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Conserved domains on  [gi|493753820|ref|WP_006702714|]
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ABC transporter ATP-binding protein [Granulicatella elegans]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438412)

ABC transporter ATP-binding protein is part of a complex involved in the transport of a wide variety of different compounds, including sugars, ions, peptides, and drugs; similar to ATPase component of ABC-type multidrug transport systems

CATH:  3.40.50.300
Gene Ontology:  GO:0140359|GO:0016887|GO:0005524
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NatA super family cl34774
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-195 5.57e-38

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG4555:

Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 131.13  E-value: 5.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII------------APSSLFYYE 67
Cdd:COG4555    1 MIEVENLSKKYGKvPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreARRQIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 TIEWFDGNLSGMDYLLYIKNVW-NSSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEIT 142
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYgLFDEELKKRIEELiellGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 143 NGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIVKIENCRIEEVQ 195
Cdd:COG4555  161 NGLDVMARRLLREILRALKKEGKtVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
 
Name Accession Description Interval E-value
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-195 5.57e-38

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: 131.13  E-value: 5.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII------------APSSLFYYE 67
Cdd:COG4555    1 MIEVENLSKKYGKvPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreARRQIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 TIEWFDGNLSGMDYLLYIKNVW-NSSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEIT 142
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYgLFDEELKKRIEELiellGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 143 NGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIVKIENCRIEEVQ 195
Cdd:COG4555  161 NGLDVMARRLLREILRALKKEGKtVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
15-191 1.04e-34

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: 120.58  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETIEW------FDGNLSGMDYL 82
Cdd:cd03230   15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdIKKEPEEVKRRIGYlpeepsLYENLTVRENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 lyiknvwnssqnleheieywemadyihlpirKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHS 162
Cdd:cd03230   95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK 143
                        170       180       190
                 ....*....|....*....|....*....|
gi 493753820 163 QQ-LIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03230  144 EGkTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
16-143 2.59e-16

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: 72.30  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSgmdYLLYIKNVWNSSQNL 95
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIG---YVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493753820   96 EHEIEYWEMADY-------------------------IHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITN 143
Cdd:pfam00005  78 ENLRLGLLLKGLskrekdaraeealeklglgdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
16-193 1.26e-15

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 72.54  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSGMDYLLYIKNVWNSSQN- 94
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKe 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 ----LEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ-QLIIIS 169
Cdd:PRK13546 120 ikamTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnKTIFFV 199
                        170       180
                 ....*....|....*....|....
gi 493753820 170 SHYKEELMNVCDKIVKIENCRIEE 193
Cdd:PRK13546 200 SHNLGQVRQFCTKIAWIEGGKLKD 223
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
14-171 2.29e-14

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: 68.15  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   14 MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFD-----GNLSGMdyllyiKNV 88
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilylGHLPGL------KPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   89 WNSSQNLE--------HEIEYWE------MADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFF 154
Cdd:TIGR01189  88 LSALENLHfwaaihggAQRTIEDalaavgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
                         170
                  ....*....|....*...
gi 493753820  155 NRITE-IHSQQLIIISSH 171
Cdd:TIGR01189 168 GLLRAhLARGGIVLLTTH 185
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
15-140 3.34e-06

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 45.89  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------APSSLFYYETIEWFDGNLSGMDYLLYI 85
Cdd:NF040729  20 VLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILvngnevtkpGPDRGFVFQNYALFPWMTVKENIEYPM 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820  86 KNVWNSSQNLEHEIEYW-EMAD---YIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDE 140
Cdd:NF040729 100 KQQKMPKQEREKRLNELlEMAQltgKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
25-177 5.57e-05

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: 41.59  E-value: 5.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    25 KGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfYYETIEWFDGNLSGMDYLLYIKNVWNSSQnleheieywem 104
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------YIDGEDILEEVLDQLLLIIVGGKKASGSG----------- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   105 adyihlpirkyslGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR-------TKFFNRITEIHSQQLIIISSHYKEELM 177
Cdd:smart00382  64 -------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEallllleELRLLLLLKSEKNLTVILTTNDEKDLG 130
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
114-191 9.93e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 38.95  E-value: 9.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820 114 KYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRI-TEIHSQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
 
Name Accession Description Interval E-value
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-195 5.57e-38

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: 131.13  E-value: 5.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII------------APSSLFYYE 67
Cdd:COG4555    1 MIEVENLSKKYGKvPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreARRQIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 TIEWFDGNLSGMDYLLYIKNVW-NSSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEIT 142
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYgLFDEELKKRIEELiellGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 143 NGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIVKIENCRIEEVQ 195
Cdd:COG4555  161 NGLDVMARRLLREILRALKKEGKtVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
15-191 2.52e-35

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 124.02  E-value: 2.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETI------EWFDGNLSGMDYL 82
Cdd:COG1131   15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRRIgyvpqePALYPDLTVRENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNVWNSSQNLEHE-----IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRI 157
Cdd:COG1131   95 RFFARLYGLPRKEAREridelLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELL 174
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 158 TEIHSQQL-IIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:COG1131  175 RELAAEGKtVLLSTHYLEEAERLCDRVAIIDKGRI 209
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
15-191 1.04e-34

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: 120.58  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETIEW------FDGNLSGMDYL 82
Cdd:cd03230   15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdIKKEPEEVKRRIGYlpeepsLYENLTVRENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 lyiknvwnssqnleheieywemadyihlpirKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHS 162
Cdd:cd03230   95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK 143
                        170       180       190
                 ....*....|....*....|....*....|
gi 493753820 163 QQ-LIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03230  144 EGkTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2-191 1.94e-31

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: 113.08  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQV--RLKTREmILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYET---------IE 70
Cdd:cd03268    1 LKTNDLtkTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIealrrigalIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  71 --WFDGNLSGMDYLLYIKNVWN-SSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDE 147
Cdd:cd03268   80 apGFYPNLTARENLRLLARLLGiRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 148 YyrtkffnRITEIhsQQLI----------IISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03268  160 D-------GIKEL--RELIlslrdqgitvLISSHLLSEIQKVADRIGIINKGKL 204
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
15-193 2.78e-31

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: 113.01  E-value: 2.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---APSSLFYYETieWFDGNLSGMDYLLYIKNVWNS 91
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgRVSSLLGLGG--GFNPELTGRENIYLNGRLLGL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  92 S----QNLEHEI-EYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ-L 165
Cdd:cd03220  115 SrkeiDEKIDEIiEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkT 194
                        170       180
                 ....*....|....*....|....*...
gi 493753820 166 IIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:cd03220  195 VILVSHDPSSIKRLCDRALVLEKGKIRF 222
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-171 1.39e-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: 108.34  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRlKTR--EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETIEW- 71
Cdd:COG4133    2 MLEAENLS-CRRgeRLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepIRDAREDYRRRLAYl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 -----FDGNLSGMDYLLY---IKNVWNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITN 143
Cdd:COG4133   81 ghadgLKPELTVRENLRFwaaLYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 493753820 144 GLDEYYRTKFFNRITEiHSQQ--LIIISSH 171
Cdd:COG4133  161 ALDAAGVALLAELIAA-HLARggAVLLTTH 189
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
15-190 5.88e-27

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: 100.01  E-value: 5.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetiEWFDGNLSGMDYLLYIKNVWnssqn 94
Cdd:cd00267   14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------LIDGKDIAKLPLEELRRRIG----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 leheieywemadYIHlpirKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYK 173
Cdd:cd00267   77 ------------YVP----QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDP 140
                        170
                 ....*....|....*..
gi 493753820 174 EELMNVCDKIVKIENCR 190
Cdd:cd00267  141 ELAELAADRVIVLKDGK 157
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
15-193 3.96e-26

