplwiaKRSSEqqrRALAEELAVQVGIRPeYLDRLPH 141
Cdd:PRK13409 146 TE--LQNYFKK-LYNGEIKvvhkpqyvdlIPkvfkgkVRELL-------KKVDE---RGKLDEVVERLGLEN-ILDRDIS 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHgltYVL-ISHNVSVIRHMSDRVAVMY 217
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK---YVLvVEHDLAVLDYLADNVHIAY 285

PRK10762

D-ribose transporter ATP binding protein; Provisional

4-223

6.79e-14

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 6.79e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    4 TLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRimq 83
Cdd:PRK10762   3 ALLQLKGIDKAFPG-----------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   84 mVFQDPLSS-----------LN--PRLPVWRII---TEPLWIAKRSSEQQRRALAEELAVQVGIRPEYlDRLPHAFSGGQ 147
Cdd:PRK10762  69 -TFNGPKSSqeagigiihqeLNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQ-ENHGLTYvlISHNVSVIRHMSDRVAVMYLGQ-IVE 223
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVY--ISHRLKEIFEICDDVTVFRDGQfIAE 222

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

13-217

1.43e-13

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: 70.97 E-value: 1.43e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  13 INFPARknwLGKTTEHVHAINGIDL----QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-----QRIMQ 83
Cdd:COG1245  69 VNLPEE---LEEDPVHRYGENGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlKRFRG 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  84 MVFQDPLSSL-NPRLpvwRIITEPLWIA--------------KRSSEqqrRALAEELAVQVGIRPeYLDRLPHAFSGGQR 148
Cdd:COG1245 146 TELQDYFKKLaNGEI---KVAHKPQYVDlipkvfkgtvrellEKVDE---RGKLDELAEKLGLEN-ILDRDISELSGGEL 218

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVL-ISHNVSVIRHMSDRVAVMY 217
Cdd:COG1245 219 QRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG--KYVLvVEHDLAILDYLADYVHILY 286

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

29-213

1.64e-13

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: 67.35 E-value: 1.64e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQllmgmlqpsHGQYiRSGSQRIMQmvfqdpLSSLNPRLPVWRIiteplw 108
Cdd:cd03238   8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLY-ASGKARLIS------FLPKFSRNKLIFI------ 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 109 iakrsseQQRRALaeelaVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL--SSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:cd03238  66 -------DQLQFL-----IDVGLGYLTLGQKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIK 133

                       170       180
                ....*....|....*....|....*..
gi 16129442 187 TLQENhGLTYVLISHNVSVIRHmSDRV 213
Cdd:cd03238 134 GLIDL-GNTVILIEHNLDVLSS-ADWI 158

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

5-268

1.99e-13

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 1.99e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    5 LLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI--- 81
Cdd:PRK15439  11 LLCARSISKQYSG-----------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-LEIGGNPCarl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   82 ---------MQMVFQDPLssLNPRLPVWRIITepLWIAKRSSEQQR-RALAEELAVQVGirpeyLDRLPHAFSGGQRQRI 151
Cdd:PRK15439  79 tpakahqlgIYLVPQEPL--LFPNLSVKENIL--FGLPKRQASMQKmKQLLAALGCQLD-----LDSSAGSLEVADRQIV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  152 AIARALSSQPDVIVLDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQIvelgdaqq 229
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTI-------- 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 16129442  230 VLTAPAHPYTRlllDSLPAIDKPLEEEWALRKT-----DLPGNR 268
Cdd:PRK15439 219 ALSGKTADLST---DDIIQAITPAAREKSLSASqklwlELPGNR 259

PTZ00265

multidrug resistance protein (mdr1); Provisional

6-208

2.88e-13

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 2.88e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     6 LTLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRI---- 81
Cdd:PTZ00265  383 IQFKNVRFHYDTRKD--------VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkdin 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    82 -------MQMVFQDPL-----------------------------------SSLNPRLPVWRIITEPLWIAKRSSE---- 115
Cdd:PTZ00265  455 lkwwrskIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLNDMSNTTDsnel 534

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   116 ----QQRRALAEELAVQVGIR---PEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PTZ00265  535 iemrKNYQTIKDSEVVDVSKKvliHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614

                         250       260       270
                  ....*....|....*....|....*....|.
gi 16129442   178 QAQILNLLVTLQENHGLTYVLISHNVSVIRH 208
Cdd:PTZ00265  615 EYLVQKTINNLKGNENRITIIIAHRLSTIRY 645

PLN03073

ABC transporter F family; Provisional

34-186

3.49e-13

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 69.89 E-value: 3.49e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   34 GIDLQIRrgetLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMqmVFQ----DPLS-SLNPRLPVWRIITEPLw 108
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA--VFSqhhvDGLDlSSNPLLYMMRCFPGVP- 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  109 iakrssEQQRRALAEELAV--QVGIRPEYldrlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQAQILNLL 185
Cdd:PLN03073 604 ------EQKLRAHLGSFGVtgNLALQPMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV 671


                 .
gi 16129442  186 V 186
Cdd:PLN03073 672 L 672

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

35-228

4.56e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 4.56e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRImqmVFQDPLSS------LNPR-------LPVwR 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQ-VYLDGKPI---DIRSPRDAiragimLCPEdrkaegiIPV-H 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 IITEPLWIAKRS---------SEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK11288 347 SVADNINISARRhhlragcliNNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  173 LDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV-ELGDAQ 228
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAgELAREQ 482