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 100.16  E-value: 3.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA---PSSLFYYETIewFDGNLSGMDyllyikNVWNS 91
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVngrVSALLELGAG--FHPELTGRE------NIYLN 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  92 S----------QNLEHEI-EYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEI 160
Cdd:COG1134  113 GrllglsrkeiDEKFDEIvEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL 192
                        170       180       190
                 ....*....|....*....|....*....|....
gi 493753820 161 HSQ-QLIIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:COG1134  193 RESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
15-191 2.49e-24

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: 94.88  E-value: 2.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII------------APSSLFY---YETIewfDGNLSGM 79
Cdd:cd03263   17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrkaARQSLGYcpqFDAL---FDELTVR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 DYLLYI-----KNVWNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFF 154
Cdd:cd03263   94 EHLRFYarlkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493753820 155 NRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03263  174 DLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
4-188 4.69e-23

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: 91.37  E-value: 4.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   4 LNQVRL---KTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGkiiapsslfyyeTIEWFDGNLSGMD 80
Cdd:cd03225    2 LKNLSFsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG------------EVLVDGKDLTKLS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  81 YLLYIKNVWNSSQNLEH---------EIEYW----------------------EMADYIHLPIRKYSLGMKQRLLIAMYF 129
Cdd:cd03225   70 LKELRRKVGLVFQNPDDqffgptveeEVAFGlenlglpeeeieerveealelvGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820 130 MSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIVKIEN 188
Cdd:cd03225  150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLED 209
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
15-191 1.56e-21

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: 86.72  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG-NLSGMDYLLYIKNVWNSSQ 93
Cdd:cd03214   14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------LLDGkDLASLSPKELARKIAYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  94 NLeheiEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSH 171
Cdd:cd03214   81 AL----ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLH 156
                        170       180
                 ....*....|....*....|
gi 493753820 172 YKEELMNVCDKIVKIENCRI 191
Cdd:cd03214  157 DLNLAARYADRVILLKDGRI 176
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
15-184 1.87e-20

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: 84.51  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI-IAPSSLFY----------YETIEWfDGNLSGMDYL- 82
Cdd:cd03235   14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKerkrigyvpqRRSIDR-DFPISVRDVVl 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 --LYIKNVWNSSQNLEHE------IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFF 154
Cdd:cd03235   93 mgLYGHKGLFRRLSKADKakvdeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY 172
                        170       180       190
                 ....*....|....*....|....*....|.
gi 493753820 155 NRITEIHSQQL-IIISSHYKEELMNVCDKIV 184
Cdd:cd03235  173 ELLRELRREGMtILVVTHDLGLVLEYFDRVL 203
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
12-191 2.60e-20

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: 84.17  E-value: 2.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  12 REMILKDIDFTFEKGnIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETIEW------FDGNLSGM 79
Cdd:cd03264   12 KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdVLKQPQKLRRRIGYlpqefgVYPNFTVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 DYLLYI---KNVwnSSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTK 152
Cdd:cd03264   91 EFLDYIawlKGI--PSKEVKARVDEVlelvNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493753820 153 FFNRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03264  169 FRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
16-191 8.34e-20

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: 83.19  E-value: 8.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGK-IIAPSSLF-----YYETIEW------FDGNLSGMDYLL 83
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVrepreVRRRIGIvfqdlsVDDELTGWENLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  84 YIKNVWNSS-----QNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRIT 158
Cdd:cd03265   96 IHARLYGVPgaerrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 159 EIHSQQ--LIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03265  176 KLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
15-191 2.32e-19

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: 81.56  E-value: 2.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapssLFYYETIEWFDGNLSG--------------MD 80
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-----LFDGKPLDIAARNRIGylpeerglypkmkvID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  81 YLLYIKNVWN-SSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFN 155
Cdd:cd03269   90 QLVYLAQLKGlKKEEARRRIDEWlerlELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493753820 156 RITEIHSQ-QLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03269  170 VIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRA 206
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
15-188 1.87e-18

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: 79.22  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDGNLSG--------------MD 80
Cdd:cd03226   15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-------------LNGKPIKakerrksigyvmqdVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  81 YLLYIKNVWN-----------SSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYY 149
Cdd:cd03226   82 YQLFTDSVREelllglkeldaGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493753820 150 RTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIEN 188
Cdd:cd03226  162 MERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLAN 201
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-184 2.13e-18

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 79.75  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLK-TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI-------------IApsslfY- 65
Cdd:COG1121    6 AIELENLTVSyGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpprrarrrIG-----Yv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  66 --YETIEW-FdgNLSGMD----YLLYIKNVWNSSQNLEHE-----IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQA 133
Cdd:COG1121   81 pqRAEVDWdF--PITVRDvvlmGRYGRRGLFRRPSRADREavdeaLERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493753820 134 ECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIV 184
Cdd:COG1121  159 DLLLLDEPFAGVDAATEEALYELLRELRREGKtILVVTHDLGAVREYFDRVL 210
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1-191 2.19e-18

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: 79.33  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQV-----RLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyeTIEWFDGN 75
Cdd:cd03266    1 MITADALtkrfrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA----------TVDGFDVV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  76 ----------------------LSGMDYLLYIKNVW-----NSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMY 128
Cdd:cd03266   71 kepaearrrlgfvsdstglydrLTARENLEYFAGLYglkgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493753820 129 FMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ-LIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03266  151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGkCILFSTHIMQEVERLCDRVVVLHRGRV 214
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-191 5.00e-18

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: 78.53  E-value: 5.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLK--TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfYYETIEWFDGNLS-- 77
Cdd:COG1122    1 IELENLSFSypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV-------LVDGKDITKKNLRel 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  78 ----GM-----DYLLYIKNVWN----SSQNL---EHEI--------EYWEMADYIHLPIRKYSLGMKQRLLIA----Myf 129
Cdd:COG1122   74 rrkvGLvfqnpDDQLFAPTVEEdvafGPENLglpREEIrerveealELVGLEHLADRPPHELSGGQKQRVAIAgvlaM-- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493753820 130 msQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:COG1122  152 --EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDDGRI 212
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
16-184 2.78e-17

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: 75.16  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDGnlsgmdyllyiknvwnssqnl 95
Cdd:cd03216   16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI-------------LVDG--------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  96 eHEIEYWEMADYIHLPIR---KYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSH 171
Cdd:cd03216   62 -KEVSFASPRDARRAGIAmvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISH 140
                        170
                 ....*....|...
gi 493753820 172 YKEELMNVCDKIV 184
Cdd:cd03216  141 RLDEVFEIADRVT 153
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
15-188 9.57e-17

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: 73.96  E-value: 9.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG-NLSGMDYLLYIKNVWNSSQ 93
Cdd:cd03228   17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-------------IDGvDLRDLDLESLRKNIAYVPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  94 NleheieywemadyIHL---PIRK--YSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQLIII 168
Cdd:cd03228   84 D-------------PFLfsgTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIV 150
                        170       180
                 ....*....|....*....|
gi 493753820 169 SSHyKEELMNVCDKIVKIEN 188
Cdd:cd03228  151 IAH-RLSTIRDADRIIVLDD 169
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
16-143 2.59e-16

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: 72.30  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSgmdYLLYIKNVWNSSQNL 95
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIG---YVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493753820   96 EHEIEYWEMADY-------------------------IHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITN 143
Cdd:pfam00005  78 ENLRLGLLLKGLskrekdaraeealeklglgdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-184 3.48e-16