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

34-185

4.81e-13

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: 66.75 E-value: 4.81e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQ-------MVFQDPLSSLNPRLPVWRIITep 106
Cdd:cd03231  18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdsiargLLYLGHAPGIKTTLSVLENLR-- 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442 107 LWIAKRSSEQQRRALAeelavQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:cd03231  96 FWHADHSDEQVEEALA-----RVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

39-217

5.57e-13

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: 66.06 E-value: 5.57e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  39 IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqyirsgsqrimqmvfqdplsslNPRLPVWRIIteplwiakrsseqqr 118
Cdd:cd03222  22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD----------------------NDEWDGITPV--------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 119 ralaeelavqvgIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVL 198
Cdd:cd03222  65 ------------YKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127

                       170
                ....*....|....*....
gi 16129442 199 ISHNVSVIRHMSDRVAVMY 217
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVFE 146

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

35-182

5.90e-13

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

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.55 E-value: 5.90e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqRImqmvfqdplsSLNPRLPvWRI---ITEPLWIAK 111
Cdd:TIGR01271  445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RI----------SFSPQTS-WIMpgtIKDNIIFGL 511

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442    112 RSSEQQRRAL--AEELAVQVGIRPEYlDRLPH-----AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:TIGR01271  512 SYDEYRYTSVikACQLEEDIALFPEK-DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

35-220

9.58e-13

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.

Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.19 E-value: 9.58e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimQMVFQDPLSSLNPrlpvwRIITEPLWIAKRSS 114
Cdd:cd03291  56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSWIMP-----GTIKENIIFGVSYD 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 115 EQQRRALAEELAVQVGIR--PEYlDRLPHA-----FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV- 186
Cdd:cd03291 126 EYRYKSVVKACQLEEDITkfPEK-DNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVc 204

                       170       180       190
                ....*....|....*....|....*....|....
gi 16129442 187 TLQENHglTYVLISHNVSVIRhMSDRVAVMYLGQ 220
Cdd:cd03291 205 KLMANK--TRILVTSKMEHLK-KADKILILHEGS 235

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

34-185

1.23e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.23e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM---VFQDPL-----SSLNPRLPVWriitE 105
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRRQrdeYHQDLLylghqPGIKTELTAL----E 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  106 PL-WIAKRSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:PRK13538  94 NLrFYQRLHGPGDDEALWEALA-QVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171


                 .
gi 16129442  185 L 185
Cdd:PRK13538 172 L 172

3a01204

TIGR00955

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

6-229

1.25e-12

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 1.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     6 LTLRDVHINFPARKNWLGKTTEHVhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLM-----GML-QPS---HGQYI-R 75
Cdd:TIGR00955  17 DGSWKQLVSRLRGCFCRERPRKHL--LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKgSGSvllNGMPIdA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    76 SGSQRIMQMVFQDPLssLNPRLPVWR--IITEPLWIAKRSSEQQRRALAEELAVQVGIR---------PEYLDRLphafS 144
Cdd:TIGR00955  95 KEMRAISAYVQQDDL--FIPTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcantrigvPGRVKGL----S 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   145 GGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSV-IRHMSDRVAVMYLGQIVE 223
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSeLFELFDKIILMAEGRVAY 247


                  ....*.
gi 16129442   224 LGDAQQ 229
Cdd:TIGR00955 248 LGSPDQ 253

PRK11147

ABC transporter ATPase component; Reviewed

38-201

1.28e-12

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 1.28e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmvfqdplsslnprlpvwriitepLWIAkrSSEQQ 117
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHCGTK---------------------------LEVA--YFDQH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  118 RRALAEE------LA-----VQVGIRPE----YL-DRLPH---------AFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK11147 391 RAELDPEktvmdnLAegkqeVMVNGRPRhvlgYLqDFLFHpkramtpvkALSGGERNRLLLARLFLKPSNLLILDEPTND 470

                        170       180
                 ....*....|....*....|....*....
gi 16129442  173 LDIsvqaQILNLLVTLQENHGLTYVLISH 201
Cdd:PRK11147 471 LDV----ETLELLEELLDSYQGTVLLVSH 495

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

32-214

1.42e-12

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: 67.65 E-value: 1.42e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMVFQDPlSSLNPRLPVWRIITEPLWIAK 111
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETVKLAYVDQSR-DALDPNKTVWEEISGGLDIIK 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   112 -----------------RSSEQQRRalaeelavqVGIrpeyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR03719 416 lgkreipsrayvgrfnfKGSDQQKK---------VGQ-----------LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 16129442   175 IsvqaqilNLLVTLQE---NHGLTYVLISHNvsviRHMSDRVA 214
Cdd:TIGR03719 476 V-------ETLRALEEallNFAGCAVVISHD----RWFLDRIA 507

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

34-185

1.73e-12

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 1.73e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMVFQDPLSSLNPRLPVWRIITepLW 108
Cdd:PRK13539  20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddPDVAEACHYLGHRNAMKPALTVAENLE--FW 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  109 IAKRSseqQRRALAEELAVQVGIRPeyLDRLPHAF-SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:PRK13539  98 AAFLG---GEELDIAAALEAVGLAP--LAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

35-233

2.19e-12

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.66 E-value: 2.19e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMVFQDPLSSLN--PRLPVW-----RIITEPL 107
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN-IAKIGLHDLRFKITiiPQDPVLfsgslRMNLDPF 1383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    108 wiAKRSSEQQRRALaeELAVQVGIRPEYLDRLPHA-------FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:TIGR00957 1384 --SQYSDEEVWWAL--ELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1459