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: 73.92  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG-NLSG 78
Cdd:COG1120    1 MLEAENLSVGYGGrPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-------------LLDGrDLAS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  79 MD---------YLL---------------------YIKNVWNSSQNLEHEI----EYWEMADYIHLPIRKYSLGMKQRLL 124
Cdd:COG1120   68 LSrrelarriaYVPqeppapfgltvrelvalgrypHLGLFGRPSAEDREAVeealERTGLEHLADRPVDELSGGERQRVL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493753820 125 IAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSHykeEL---MNVCDKIV 184
Cdd:COG1120  148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLH---DLnlaARYADRLV 209
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
16-193 1.26e-15

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 72.54  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSGMDYLLYIKNVWNSSQN- 94
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKe 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 ----LEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ-QLIIIS 169
Cdd:PRK13546 120 ikamTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnKTIFFV 199
                        170       180
                 ....*....|....*....|....
gi 493753820 170 SHYKEELMNVCDKIVKIENCRIEE 193
Cdd:PRK13546 200 SHNLGQVRQFCTKIAWIEGGKLKD 223
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
7-191 1.41e-15

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: 71.98  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   7 VRLKTREM-ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI----IAPSS-----------LFYYETIE 70
Cdd:cd03267   27 FKRKYREVeALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKrrkkflrrigvVFGQKTQL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  71 WFDgnLSGMDYLLYIKNVWNSS-----QNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGL 145
Cdd:cd03267  107 WWD--LPVIDSFYLLAAIYDLPparfkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493753820 146 D----EYYRtKFFNRITEIHsQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03267  185 DvvaqENIR-NFLKEYNRER-GTTVLLTSHYMKDIEALARRVLVIDKGRL 232
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
18-192 1.92e-15

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: 71.17  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  18 DIDFTFEkGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfYYETIEWFDG----NLSGMD---------YLLY 84
Cdd:cd03297   16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTI-------VLNGTVLFDSrkkiNLPPQQrkiglvfqqYALF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  85 --------IKNVWNSSQNLEHEIEYWEMADYIHL------PIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR 150
Cdd:cd03297   88 phlnvrenLAFGLKRKRNREDRISVDELLDLLGLdhllnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493753820 151 TKFFNRITEIHS--QQLIIISSHYKEELMNVCDKIVKIENCRIE 192
Cdd:cd03297  168 LQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
16-195 5.02e-15

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 71.29  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGkiiapsslfyyeTIEWFDGNLSGMD-----YL-----LYI 85
Cdd:COG4152   17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG------------EVLWDGEPLDPEDrrrigYLpeergLYP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  86 K-NVWN-----------SSQNLEHEIEYW----EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYY 149
Cdd:COG4152   85 KmKVGEqlvylarlkglSKAEAKRRADEWlerlGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820 150 RTKFFNRITEIHSQQLIII-SSH---YKEELmnvCDKIV------KIENCRIEEVQ 195
Cdd:COG4152  165 VELLKDVIRELAAKGTTVIfSSHqmeLVEEL---CDRIViinkgrKVLSGSVDEIR 217
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-191 6.83e-15

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: 69.83  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRL-----KTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG-N 75
Cdd:cd03255    1 IELKNLSKtygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR-------------VDGtD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  76 LSGMD-----------------------YLLYIKNV-----------WNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQ 121
Cdd:cd03255   68 ISKLSekelaafrrrhigfvfqsfnllpDLTALENVelplllagvpkKERRERAEELLERVGLGDRLNHYPSELSGGQQQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493753820 122 RLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSHyKEELMNVCDKIVKIENCRI 191
Cdd:cd03255  148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTH-DPELAEYADRIIELRDGKI 218
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-193 1.66e-14

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: 71.02  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLK---TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI---------IAPSSL-----F 64
Cdd:COG2274  474 IELENVSFRypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDPASLrrqigV 553
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  65 YYETIEWFDG----NLSGMDYLLYIKNVWNSSQ--NLEHEIEywEMADYIHLPI----RKYSLGMKQRLLIAMYFMSQAE 134
Cdd:COG2274  554 VLQDVFLFSGtireNITLGDPDATDEEIIEAARlaGLHDFIE--ALPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPR 631
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820 135 CWLMDEITNGLDEYYRTKFFNRITEIHSQQLIIISSHyKEELMNVCDKIVKIENCRIEE 193
Cdd:COG2274  632 ILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH-RLSTIRLADRIIVLDKGRIVE 689
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
14-171 2.29e-14

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: 68.15  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   14 MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFD-----GNLSGMdyllyiKNV 88
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilylGHLPGL------KPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   89 WNSSQNLE--------HEIEYWE------MADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFF 154
Cdd:TIGR01189  88 LSALENLHfwaaihggAQRTIEDalaavgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
                         170
                  ....*....|....*...
gi 493753820  155 NRITE-IHSQQLIIISSH 171
Cdd:TIGR01189 168 GLLRAhLARGGIVLLTTH 185
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
15-188 3.35e-14

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: 66.32  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLF--YYEtiewfdgNLSGmdyllyiknvwnss 92
Cdd:cd03221   15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKigYFE-------QLSG-------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  93 qnleheieywemadyihlpirkyslGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEihSQQLIIISSHY 172
Cdd:cd03221   74 -------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHD 126
                        170
                 ....*....|....*.
gi 493753820 173 KEELMNVCDKIVKIEN 188
Cdd:cd03221  127 RYFLDQVATKIIELED 142
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
16-195 3.48e-14

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: 68.23  E-value: 3.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG-NLSGMD-------------- 80
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL-------------FDGeDITGLPpheiarlgigrtfq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  81 -----------------YLLYIKNVWNSSQNLEHEIEYWE----------MADYIHLPIRKYSLGMKQRLLIAMYFMSQA 133
Cdd:cd03219   83 iprlfpeltvlenvmvaAQARTGSGLLLARARREEREAREraeellervgLADLADRPAGELSYGQQRRLEIARALATDP 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820 134 ECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIV------KIENCRIEEVQ 195
Cdd:cd03219  163 KLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTvldqgrVIAEGTPDEVR 231
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
15-188 5.29e-14

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: 66.83  E-value: 5.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDGnlsgmdyllyiKNVWNSSQN 94
Cdd:cd03229   15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------LIDG-----------EDLTDLEDE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 LEHEIEYWEMA--DYI---HLPIRK---YSL--GMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ 164
Cdd:cd03229   71 LPPLRRRIGMVfqDFAlfpHLTVLEniaLGLsgGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
                        170       180
                 ....*....|....*....|....*.
gi 493753820 165 --LIIISSHYKEELMNVCDKIVKIEN 188
Cdd:cd03229  151 giTVVLVTHDLDEAARLADRVVVLRD 176
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-191 2.14e-12

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 64.70  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLfyyeTIEW------FDGNLSGMDYL------ 82
Cdd:COG0488   13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL----RIGYlpqeppLDDDLTVLDTVldgdae 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 ----------LYIKNVWNSS-----QNLEHEIEY---WEM--------------ADYIHLPIRKYSLGMKQRLLIAMYFM 130
Cdd:COG0488   89 lraleaeleeLEAKLAEPDEdlerlAELQEEFEAlggWEAearaeeilsglgfpEEDLDRPVSELSGGWRRRVALARALL 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493753820 131 SQAECWLMDEITNGLDeyyrtkffnriteIHSQQ------------LIIIsSHYKEELMNVCDKIVKIENCRI 191
Cdd:COG0488  169 SEPDLLLLDEPTNHLD-------------LESIEwleeflknypgtVLVV-SHDRYFLDRVATRILELDRGKL 227
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
2-187 2.81e-12