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16129442    181 ILNLLVTLQENhgLTYVLISHNVSVIRHMSdRVAVMYLGQIVELGDAQQVLTA 233
Cdd:TIGR00957 1460 IQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

6-235

2.61e-12

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 2.61e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    6 LTLRDVHINFPARKnwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmv 85
Cdd:PRK10522 323 LELRNVTFAYQDNG----------FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------- 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   86 fqdPLSSLNPRlpVWR-----IITEpLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHA--------FSGGQRQRIA 152
Cdd:PRK10522 386 ---PVTAEQPE--DYRklfsaVFTD-FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEdgrisnlkLSKGQKKRLA 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIrHMSDRVAVMYLGQIVEL-GDAQQVL 231
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSELtGEERDAA 538


                 ....
gi 16129442  232 TAPA 235
Cdd:PRK10522 539 SRDA 542

PRK03695

vitamin B12-transporter ATPase; Provisional

38-234

2.96e-12

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 2.96e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   38 QIRRGETLGIVGESGCGKSTLAQLLMGMLqPShgqyirSGSQRIMQMVFQD-PLSSLNPR-------------LPVWRII 103
Cdd:PRK03695  18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PG------SGSIQFAGQPLEAwSAAELARHraylsqqqtppfaMPVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  104 TepLWIAKRSSEQQRRALAEELAVQVGIRPEyLDRLPHAFSGG--QRQRIA-----IARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK03695  91 T--LHQPDKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSLDVA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  177 VQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAP 234
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

32-223

3.05e-12

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 3.05e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY----------IRSGSQRImQMVFQdpLSSLNPRLPVwr 101
Cdd:PRK13536  57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARI-GVVPQ--FDNLDLEFTV-- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 iiTEPLWIAKRSSEQQRRALAEelavqvgIRPEYLD--RLPHA-------FSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK13536 132 --RENLLVFGRYFGMSTREIEA-------VIPSLLEfaRLESKadarvsdLSGGMKRRLTLARALINDPQLLILDEPTTG 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16129442  173 LDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLG-QIVE 223
Cdd:PRK13536 203 LDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253

PLN03232

ABC transporter C family member; Provisional

32-248

3.25e-12

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 3.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMVFQDP-LSSLNPRLPVw 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfgltdlRRVLSIIPQSPvLFSGTVRFNI- 1330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   101 riitEPLwiakrsSEQQRRALAEelAVQVGIRPEYLDRLP-----------HAFSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:PLN03232 1331 ----DPF------SEHNDADLWE--ALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEA 1398

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   170 TSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDSLPA 248
Cdd:PLN03232 1399 TASVDVRTDSLIQRTI--REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474

PRK15064

ABC transporter ATP-binding protein; Provisional

46-211

5.85e-12

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 5.85e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   46 GIVGESGCGKSTLAQLLMGMLQPSHGQY-----IRSGSQRIMQMVFQDplsslnprlpvWRIIT------EPLWIAKrsS 114
Cdd:PRK15064  31 GLIGANGCGKSTFMKILGGDLEPSAGNVsldpnERLGKLRQDQFAFEE-----------FTVLDtvimghTELWEVK--Q 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  115 EQQR-RALAE-----------------------------ELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVI 164
Cdd:PRK15064  98 ERDRiYALPEmseedgmkvadlevkfaemdgytaearagELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDIL 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  165 VLDEPTSALDISV---QAQILNllvtlqeNHGLTYVLISH-----NvSVIRHMSD 211
Cdd:PRK15064 178 LLDEPTNNLDINTirwLEDVLN-------ERNSTMIIISHdrhflN-SVCTHMAD 224

PLN03232

ABC transporter C family member; Provisional

20-225

7.59e-12

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 7.59e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    20 NWLGKTTEHvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHgqyirSGSQRIMQMVFQDPLSSLNPRLPV 99
Cdd:PLN03232  623 SWDSKTSKP--TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----TSSVVIRGSVAYVPQVSWIFNATV 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   100 WRIItepLWIAKRSSEQQRRALaEELAVQvgirpEYLDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PLN03232  696 RENI---LFGSDFESERYWRAI-DVTALQ-----HDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDD 766

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442   169 PTSALDISVQAQILNLLVTlQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:PLN03232  767 PLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821

PTZ00265

multidrug resistance protein (mdr1); Provisional

134-215

7.99e-12

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 7.99e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   134 EYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN 202
Cdd:PTZ00265 1339 EFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418

                          90
                  ....*....|...
gi 16129442   203 VSVIRHmSDRVAV 215
Cdd:PTZ00265 1419 IASIKR-SDKIVV 1430

PRK11147

ABC transporter ATPase component; Reviewed

36-233

1.28e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 1.28e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   36 DLQIRRGETLGIVGESGCGKSTLAQLLMG------------------MLQ---PSHGQ-----YIRSGSQ---------- 79
Cdd:PRK11147  23 ELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivaRLQqdpPRNVEgtvydFVAEGIEeqaeylkryh 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   80 RIMQMVFQDPLSSLNPRLPVWRIITE--PLWiakrsseqQRRALAEELAVQVGIRPeylDRLPHAFSGGQRQRIAIARAL 157
Cdd:PRK11147 103 DISHLVETDPSEKNLNELAKLQEQLDhhNLW--------QLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRAL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhglTYVLISHNVSVIRHMSDRVAVMYLGQIVEL-GDAQQVLTA 233
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLVSYpGNYDQYLLE 244

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

8-231

1.43e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.43e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    8 LRDVHInfPARKNwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVfq 87
Cdd:PRK13546  24 MKDALI--PKHKN------KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   88 dplSSLNPRLPVWRIItEPLWIAKRSSEQQRRALAEELaVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13546  94 ---AGLSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKI-IEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129442  168 EPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVL 231
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

6-168

1.61e-11

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: 64.43 E-value: 1.61e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   6 LTLRDVHINFPARKNwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI---- 81
Cdd:COG4615 328 LELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE-ILLDGQPVtadn 400

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  82 ----MQM---VFQDPlsSLNPRLpvwriitepLWIAKRSSEQQRRALAEELAVQ--VGIRPEYLDRLphAFSGGQRQRIA 152
Cdd:COG4615 401 reayRQLfsaVFSDF--HLFDRL---------LGLDGEADPARARELLERLELDhkVSVEDGRFSTT--DLSQGQRKRLA 467

                       170
                ....*....|....*.
gi 16129442 153 IARALSSQPDVIVLDE 168
Cdd:COG4615 468 LLVALLEDRPILVFDE 483

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

31-230

1.71e-11

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: 65.03 E-value: 1.71e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQDPLSSLNPRL-PVWRIIT--EPL 107
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFdAIDDLLTgrEHL 2033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    108 WIAKRsseqQRRALAEEL------AVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:TIGR01257 2034 YLYAR----LRGVPAEEIekvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 16129442    182 LNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQV 230
Cdd:TIGR01257 2110 WNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157

PRK10636

putative ABC transporter ATP-binding protein; Provisional

32-232

2.04e-11

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 2.04e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY-----IRSGSQRIMQMVF----QDPLSSLNPrlpvwri 102
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYFAQHQLEFlradESPLQHLAR------- 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  103 iteplwIAKRSSEQQRRALAEELAVQVGIRPEYLDRlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK10636 401 ------LAPQELEQKLRDYLGGFGFQGDKVTEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129442  183 NLLVTLQEnhglTYVLISHNVSVIRHMSDRVAVMYLGQIV----ELGDAQQVLT 232
Cdd:PRK10636 471 EALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgDLEDYQQWLS 520

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

31-174

2.46e-11

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 2.46e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGS----QRI--MQMVFqdplsSLNPRLP 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgQPVDAGDiatrRRVgyMSQAF-----SLYGELT 355

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   99 VwRiitEPLWI-AK--RSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:NF033858 356 V-R---QNLELhARlfHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

30-201

2.96e-11

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 2.96e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqpshgqyirsgSQRIMQMVFQDPLSSLNPRLPvwriITEPLWI 109
Cdd:COG2401  44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-----------KGTPVAGCVDVPDNQFGREAS----LIDAIGR 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 110 AKRSSEqqrralAEELAVQVGIRPEYL-DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLV-T 187
Cdd:COG2401 109 KGDFKD------AVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD-RQTAKRVARNLqK 181

                       170
                ....*....|....
gi 16129442 188 LQENHGLTYVLISH 201
Cdd:COG2401 182 LARRAGITLVVATH 195

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

32-208

3.03e-11

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: 64.00 E-value: 3.03e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLmGMLQPSHGQYIRSGSQRIMQMVFQDPLSSLnprlpvwRIITEPLWIAK 111
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAKGKLFYVPQRPYMTL-------GTLRDQIIYPD 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   112 RSSEQQRRALAEELAVQvgirpeYLD--RLPH----------------AFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:TIGR00954 540 SSEDMKRRGLSDKDLEQ------ILDnvQLTHilereggwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16129442   174 DISVQAQILNLLvtlqENHGLTYVLISHNVSVIRH 208
Cdd:TIGR00954 614 SVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

4-232

3.32e-11

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 3.32e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    4 TLLTLRDVHINFPARK----NWLGKTTEHVHAI--------NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG 71
Cdd:PRK09700 239 RLMVGRELQNRFNAMKenvsNLAHETVFEVRNVtsrdrkkvRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   72 QYIRSGSQrimqMVFQDPLSSL-------------NPRLPVWRI-----ITEPLWIAKRS------SEQQRRALAEELAV 127
Cdd:PRK09700 319 EIRLNGKD----ISPRSPLDAVkkgmayitesrrdNGFFPNFSIaqnmaISRSLKDGGYKgamglfHEVDEQRTAENQRE 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  128 QVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIR 207
Cdd:PRK09700 395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEII 473

                        250       260
                 ....*....|....*....|....*
gi 16129442  208 HMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQILTNRDDMS 498

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

32-236

3.69e-11

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 3.69e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyIRSGSQRIMQMVFQD--PLSSLN-PRLPVWRII----T 104
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG----GAPRGARVTGDVTLNgePLAAIDaPRLARLRAVlpqaA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 EPLWI--------------AKRSSEQQRR--ALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALS---------S 159
Cdd:PRK13547  93 QPAFAfsareivllgryphARRAGALTHRdgEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTaPAH 236
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