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 63.75  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTR--EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA---------PSSLFYY---- 66
Cdd:PRK15056   7 IVVNDVTVTWRngHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalQKNLVAYvpqs 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  67 ETIEW----------FDGNLSGMDYLLYIKNvwNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECW 136
Cdd:PRK15056  87 EEVDWsfpvlvedvvMMGRYGHMGWLRRAKK--RDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493753820 137 LMDEITNGLDEYYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIE 187
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVK 216
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
13-171 3.23e-12

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: 62.51  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  13 EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEW-----FDGNLSGMDYLLYI-K 86
Cdd:cd03231   13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIargllYLGHAPGIKTTLSVlE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  87 NV--W---NSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEiH 161
Cdd:cd03231   93 NLrfWhadHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-H 171
                        170
                 ....*....|..
gi 493753820 162 SQQ--LIIISSH 171
Cdd:cd03231  172 CARggMVVLTTH 183
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
15-193 4.50e-12

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: 63.77  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLIsvnsgkiiaPSSLFYYETIEWFDGNLSGMDYLLYIKNVWNSSQN 94
Cdd:COG1123   21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL---------PHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 ---------LEHEIEY----------------WEMADYIHLP--IRKY----SLGMKQRLLIAMYFMSQAECWLMDEITN 143
Cdd:COG1123   92 pmtqlnpvtVGDQIAEalenlglsraeararvLELLEAVGLErrLDRYphqlSGGQRQRVAIAMALALDPDLLIADEPTT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493753820 144 GLDEYYRTKFFNRITEIHSQQ--LIIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:COG1123  172 ALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-193 5.80e-12

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 63.55  E-value: 5.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLfyyeTIEWFDGNLSGMDyllyiknvwnSSQN 94
Cdd:COG0488  330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----KIGYFDQHQEELD----------PDKT 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  95 LEHEI-EYWEMADYIHL----------------PIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDeyyrtkffnri 157
Cdd:COG0488  396 VLDELrDGAPGGTEQEVrgylgrflfsgddafkPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----------- 464
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493753820 158 teIHSQQL-----------IIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:COG0488  465 --IETLEAleealddfpgtVLLVSHDRYFLDRVATRILEFEDGGVRE 509
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
1-171 1.62e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 60.27  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI---------IAPSSLFYYETIEW 71
Cdd:PRK13541   1 MLSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninnIAKPYCTYIGHNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDGNLSGMDYLLYIKNVWNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRT 151
Cdd:PRK13541  81 LKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
                        170       180
                 ....*....|....*....|.
gi 493753820 152 KFFNRIT-EIHSQQLIIISSH 171
Cdd:PRK13541 161 LLNNLIVmKANSGGIVLLSSH 181
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
13-176 1.63e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 60.35  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  13 EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII-----APSSLFYYETIEWFDGNLSGMDYLLYIK- 86
Cdd:PRK13540  14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsIKKDLCTYQKQLCFVGHRSGINPYLTLRe 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  87 ----NVWNSSQNLEHE--IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEi 160
Cdd:PRK13540  94 nclyDIHFSPGAVGITelCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE- 172
                        170
                 ....*....|....*...
gi 493753820 161 HSQQ--LIIISSHYKEEL 176
Cdd:PRK13540 173 HRAKggAVLLTSHQDLPL 190
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
15-191 1.82e-11

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: 61.04  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapssLFYYETIEWFDGNL------SGM---DYLL-- 83
Cdd:cd03256   16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTDINKLKGKALrqlrrqIGMifqQFNLie 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  84 ---YIKNV----------WNSSQNLEHEIEYWE---------MADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEI 141
Cdd:cd03256   92 rlsVLENVlsgrlgrrstWRSLFGLFPKEEKQRalaalervgLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493753820 142 TNGLDEYYRTKFFNRITEIHSQQ--LIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03256  172 VASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRI 223
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-176 1.93e-11

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: 60.87  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGN---IYGMvaiNGSGKTTLFRAISQLISVNSG--------------------K 56
Cdd:COG1119    3 LLELRNVTVRRGGkTILDDISWTVKPGEhwaILGP---NGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelrkR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  57 I-IAPSSLFyyetiEWFDGNLSGMDYLL-----YIkNVWNSSQNLEHE-----IEYWEMADYIHLPIRKYSLGMKQRLLI 125
Cdd:COG1119   80 IgLVSPALQ-----LRFPRDETVLDVVLsgffdSI-GLYREPTDEQRErarelLELLGLAHLADRPFGTLSQGEQRRVLI 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493753820 126 AMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL--IIISSHYKEEL 176
Cdd:COG1119  154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEI 206
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
15-193 2.30e-11

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 61.39  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------APSSLFYYETIEWFDgNLSgMDY---- 81
Cdd:PRK13536  56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparARLARARIGVVPQFD-NLD-LEFtvre 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  82 --LLYIKNVWNSSQNLEHEI----EYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFN 155
Cdd:PRK13536 134 nlLVFGRYFGMSTREIEAVIpsllEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493753820 156 RITEIHSQ-QLIIISSHYKEELMNVCDKIVKIEN-CRIEE 193
Cdd:PRK13536 214 RLRSLLARgKTILLTTHFMEEAERLCDRLCVLEAgRKIAE 253
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
15-169 2.59e-11

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: 60.21  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------------------------APSSLFYYE 67
Cdd:cd03257   20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrkirrkeiqmvfqdPMSSLNPRM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 TIEWfdgnlSGMDYLLYIKNVWNSSQNLEHEIEYWEMadyIHLP---IRKY----SLGMKQRLLIAMYFMSQAECWLMDE 140
Cdd:cd03257  100 TIGE-----QIAEPLRIHGKLSKKEARKEAVLLLLVG---VGLPeevLNRYphelSGGQRQRVAIARALALNPKLLIADE 171
                        170       180       190
                 ....*....|....*....|....*....|..
gi 493753820 141 ITNGLDEYYRTKFFNRITEIHSQQ---LIIIS 169
Cdd:cd03257  172 PTSALDVSVQAQILDLLKKLQEELgltLLFIT 203
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
16-184 3.60e-11

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: 60.05  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG-NLSGM--------------- 79
Cdd:COG0411   20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI-------------LFDGrDITGLpphriarlgiartfq 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 ---------------------------DYLLYIKNVWNSSQNLEHE----IEYWEMADYIHLPIRKYSLGMKQRLLIAMY 128
Cdd:COG0411   87 nprlfpeltvlenvlvaaharlgrgllAALLRLPRARREEREARERaeelLERVGLADRADEPAGNLSYGQQRRLEIARA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820 129 FMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ---LIIIsSHYKEELMNVCDKIV 184
Cdd:COG0411  167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgitILLI-EHDMDLVMGLADRIV 224
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
13-183 9.61e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 59.25  E-value: 9.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  13 EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYY----------ETIEWFDGNLSGMDYL 82
Cdd:PRK13638  14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgllalrqQVATVFQDPEQQIFYT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNVWNSSQNL---EHEI-----EYWEMAD---YIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRT 151
Cdd:PRK13638  94 DIDSDIAFSLRNLgvpEAEItrrvdEALTLVDaqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
                        170       180       190
                 ....*....|....*....|....*....|...
gi 493753820 152 KFFNRITEIHSQ-QLIIISSHYKEELMNVCDKI 183
Cdd:PRK13638 174 QMIAIIRRIVAQgNHVIISSHDIDLIYEISDAV 206
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
15-194 1.30e-10