20-242

8.43e-11

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: 61.08 E-value: 8.43e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  20 NWLGKTTEHVHAIngidlqIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmVFQDPLSSLNPRLPV 99
Cdd:cd03288  31 NNLKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID-----ISKLPLHTLRSRLSI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 100 wrIITEPLWIA-----------KRSSEQQRRALA-EELAVQVGIRPEYLDRL----PHAFSGGQRQRIAIARALSSQPDV 163
Cdd:cd03288 100 --ILQDPILFSgsirfnldpecKCTDDRLWEALEiAQLKNMVKSLPGGLDAVvtegGENFSVGQRQLFCLARAFVRKSSI 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442 164 IVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLL 242
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

30-224

1.21e-10

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 1.21e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQMVFQDPlsSLNPRLPVWRIITEPLW- 108
Cdd:TIGR03719  19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV-GYLPQEP--QLDPTKTVRENVEEGVAe 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   109 ----------IAKRSSEQQRR--ALAEE---------------LAVQVGIRPEYLdRLP------HAFSGGQRQRIAIAR 155
Cdd:TIGR03719  96 ikdaldrfneISAKYAEPDADfdKLAAEqaelqeiidaadawdLDSQLEIAMDAL-RCPpwdadvTKLSGGERRRVALCR 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   156 ALSSQPDVIVLDEPTSALDISVQAQILNLlvtLQENHGlTYVLISHNvsviRHMSDRVAvmylGQIVEL 224
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPG-TVVAVTHD----RYFLDNVA----GWILEL 231

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

29-222

1.22e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.22e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQ----MVFQDplssLNprL 97
Cdd:PRK10982  11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksSKEALEngisMVHQE----LN--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   98 PVWRIITEPLWIAKRSSE----------QQRRALAEELAVQVGIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK10982  85 VLQRSVMDNMWLGRYPTKgmfvdqdkmyRDTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129442  168 EPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213

PLN03130

ABC transporter C family member; Provisional

32-232

1.48e-10

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 1.48e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMVFQDPLSSLN--PRLPVW-----RIIT 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCD-ISKFGLMDLRKVLGiiPQAPVLfsgtvRFNL 1333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   105 EP--------LWiakrssEQQRRALAEELavqvgIR--PEYLD----RLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PLN03130 1334 DPfnehndadLW------ESLERAHLKDV-----IRrnSLGLDaevsEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129442   171 SALDISVQAQILNllvTLQEN-HGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:PLN03130 1403 AAVDVRTDALIQK---TIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461

PRK10636

putative ABC transporter ATP-binding protein; Provisional

37-202

1.67e-10

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 1.67e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   37 LQIRRG---------------ETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRiMQMVFQDplsslNPRLPV-- 99
Cdd:PRK10636   7 LQIRRGvrvlldnatatinpgQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-LAWVNQE-----TPALPQpa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  100 ----------WRIITEPLWIAKRSSEQQR----------------RALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAI 153
Cdd:PRK10636  81 leyvidgdreYRQLEAQLHDANERNDGHAiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16129442  154 ARALSSQPDVIVLDEPTSALDisvqaqiLNLLVTLQ---ENHGLTYVLISHN 202
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHD 205

PTZ00243

ABC transporter; Provisional

35-226

6.72e-10

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 6.72e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-----QR--IMQMVFQDPLSSLNPRLPvwriitEPL 107
Cdd:PTZ00243  679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSiayvpQQawIMNATVRGNILFFDEEDA------ARL 752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   108 WIAKRSS--EQQRRALAEELAVQVGIRPEYLdrlphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:PTZ00243  753 ADAVRVSqlEADLAQLGGGLETEIGEKGVNL-------SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 16129442   186 VtLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGD 226
Cdd:PTZ00243  826 F-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864

PTZ00243

ABC transporter; Provisional

32-225

1.24e-09

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 1.24e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMVFQDP-LSSLNPRLPVw 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglrelRRQFSMIPQDPvLFDGTVRQNV- 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   101 riitEPLWIAkrSSEQQRRALaeELavqVGIR------PEYLD-RLPHA---FSGGQRQRIAIARALSSQ-PDVIVLDEP 169
Cdd:PTZ00243 1405 ----DPFLEA--SSAEVWAAL--EL---VGLRervaseSEGIDsRVLEGgsnYSVGQRQLMCMARALLKKgSGFILMDEA 1473

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129442   170 TSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMG 1526

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

31-221

2.08e-09

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 2.08e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmvFQDPLSSLNPRL---PVWRIITEPL 107
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD------IETNLDAVRQSLgmcPQHNILFHHL 1018

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    108 WIAK----------RSSEQ---QRRALAEELAVQVGIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01257 1019 TVAEhilfyaqlkgRSWEEaqlEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 16129442    175 ISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:TIGR01257 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

32-226

2.14e-09

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 2.14e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQYIRSGSQRI-----------MQMVFQDPL-------- 90
Cdd:PRK09580  17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLelspedragegIFMAFQYPVeipgvsnq 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   91 ----SSLNprlpvwriiteplwiAKRSSEQQR-------RALAEELAVQVGIRPEYLDR-LPHAFSGGQRQRIAIARALS 158
Cdd:PRK09580  97 fflqTALN---------------AVRSYRGQEpldrfdfQDLMEEKIALLKMPEDLLTRsVNVGFSGGEKKRNDILQMAV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442  159 SQPDVIVLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMS-DRVAVMYLGQIVELGD 226
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229

PRK15064

ABC transporter ATP-binding protein; Provisional

22-201

2.48e-09

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 2.48e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVfQDPLSSLNPRLPVWR 101
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA-QDHAYDFENDLTLFD 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  102 iiteplWIAkrsseQQRRALAEELAVQvGIrpeyLDRL----------PHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK15064 404 ------WMS-----QWRQEGDDEQAVR-GT----LGRLlfsqddikksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467

                        170       180       190
                 ....*....|....*....|....*....|.
gi 16129442  172 ALDI-SVQAqiLNLLVtlqENHGLTYVLISH 201
Cdd:PRK15064 468 HMDMeSIES--LNMAL---EKYEGTLIFVSH 493

40850658_otr

NF000106

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

29-232

3.45e-09

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 3.45e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   29 VHAINGIDLQIRRGETLGIVGESGcgkstlAQLLMGMLqPSHGQYIRSGSQRIMQMVFQDPLSSLNPRLPVWRIIT---- 104
Cdd:NF000106  26 VKAVDGVDLDVREGTVLGVLGP*G------AA**RGAL-PAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*grr 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 ------EPLWIAKRS---SEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:NF000106  99 esfsgrENLYMIGR*ldlSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  176 SVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLT 232
Cdd:NF000106 178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233

PLN03130

ABC transporter C family member; Provisional

144-225

3.91e-09

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 3.91e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTlQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:PLN03130  742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819


                  ..
gi 16129442   224 LG 225
Cdd:PLN03130  820 EG 821

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

29-213

1.39e-08

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: 54.19 E-value: 1.39e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAqllMGMLQpSHGQ--YIRSGS----QRIMQMvfQDP-------LS---- 91
Cdd:cd03270   8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLA---FDTIY-AEGQrrYVESLSayarQFLGQM--DKPdvdsiegLSpaia 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  92 ------SLNPRLPVwRIITEP------LWiakrsseqQRRALAEELAVQVGIRPEYL--DRLPHAFSGGQRQRIAIARAL 157
Cdd:cd03270  82 idqkttSRNPRSTV-GTVTEIydylrlLF--------ARVGIRERLGFLVDVGLGYLtlSRSAPTLSGGEAQRIRLATQI 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 158 SSQ-PDVI-VLDEPTSALDisvQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHmSDRV 213
Cdd:cd03270 153 GSGlTGVLyVLDEPSIGLH---PRDNDRLIETLKRlrDLGNTVLVVEHDEDTIRA-ADHV 208

PLN03073

ABC transporter F family; Provisional

133-219

1.75e-08

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 1.75e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  133 PEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhglTYVLISHN-------VSV 205
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAreflntvVTD 410

                         90
                 ....*....|....
gi 16129442  206 IRHMSDRVAVMYLG 219
Cdd:PLN03073 411 ILHLHGQKLVTYKG 424

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

142-229

2.04e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.04e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLtyVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGL 468

                         90
                 ....*....|..
gi 16129442  221 ---IVELGDAQQ 229
Cdd:PRK10982 469 vagIVDTKTTTQ 480

GguA

NF040905

sugar ABC transporter ATP-binding protein;

9-229

2.95e-08

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 2.95e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    9 RDVHINFPAR-----------KNWlgkTTEH-VHA----INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMlqpSHGQ 72
Cdd:NF040905 240 RDLEDRYPERtpkigevvfevKNW---TVYHpLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   73 YIrSGSqrimqmVFQD----PLSS--------------------LNPRLPVWRIITEPLW--IAKRS--SEQQRRALAEE 124
Cdd:NF040905 314 NI-SGT------VFKDgkevDVSTvsdaidaglayvtedrkgygLNLIDDIKRNITLANLgkVSRRGviDENEEIKVAEE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  125 LAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDisVQA-----QILNLLVtlqeNHGLTYVLI 199
Cdd:NF040905 387 YRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyeiyTIINELA----AEGKGVIVI 460

                        250       260       270
                 ....*....|....*....|....*....|...
gi 16129442  200 SHNVSVIRHMSDRVAVMYLGQIV-EL--GDAQQ 229
Cdd:NF040905 461 SSELPELLGMCDRIYVMNEGRITgELprEEASQ 493

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

32-214

3.18e-08

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.18e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyirSGSQRI---MQMVFQDPL-SSLNPRLPVWRIIT--- 104
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD------SGTIKIgetVKLAYVDQSrDALDPNKTVWEEISggl 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  105 EPLWIAKRS--------------SEQQRRalaeelavqVGIrpeyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK11819 414 DIIKVGNREipsrayvgrfnfkgGDQQKK---------VGV-----------LSGGERNRLHLAKTLKQGGNVLLLDEPT 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129442  171 SALDISvqaqilnllvTLQ--ENHGLTY----VLISHNvsviRHMSDRVA 214
Cdd:PRK11819 474 NDLDVE----------TLRalEEALLEFpgcaVVISHD----RWFLDRIA 509

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

46-224

5.36e-08

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 5.36e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   46 GIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQMVFQDPLssLNPRLPVWRIITEPL-----------WIAKRSS 114
Cdd:PRK11819  37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV-GYLPQEPQ--LDPEKTVRENVEEGVaevkaaldrfnEIYAAYA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  115 EQQRR--ALAEELA-VQvgirpEYLD------------------RLPHA------FSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK11819 114 EPDADfdALAAEQGeLQ-----EIIDaadawdldsqleiamdalRCPPWdakvtkLSGGERRRVALCRLLLEKPDMLLLD 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129442  168 EPTSALDI-SVQAqilnLLVTLQENHGlTYVLISHNvsviRHMSDRVAvmylGQIVEL 224
Cdd:PRK11819 189 EPTNHLDAeSVAW----LEQFLHDYPG-TVVAVTHD----RYFLDNVA----GWILEL 233