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: 58.30  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG-NLSGM------------DY 81
Cdd:cd03259   15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-------------LIDGrDVTGVpperrnigmvfqDY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  82 LLY-----IKNVW-----------NSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGL 145
Cdd:cd03259   82 ALFphltvAENIAfglklrgvpkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493753820 146 DEYYRTKFFNRITEIHSQQLI--IISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03259  162 DAKLREELREELKELQRELGIttIYVTHDQEEALALADRIAVMNEGRIVQV 212
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-190 1.33e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 59.05  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------APSSLFYYETIEW 71
Cdd:PRK13537   8 IDFRNVEKRYGDkLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrARHARQRVGVVPQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDgNLSGmDY------LLYIKNVWNSSQNLEHEI----EYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEI 141
Cdd:PRK13537  88 FD-NLDP-DFtvrenlLVFGRYFGLSAAAARALVppllEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493753820 142 TNGLDEYYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIENCR 190
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLCDRLCVIEEGR 215
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
13-190 3.03e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 57.19  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  13 EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII----APSSLFYYETIEW------FDGNLSGMDYL 82
Cdd:PRK13539  15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggDIDDPDVAEACHYlghrnaMKPALTVAENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNVWNSSQNLEHE-IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEiH 161
Cdd:PRK13539  95 EFWAAFLGGEELDIAAaLEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-H 173
                        170       180       190
                 ....*....|....*....|....*....|.
gi 493753820 162 SQQ--LIIISSHYKEELMNVcdKIVKIENCR 190
Cdd:PRK13539 174 LAQggIVIAATHIPLGLPGA--RELDLGPFA 202
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
7-169 3.41e-10

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: 58.38  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   7 VRLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG----NLSGMDYL 82
Cdd:COG1123  272 VRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL-------------FDGkdltKLSRRSLR 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNV----------WNSSQNLEHEIEYW-----------------EMADYIHLP---IRKY----SLGMKQRLLIAMY 128
Cdd:COG1123  339 ELRRRVqmvfqdpyssLNPRMTVGDIIAEPlrlhgllsraerrervaELLERVGLPpdlADRYphelSGGQRQRVAIARA 418
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493753820 129 FMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ---LIIIS 169
Cdd:COG1123  419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltYLFIS 462
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
15-194 5.53e-10

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: 56.42  E-value: 5.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGkiiAPSSlfyyETIEWFDGNLSGMD-------------- 80
Cdd:cd03260   15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---APDE----GEVLLDGKDIYDLDvdvlelrrrvgmvf 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  81 ---------------YLLYIKNVWNSSQnlEHEIEYW---------EMADyiHLPIRKYSLGMKQRLLIAMYFMSQAECW 136
Cdd:cd03260   88 qkpnpfpgsiydnvaYGLRLHGIKLKEE--LDERVEEalrkaalwdEVKD--RLHALGLSGGQQQRLCLARALANEPEVL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493753820 137 LMDEITNGLDEYYRTKFFNRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03260  164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
16-193 5.78e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 57.59  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSGMDYL----LYIKNVWNS 91
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIelkgLMMGLTKEK 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  92 SQNLEHE-IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ-QLIIIS 169
Cdd:PRK13545 120 IKEIIPEiIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFI 199
                        170       180
                 ....*....|....*....|....
gi 493753820 170 SHYKEELMNVCDKIVKIENCRIEE 193
Cdd:PRK13545 200 SHSLSQVKSFCTKALWLHYGQVKE 223
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
15-193 5.90e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 56.98  E-value: 5.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYY-ETIEWFDG------------------N 75
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgKDIFQIDAiklrkevgmvfqqpnpfpH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  76 LSGMDYLLY------IKNVWNSSQNLEH---EIEYW-EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGL 145
Cdd:PRK14246 105 LSIYDNIAYplkshgIKEKREIKKIVEEclrKVGLWkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493753820 146 DEYYRTKFFNRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-195 1.14e-09

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 55.82  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRlKTREM------ILKDIDFTFEKGniyGMVAI---NGSGKTTLFRAISQLISVNSGKIiapsslfyyetieW 71
Cdd:COG1136    4 LLELRNLT-KSYGTgegevtALRGVSLSIEAG---EFVAIvgpSGSGKSTLLNILGGLDRPTSGEV-------------L 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDG-NLSGMD-------------------YL-------------LYIKNVwnSSQNLEHEIEYW----EMADYIHLPIRK 114
Cdd:COG1136   67 IDGqDISSLSerelarlrrrhigfvfqffNLlpeltalenvalpLLLAGV--SRKERRERARELlervGLGDRLDHRPSQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820 115 YSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ--QLIIISSHyKEELMNVCDKIVKIENCRIE 192
Cdd:COG1136  145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTH-DPELAARADRVIRLRDGRIV 223

                 ...
gi 493753820 193 EVQ 195
Cdd:COG1136  224 SDE 226
cbiO PRK13637
energy-coupling factor transporter ATPase;
16-192 2.26e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 55.44  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA-------------------------PSSLFYYETIE 70
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklsdirkkvglvfqyPEYQLFEETIE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  71 wfdgnlsgmdyllyiKNVWNSSQNL---EHEIE--YWEMADYIHLPIRKY--------SLGMKQRLLIAMYFMSQAECWL 137
Cdd:PRK13637 103 ---------------KDIAFGPINLglsEEEIEnrVKRAMNIVGLDYEDYkdkspfelSGGQKRRVAIAGVVAMEPKILI 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493753820 138 MDEITNGLDEYYRTKFFNRITEIHSQ--QLIIISSHYKEELMNVCDKIVKIENCRIE 192
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEynMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
19-191 2.86e-09

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: 55.79  E-value: 2.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    19 IDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSS---------------------LFYYETIEwfdgnls 77
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqslgmcpqhniLFHHLTVA------- 1021
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    78 gmDYLLYIKNVWNSSQNlEHEIEYWEMADYIHL------PIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRT 151
Cdd:TIGR01257 1022 --EHILFYAQLKGRSWE-EAQLEMEAMLEDTGLhhkrneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 493753820   152 KFFNRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-146 3.64e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 54.73  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLK-TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSL--------FYYE---- 67
Cdd:PRK09544   4 LVSLENVSVSfGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLrigyvpqkLYLDttlp 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 -TIEWF---DGNLSGMDYLLYIKNVwnssqNLEHEIEYwemadyihlPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITN 143
Cdd:PRK09544  84 lTVNRFlrlRPGTKKEDILPALKRV-----QAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149

                 ...
gi 493753820 144 GLD 146
Cdd:PRK09544 150 GVD 152
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-184 3.79e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 54.71  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLK-------TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewfd 73
Cdd:PRK13633   4 MIKCKNVSYKyesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY--------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  74 gnLSGMDYLLyIKNVWN---------------------------SSQNL-----------EHEIEYWEMADYIHLPIRKY 115
Cdd:PRK13633  69 --VDGLDTSD-EENLWDirnkagmvfqnpdnqivativeedvafGPENLgippeeirervDESLKKVGMYEYRRHAPHLL 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493753820 116 SLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSHYKEELMNVcDKIV 184
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEA-DRII 215
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
12-194 7.19e-09

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 54.32  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  12 REMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI--------------------IAPSSLFYYETIew 71
Cdd:PRK10851  14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrlhardrkvgfvFQHYALFRHMTV-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDGNLSGMDYLLYIKNVwNSSQNLEHEIEYWEMADYIHLPIR---KYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEY 148
Cdd:PRK10851  92 FDNIAFGLTVLPRRERP-NAAAIKAKVTQLLEMVQLAHLADRypaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493753820 149 YRTKFFNRITEIHsQQLIIIS---SHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:PRK10851 171 VRKELRRWLRQLH-EELKFTSvfvTHDQEEAMEVADRVVVMSQGNIEQA 218
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
26-183 7.62e-09