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

143-222

1.65e-07

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: 50.72 E-value: 1.65e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSV-IRHMSDRVAVMYLGQI 221
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198


                .
gi 16129442 222 V 222
Cdd:cd03233 199 I 199

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

32-219

9.55e-07

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: 48.39 E-value: 9.55e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLmgmlqpshgqyirsgSQR-IMQMVFQDPLSSLNPRLPVWRIITeplwia 110
Cdd:cd03232  23 LNNISGYVKPGTLTALMGESGAGKTTLLDVL---------------AGRkTAGVITGEILINGRPLDKNFQRST------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 111 krSSEQQRRALAEELAVQVGIRPEYLDRlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQe 190
Cdd:cd03232  82 --GYVEQQDVHSPNLTVREALRFSALLR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA- 155

                       170       180       190
                ....*....|....*....|....*....|
gi 16129442 191 NHGLTYVLISHNVS-VIRHMSDRVAVMYLG 219
Cdd:cd03232 156 DSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185

PRK13543

heme ABC exporter ATP-binding protein CcmA;

35-175

1.01e-06

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 1.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMVFQDPLSSLNPRLPVwriiTEPL-W 108
Cdd:PRK13543  30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrGDRSRFMAYLGHLPGLKADLST----LENLhF 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442  109 IAKRSSEQQRRALAEELAVqVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAI-VGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

144-207

1.80e-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: 49.24 E-value: 1.80e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   144 SGGQRQRIAIARALSSQ---PDVIVLDEPTSAL---DIsvqAQILNLLVTLQENhGLTYVLISHNVSVIR 207
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDK-GNTVVVIEHNLDVIK 896

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

47-207

2.41e-06

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 2.41e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   47 IVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQRIMQMVFQDPLSSlNPRLPVWRIITEPLwiaKRSSEQQRRALAEEL 125
Cdd:PRK13541  31 IKGANGCGKSSLLRMIAGIMQPSSGNiYYKNCNINNIAKPYCTYIGH-NLGLKLEMTVFENL---KFWSEIYNSAETLYA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  126 AVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLVTLQENHGLTYVLISHNVSV 205
Cdd:PRK13541 107 AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGIVLLSSHLESS 185


                 ..
gi 16129442  206 IR 207
Cdd:PRK13541 186 IK 187

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

144-207

2.86e-06

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 2.86e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129442 144 SGGQRQRIAIARALSSQ---PDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIR 207
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIK 236

3a01205

TIGR00956

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

144-232

9.05e-06

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 9.05e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:TIGR00956  211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQI 290

                           90
                   ....*....|
gi 16129442    223 ELGDAQQVLT 232
Cdd:TIGR00956  291 YFGPADKAKQ 300

UvrA

COG0178

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

144-207

1.17e-05

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

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 1.17e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 144 SGGQRQRIAIARALS---SQPDVIVLDEPTSAL---DISVQAQILNLLVtlqeNHGLTYVLISHNVSVIR 207
Cdd:COG0178 828 SGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRLV----DKGNTVVVIEHNLDVIK 893

PRK00635

excinuclease ABC subunit A; Provisional

136-249

2.21e-05

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   136 LDRLP-----HAFSGGQRQRIAIARAL---SSQPDVIVLDEPTSALDI-SVQAQILNLLVTLQENHglTYVLISHNVSVI 206
Cdd:PRK00635  798 LDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGH--TVVIIEHNMHVV 875

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 16129442   207 RhMSDRvaVMYLGQivELGDAQQVLTAPAHPYTRLLLDSLPAI 249
Cdd:PRK00635  876 K-VADY--VLELGP--EGGNLGGYLLASCSPEELIHLHTPTAK 913

PLN03140

ABC transporter G family member; Provisional

10-225

2.69e-05

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 2.69e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    10 DVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMlqpSHGQYIrSGSQRI-----MQM 84
Cdd:PLN03140  874 NYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGYI-EGDIRIsgfpkKQE 949

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    85 VF--------QDPLSSlnPRLPVWR--IITEPLWIAKRSSEQQRRALAEELAVQVgirpeYLDRLPHAFSG--------- 145
Cdd:PLN03140  950 TFarisgyceQNDIHS--PQVTVREslIYSAFLRLPKEVSKEEKMMFVDEVMELV-----ELDNLKDAIVGlpgvtglst 1022

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   146 GQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLVTLQENHGLTYVLISHNVSV-IRHMSDRVAVMYL-GQIVE 223
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIY 1101


                  ..
gi 16129442   224 LG 225
Cdd:PLN03140 1102 SG 1103

uvrA

PRK00349

excinuclease ABC subunit UvrA;

144-207

2.71e-05

excinuclease ABC subunit UvrA;

Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 2.71e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442  144 SGGQRQRIAIARALSSQPD---VIVLDEPTSAL---DISVQAQILNLLVtlqeNHGLTYVLISHNVSVIR 207
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIRKLLEVLHRLV----DKGNTVVVIEHNLDVIK 897

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

133-211

6.01e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.

Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 6.01e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 133 PEYLDRLphafSGGQRQ------RIAIARALSSQPDVIVLDEPTSALDI-SVQAQILNLLVTLQENHGLTYVLISHNVSV 205
Cdd:cd03240 110 LDMRGRC----SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEEL 185


                ....*.
gi 16129442 206 IRHMSD 211
Cdd:cd03240 186 VDAADH 191

3a01205

TIGR00956

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

26-206

7.53e-05

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 7.53e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     26 TEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLL-----MGMLQP----SHGQYIRSGSQRIMQMVFQDPLSSlnPR 96
Cdd:TIGR00956  773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVITGgdrlVNGRPLDSSFQRSIGYVQQQDLHL--PT 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442     97 LPVwriiTEPLWIAKRSSEQQRRALAEELA-VQVGIRPEYLDRLPHAFSG--------GQRQRIAIARALSSQPDVIV-L 166
Cdd:TIGR00956  851 STV----RESLRFSAYLRQPKSVSKSEKMEyVEEVIKLLEMESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfL 926

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 16129442    167 DEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVI 206
Cdd:TIGR00956  927 DEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSAI 965

AAA_25

pfam13481

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.

16-201

2.13e-04

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.

Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 41.60 E-value: 2.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    16 PARKNWLgkttehvhaINGIdlqIRRGETLGIVGESGCGKSTLA-QLLMGMLQ--PSHGQYIRSGSQRIMQMVFQDPLSS 92
Cdd:pfam13481  19 PPPRRWL---------IKGL---LPAGGLGLLAGAPGTGKTTLAlDLAAAVATgkPWLGGPRVPEQGKVLYVSAEGPADE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    93 LNPRLPVWRiiteplwiakrsseQQRRALAEELAVQVG--IRPEYLDRLPHAFSGGQRQRIAIARAlSSQPDVIVLDEPT 170
Cdd:pfam13481  87 LRRRLRAAG--------------ADLDLPARLLFLSLVesLPLFFLDRGGPLLDADVDALEAALEE-VEDPDLVVIDPLA 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 16129442   171 SALDISVQA-----QILNLLVTLQENHGLTYVLISH 201
Cdd:pfam13481 152 RALGGDENSnsdvgRLVKALDRLARRTGATVLLVHH 187

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

32-174

2.28e-04

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 2.28e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpSHGQ-YI--------RSGS--------QRI------MQMVFQD 88
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQgYSndltlfgrRRGSgetiwdikKHIgyvsssLHLDYRV 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   89 PLSSLNPrlpvwrIIT---EPLWIAKRSSEQQRRaLAEELAVQVGIRPEYLDRLPHAFSGGQrQRIA-IARALSSQPDVI 164
Cdd:PRK10938 352 STSVRNV------ILSgffDSIGIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLL 423

                        170
                 ....*....|
gi 16129442  165 VLDEPTSALD 174
Cdd:PRK10938 424 ILDEPLQGLD 433

AAA_16

pfam13191

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...

41-199

2.80e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.

Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.95 E-value: 2.80e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442    41 RGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVfqdPLSSLNPRLPVWRIITEPLwiAKRSSEQQRRA 120
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYS---PLLEALTREGLLRQLLDEL--ESSLLEAWRAA 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129442   121 LAEELAVQVGIRPEYLDRLPHAFsggqrQRIAIARALSSQPDVIVLDEptsaLDISVQAQiLNLLVTLQENHGLTYVLI 199
Cdd:pfam13191  98 LLEALAPVPELPGDLAERLLDLL-----LRLLDLLARGERPLVLVLDD----LQWADEAS-LQLLAALLRLLESLPLLV 166

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

127-234

4.49e-04

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 4.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   127 VQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQ-PDVI-VLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVS 204
Cdd:TIGR00630 473 IDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHDED 551

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16129442   205 VIRHmSDRV------AVMYLGQIVELGDAQQVLTAP 234
Cdd:TIGR00630 552 TIRA-ADYVidigpgAGEHGGEVVASGTPEEILANP 586

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

102-202

5.34e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 5.34e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442 102 IITEPLWIAKRSSEQQRRALAEELAVQVG-IRPEYLDRLPHAfSGGQRQRIAIARALSSQP----DVIVLDEPTSALDIS 176
Cdd:cd03227  37 ILDAIGLALGGAQSATRRRSGVKAGCIVAaVSAELIFTRLQL-SGGEKELSALALILALASlkprPLYILDEIDRGLDPR 115

                        90       100
                ....*....|....*....|....*.
gi 16129442 177 VQAQILNLLVtLQENHGLTYVLISHN 202
Cdd:cd03227 116 DGQALAEAIL-EHLVKGAQVIVITHL 140

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

23-174

1.01e-03

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 1.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   23 GKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG---------------MLQPSHGqyiRSGSQRIMQMvfq 87
Cdd:NF033858  12 GKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevlggdMADARHR---RAVCPRIAYM--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129442   88 dP--L-SSLNPRLPVwriiTEPLWIAKR---SSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:NF033858  82 -PqgLgKNLYPTLSV----FENLDFFGRlfgQDAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDP 155

                        170
                 ....*....|...
gi 16129442  162 DVIVLDEPTSALD 174
Cdd:NF033858 156 DLLILDEPTTGVD 168

FliI

COG1157

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...

29-66

1.34e-03

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];

Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 40.01 E-value: 1.34e-03

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16129442  29 VHAINGIdLQIRRGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:COG1157 145 VRAIDGL-LTVGRGQRIGIFAGSGVGKST----LLGMI 177

ATPase_flagellum-secretory_path_III

cd01136

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...

29-66

5.94e-03

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.

Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 37.54 E-value: 5.94e-03

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16129442  29 VHAINGIdLQIRRGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:cd01136  55 VRAIDGL-LTCGEGQRIGIFAGSGVGKST----LLGMI 87

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