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: 54.63  E-value: 7.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    26 GNIYGMVAINGSGKTTLFRAISQLISVNSGK-IIAPSSLF-----------YYETIEWFDGNLSGMDYL-LYIKNVWNSS 92
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILtnisdvhqnmgYCPQFDAIDDLLTGREHLyLYARLRGVPA 2044
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    93 QNLEH----EIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITE-IHSQQLII 167
Cdd:TIGR01257 2045 EEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVV 2124
                          170
                   ....*....|....*.
gi 493753820   168 ISSHYKEELMNVCDKI 183
Cdd:TIGR01257 2125 LTSHSMEECEALCTRL 2140
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-193 9.14e-09

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: 53.35  E-value: 9.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRlKT------REMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetIEWFD- 73
Cdd:cd03258    1 MIELKNVS-KVfgdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL----------VDGTDl 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  74 GNLS-----------GMDY----LLYIKNVWnssQNLEH--EIEYWEMA-------DYIHL-----PIRKY----SLGMK 120
Cdd:cd03258   70 TLLSgkelrkarrriGMIFqhfnLLSSRTVF---ENVALplEIAGVPKAeieervlELLELvgledKADAYpaqlSGGQK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820 121 QRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHsQQL---IIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:cd03258  147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDIN-RELgltIVLITHEMEVVKRICDRVAVMEKGEVVE 221
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
12-184 1.57e-08

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: 53.44  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   12 REMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQL-------ISVNSGKIIAPSSLFYYETIEW-------FDGNLS 77
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvdptegsIAVNGVPLADADADSWRDQIAWvpqhpflFAGTIA 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   78 GmDYLLYIKNVwnssqnLEHEIE-------YWEMA----DYIHLPI----RKYSLGMKQRLLIAMYFMSQAECWLMDEIT 142
Cdd:TIGR02857 414 E-NIRLARPDA------SDAEIRealeragLDEFVaalpQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 493753820  143 NGLDEYYRTKFFNRITEIHSQQLIIISSHyKEELMNVCDKIV 184
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGRTVLLVTH-RLALAALADRIV 527
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
15-194 1.82e-08

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: 52.26  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDGNLS----------GM---DY 81
Cdd:cd03301   15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-------------YIGGRDVtdlppkdrdiAMvfqNY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  82 LLYI-KNVWnssQNLEH----------EI-----EYWEMADYIHLPIRK---YSLGMKQRLLIAMYFMSQAECWLMDEIT 142
Cdd:cd03301   82 ALYPhMTVY---DNIAFglklrkvpkdEIdervrEVAELLQIEHLLDRKpkqLSGGQRQRVALGRAIVREPKVFLMDEPL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493753820 143 NGLDEYYRTKFFNRITEIHsQQL---IIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03301  159 SNLDAKLRVQMRAELKRLQ-QRLgttTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
15-193 2.06e-08

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: 52.12  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfYYETIEWFDGNLS---------GM------ 79
Cdd:cd03261   15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-------LIDGEDISGLSEAelyrlrrrmGMlfqsga 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 --DYLLYIKNV----WNSSQNLEHEI-----EYWEMA---DYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGL 145
Cdd:cd03261   88 lfDSLTVFENVafplREHTRLSEEEIreivlEKLEAVglrGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493753820 146 DEYYRTKFFNRITEIH-SQQL-IIISSHYKEELMNVCDKIVKIENCRIEE 193
Cdd:cd03261  168 DPIASGVIDDLIRSLKkELGLtSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
16-194 2.37e-08

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 52.73  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI---------IAPSSL--FYYETIEWFDGNLSGMDYLLY 84
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakISDAELreVRRKKIAMVFQSFALMPHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  85 IKNVW--------NSSQNLEHEIEYWE---MADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKF 153
Cdd:PRK10070 124 LDNTAfgmelagiNAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493753820 154 FNRITEIHS--QQLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:PRK10070 204 QDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
15-58 3.50e-08

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: 51.28  E-value: 3.50e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:cd03224   15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR 58
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
15-194 4.37e-08

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: 51.47  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapssLFYYETIEWFDGNLSGM-----DYLLYIK-NV 88
Cdd:cd03300   15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-----LLDGKDITNLPPHKRPVntvfqNYALFPHlTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  89 WNS---------------SQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKF 153
Cdd:cd03300   90 FENiafglrlkklpkaeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493753820 154 FNRITEIHsQQL---IIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03300  170 QLELKRLQ-KELgitFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1-184 4.84e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 51.25  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE-MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII--------------------- 58
Cdd:PRK10247   7 LLQLQNVGYLAGDaKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfegedistlkpeiyrqqvsyc 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  59 APSSLFYYETIewfdgnlsgMDYLLY---IKNVWNSSQNLEHEIEYWEMADYI-HLPIRKYSLGMKQR--LLIAMYFMSQ 132
Cdd:PRK10247  87 AQTPTLFGDTV---------YDNLIFpwqIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRisLIRNLQFMPK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 133 AecWLMDEITNGLDEYYRTKFFNRITEIHSQQLIII--SSHYKEELmNVCDKIV 184
Cdd:PRK10247 158 V--LLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEI-NHADKVI 208
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
15-194 7.32e-08

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 51.18  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI---------IAPS---------SLFYYETIEWFDgNL 76
Cdd:PRK11000  18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndVPPAergvgmvfqSYALYPHLSVAE-NM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  77 S-GMDYLLYIKNVWNssQNLEHEIEYWEMAdyiHLPIRK---YSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTK 152
Cdd:PRK11000  97 SfGLKLAGAKKEEIN--QRVNQVAEVLQLA---HLLDRKpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493753820 153 FFNRITEIHsQQL---IIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:PRK11000 172 MRIEISRLH-KRLgrtMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
15-194 1.10e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 50.30  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLIS------VNSGKIIAPSSLFYYETIEW-------FD-----GNL 76
Cdd:PRK14247  18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIELrrrvqmvFQipnpiPNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  77 SGMDYL---LYIKNVWNSSQNLEHEIEY-------W-EMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGL 145
Cdd:PRK14247  98 SIFENValgLKLNRLVKSKKELQERVRWalekaqlWdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493753820 146 DEYYRTKFFNRITEIHSQQLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
15-146 1.46e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 50.61  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI----IAPSSL-----------FYYETIEWFD------ 73
Cdd:PRK09536  18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagDDVEALsaraasrrvasVPQDTSLSFEfdvrqv 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  74 ---------GNLSGMDYllyiknvwNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNG 144
Cdd:PRK09536  98 vemgrtphrSRFDTWTE--------TDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169

                 ..
gi 493753820 145 LD 146
Cdd:PRK09536 170 LD 171
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
15-172 1.73e-07

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 49.57  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIApsslfyyeTIEW--FDGNLSGMDYLLYIKNVwNSS 92
Cdd:COG2401   45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV--------DVPDnqFGREASLIDAIGRKGDF-KDA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  93 QNLEHEIEYWEMADYIHlPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEY--YRTKF-FNRITEIHSQQLIIIS 169
Cdd:COG2401  116 VELLNAVGLSDAVLWLR-RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtaKRVARnLQKLARRAGITLVVAT 194

                 ...
gi 493753820 170 SHY 172
Cdd:COG2401  195 HHY 197
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
13-171 2.02e-07

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 49.46  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  13 EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI--------IAPSSLF--YYETIEWFDGNLSGMDYL 82
Cdd:PRK13543  24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktatRGDRSRFmaYLGHLPGLKADLSTLENL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNV--WNSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTkFFNRI--T 158
Cdd:PRK13543 104 HFLCGLhgRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT-LVNRMisA 182
                        170
                 ....*....|...
gi 493753820 159 EIHSQQLIIISSH 171
Cdd:PRK13543 183 HLRGGGAALVTTH 195
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
8-58 2.63e-07

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: 49.08  E-value: 2.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493753820   8 RLKTREmILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:cd03218    9 RYGKRK-VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL 58
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
14-146 3.45e-07

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: 49.55  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   14 MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSS--LFYYE-TIEWFDGNlsgmdyllyiKNVWn 90
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvkLAYVDqSRDALDPN----------KTVW- 404
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820   91 ssqnleHEIEywEMADYIHL-----PIRKY------------------SLGMKQRLLIAMYFMSQAECWLMDEITNGLD 146
Cdd:TIGR03719 405 ------EEIS--GGLDIIKLgkreiPSRAYvgrfnfkgsdqqkkvgqlSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-195 3.46e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQV--RLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetieWFDGNLSG 78
Cdd:COG2884    1 MIRFENVskRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL------------VNGQDLSR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  79 M-----------------DY-LLYIKNVWnssQNL----------EHEIEYW--------EMADYIHLPIRKYSLGMKQR 122
Cdd:COG2884   69 LkrreipylrrrigvvfqDFrLLPDRTVY---ENValplrvtgksRKEIRRRvrevldlvGLSDKAKALPHELSGGEQQR 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493753820 123 LLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYkEELMNVCDK-IVKIENCRIEEVQ 195
Cdd:COG2884  146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTtVLIATHD-LELVDRMPKrVLELEDGRLVRDE 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
6-192 3.55e-07

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: 49.34  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    6 QVRLKTREMilkDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfYYETIEWFDG----------- 74
Cdd:TIGR02142   6 SKRLGDFSL---DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-------VLNGRTLFDSrkgiflppekr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   75 -------------NLSGMDYLLY-IKNVWNSSQNLEHEiEYWEMADYIHL---PIRKYSLGMKQRLLIAMYFMSQAECWL 137
Cdd:TIGR02142  76 rigyvfqearlfpHLSVRGNLRYgMKRARPSERRISFE-RVIELLGIGHLlgrLPGRLSGGEKQRVAIGRALLSSPRLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 493753820  138 MDEITNGLDEYYRTK---FFNRITEiHSQQLIIISSHYKEELMNVCDKIVKIENCRIE 192
Cdd:TIGR02142 155 MDEPLAALDDPRKYEilpYLERLHA-EFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
cbiO PRK13644
energy-coupling factor transporter ATPase;
16-191 4.49e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 48.83  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA-------PSSL--------FYYETIE-WFDGNLSGM 79
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgdFSKLqgirklvgIVFQNPEtQFVGRTVEE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 DYLLYIKNVW----NSSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFN 155
Cdd:PRK13644  98 DLAFGPENLClppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493753820 156 RITEIHSQ-QLIIISSHYKEELmNVCDKIVKIENCRI 191
Cdd:PRK13644 178 RIKKLHEKgKTIVYITHNLEEL-HDADRIIVMDRGKI 213
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
2-146 4.81e-07

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: 48.42  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLI---SVNSGKII---APSS--LFYYET--IEW 71
Cdd:cd03234    9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILfngQPRKpdQFQKCVayVRQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDGNLSGM---DYLLYIKN----VWNSSQNLEHEIEYWEMADYIHLPIRKY-----SLGMKQRLLIAMYFMSQAECWLMD 139
Cdd:cd03234   89 DDILLPGLtvrETLTYTAIlrlpRKSSDAIRKKRVEDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILD 168

                 ....*..
gi 493753820 140 EITNGLD 146
Cdd:cd03234  169 EPTSGLD 175
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-58 4.82e-07

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 48.92  E-value: 4.82e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493753820   1 MITLNQVRlKT------REMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:COG1135    1 MIELENLS-KTfptkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL 63
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
15-146 5.41e-07

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: 47.91  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG--------NLS------GM- 79
Cdd:cd03262   15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII-------------IDGlkltddkkNINelrqkvGMv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 --DYLLY-----IKNV---------WNSSQNLEHEIEYWE---MADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDE 140
Cdd:cd03262   82 fqQFNLFphltvLENItlapikvkgMSKAEAEERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161

                 ....*.
gi 493753820 141 ITNGLD 146
Cdd:cd03262  162 PTSALD 167
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
2-194 5.48e-07

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: 48.10  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------APS----------- 61
Cdd:cd03299    1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEkrdisyvpqny 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  62 SLF----YYETIEWfdgnlsGMdyllyiKNVWNSSQNLEHEI-EYWEMADYIHLPIRK---YSLGMKQRLLIAMYFMSQA 133
Cdd:cd03299   81 ALFphmtVYKNIAY------GL------KKRKVDKKEIERKVlEIAEMLGIDHLLNRKpetLSGGEQQRVAIARALVVNP 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493753820 134 ECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03299  149 KILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
15-80 5.85e-07

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: 48.05  E-value: 5.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG-NLSGMD 80
Cdd:COG1127   20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI-------------LVDGqDITGLS 73
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
2-147 7.92e-07

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: 46.76  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTRE--MILKDIDFTFEKGN---IYGMvaiNGSGKTTLFRAISQLISVNSGKIIAPSS--LFY-----YETi 69
Cdd:cd03223    1 IELENLSLATPDgrVLLKDLSFEIKPGDrllITGP---SGTGKSSLFRALAGLWPWGSGRIGMPEGedLLFlpqrpYLP- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493753820  70 ewfDGNLsgMDYLLYIknvwnssqnleheieyWEmadyihlpiRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDE 147
Cdd:cd03223   77 ---LGTL--REQLIYP----------------WD---------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
2-193 9.59e-07

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: 47.48  E-value: 9.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTR---EMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWFDGNLSG 78
Cdd:cd03252    1 ITFEHVRFRYKpdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  79 M--DYLLYIKNV------WNSSQNLEHEIEYWEMADyIHLPIRK---------------YSLGMKQRLLIAMYFMSQAEC 135
Cdd:cd03252   81 VlqENVLFNRSIrdnialADPGMSMERVIEAAKLAG-AHDFISElpegydtivgeqgagLSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493753820 136 WLMDEITNGLDEYYRTKFFNRITEIHSQQLIIISSHYKEELMNVcDKIVKIENCRIEE 193
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVE 216
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-57 9.91e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 47.46  E-value: 9.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493753820   1 MITLNQ--VRLKTREmILKDIDFTFEKGNiygMVAI---NGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK13548   2 MLEARNlsVRLGGRT-LLDDVSLTLRPGE---VVAIlgpNGAGKSTLLRALSGELSPDSGEV 59
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
11-65 1.05e-06

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: 47.08  E-value: 1.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493753820  11 TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFY 65
Cdd:cd03250   16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAY 70
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
11-191 2.22e-06

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: 45.67  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  11 TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewfdgnLSGMDYllyikNVWN 90
Cdd:cd03246   13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDGADI-----SQWD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  91 SSQNLEH------EIEYWE--MADYIhlpirkYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHS 162
Cdd:cd03246   71 PNELGDHvgylpqDDELFSgsIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA 144
                        170       180
                 ....*....|....*....|....*....
gi 493753820 163 QQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:cd03246  145 AGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
2-193 2.24e-06

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: 45.77  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLK---TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewfdgnLSG 78
Cdd:cd03247    1 LSINNVSFSypeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-----------------LDG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  79 MDYLLYIKNVWNSSQNLEHEIEYWEMADYIHLPIRkYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRIT 158
Cdd:cd03247   64 VPVSDLEKALSSLISVLNQRPYLFDTTLRNNLGRR-FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 159 EIHSQQLIIISSHYKEELMNVcDKIVKIENCRIEE 193
Cdd:cd03247  143 EVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
cbiO PRK13643
energy-coupling factor transporter ATPase;
16-191 2.58e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 46.65  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLI-----SVNSGKIIAPSS---------------LFYYETIEWFDGN 75
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqptegKVTVGDIVVSSTskqkeikpvrkkvgvVFQFPESQLFEET 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  76 LSgMDYLLYIKNVWNSSQNLEH-----------EIEYWEMADYihlpirKYSLGMKQRLLIAMYFMSQAECWLMDEITNG 144
Cdd:PRK13643 102 VL-KDVAFGPQNFGIPKEKAEKiaaeklemvglADEFWEKSPF------ELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493753820 145 LDEYYRTKFFNRITEIH-SQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:PRK13643 175 LDPKARIEMMQLFESIHqSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-194 2.70e-06

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: 46.14  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQV--RLKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI---------------------- 57
Cdd:cd03295    1 IEFENVtkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvelrrkigyv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  58 IAPSSLFYYETIEwfdGNLSGMDYLLYiknvWNSSQNLEHEIEYWEMadyIHLPIRKY--------SLGMKQRLLIAMYF 129
Cdd:cd03295   81 IQQIGLFPHMTVE---ENIALVPKLLK----WPKEKIRERADELLAL---VGLDPAEFadryphelSGGQQQRVGVARAL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493753820 130 MSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ--QLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03295  151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-192 3.17e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 46.26  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLK----TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDGNl 76
Cdd:PRK13650   4 IIEVKNLTFKykedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII-------------IDGD- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  77 sgmdyLLYIKNVWNSS-------QN-----------------LEHE-IEYWEMADYIHLPIR-------------KYSLG 118
Cdd:PRK13650  70 -----LLTEENVWDIRhkigmvfQNpdnqfvgatveddvafgLENKgIPHEEMKERVNEALElvgmqdfkerepaRLSGG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493753820 119 MKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIENCRIE 192
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVE 219
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
15-140 3.34e-06

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 45.89  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII---------APSSLFYYETIEWFDGNLSGMDYLLYI 85
Cdd:NF040729  20 VLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILvngnevtkpGPDRGFVFQNYALFPWMTVKENIEYPM 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820  86 KNVWNSSQNLEHEIEYW-EMAD---YIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDE 140
Cdd:NF040729 100 KQQKMPKQEREKRLNELlEMAQltgKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
15-146 3.44e-06

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 46.16  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapssLFYYETIEWF-DGNLSGMDYLL---------- 83
Cdd:PRK11231  17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-----FLGDKPISMLsSRQLARRLALLpqhhltpegi 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  84 -------YIKNVWNS-----SQNLEHEIEyWEMAD--YIHL---PIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLD 146
Cdd:PRK11231  92 tvrelvaYGRSPWLSlwgrlSAEDNARVN-QAMEQtrINHLadrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
16-191 3.55e-06

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 46.23  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI----IAPsslfYYETIE---------------WFDgnL 76
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgYVP----FKRRKEfarrigvvfgqrsqlWWD--L 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  77 SGMDYLLYIKNVWNSS-----QNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLD----- 146
Cdd:COG4586  112 PAIDSFRLLKAIYRIPdaeykKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvske 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493753820 147 -------EYYRTKffnRITeihsqqlIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:COG4586  192 aireflkEYNRER---GTT-------ILLTSHDMDDIEALCDRVIVIDHGRI 233
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-57 6.45e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 45.54  E-value: 6.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493753820   2 ITLNQVRL--KTREMILKDIDFTFEKGniyGMVAI---NGSGKTTLFRAISQLISVNSGKI 57
Cdd:COG1132  340 IEFENVSFsyPGDRPVLKDISLTIPPG---ETVALvgpSGSGKSTLVNLLLRFYDPTSGRI 397
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
15-193 7.60e-06

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: 44.71  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyeTIEWFDGNLSGM------------DYL 82
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI----------EIDGIDISTIPLedlrssltiipqDPT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYIKNVWNssqNLEHEIEYWEMADYIHLPIRK----YSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRIT 158
Cdd:cd03369   93 LFSGTIRS---NLDPFDEYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 159 EIHSQQLIIISSHYKEELMNvCDKIVKIENCRIEE 193
Cdd:cd03369  170 EEFTNSTILTIAHRLRTIID-YDKILVMDAGEVKE 203
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
15-194 9.35e-06

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: 45.18  E-value: 9.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISV--NSGKII-----APSSLFYY-------------ETIEWFDG 74
Cdd:TIGR03269  15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalCEKCGYVErpskvgepcpvcgGTLEPEEV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   75 NLSGMD------------------YLLY-----IKNVWNSSQNLEHE-----------IEYWEMADYIHLPIRKYSLGMK 120
Cdd:TIGR03269  95 DFWNLSdklrrrirkriaimlqrtFALYgddtvLDNVLEALEEIGYEgkeavgravdlIEMVQLSHRITHIARDLSGGEK 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820  121 QRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITE--IHSQQLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
15-58 1.06e-05

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 44.70  E-value: 1.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 493753820  15 ILKDIDFTFEKGNIygmVAI---NGSGKTTLFRAISQLISVNSGKII 58
Cdd:COG3842   20 ALDDVSLSIEPGEF---VALlgpSGCGKTTLLRMIAGFETPDSGRIL 63
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
16-194 1.19e-05

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: 44.25  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPS--------------------SLFYYETIewFDgN 75
Cdd:cd03296   18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqernvgfvfqhyALFRHMTV--FD-N 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  76 LSgmdYLLYIKNVWNSSQNLEHEIEYWEMADYIHLP--IRKY----SLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYY 149
Cdd:cd03296   95 VA---FGLRVKPRSERPPEAEIRAKVHELLKLVQLDwlADRYpaqlSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493753820 150 RTKFFNRITEIHSQQLI--IISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:cd03296  172 RKELRRWLRRLHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQV 218
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
16-183 2.08e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 44.00  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPS--------SLFYYETIEWFDGNLSGMDYL----- 82
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhKLAAQLGIGIIYQELSVIDELtvlen 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  83 LYI-----KNVW--NSSQNLEHEIEYWEMADYIHLPI------RKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYY 149
Cdd:PRK09700 101 LYIgrhltKKVCgvNIIDWREMRVRAAMMLLRVGLKVdldekvANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 150 RTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKI 183
Cdd:PRK09700 181 VDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRY 215
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
19-186 2.22e-05

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: 44.02  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   19 IDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKiiapsslfYYETI--EWFDGNLSGMD---------------Y 81
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE--------VNVRVgdEWVDMTKPGPDgrgrakryigilhqeY 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   82 LLY-----IKNVwNSSQNLEHEIEYWEMADYIHLP------------IRKY----SLGMKQRLLIAMYFMSQAECWLMDE 140
Cdd:TIGR03269 375 DLYphrtvLDNL-TEAIGLELPDELARMKAVITLKmvgfdeekaeeiLDKYpdelSEGERHRVALAQVLIKEPRIVILDE 453
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820  141 ITNGLDEYYRTKFFNRI--TEIHSQQLIIISSHYKEELMNVCD--------KIVKI 186
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDVCDraalmrdgKIVKI 509
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
15-184 2.39e-05

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: 43.23  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapssLFYYETIEWFDGNLSGM--DYLLY-----IKN 87
Cdd:cd03293   19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-----LVDGEPVTGPGPDRGYVfqQDALLpwltvLDN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  88 V--------WNSSQNLEHEIEYWEM---ADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNR 156
Cdd:cd03293   94 ValglelqgVPKAEARERAEELLELvglSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
                        170       180       190
                 ....*....|....*....|....*....|
gi 493753820 157 ITEI--HSQQLIIISSHYKEELMNVCDKIV 184
Cdd:cd03293  174 LLDIwrETGKTVLLVTHDIDEAVFLADRVV 203
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
16-184 2.50e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 43.68  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapssLFYYETIEWFDGNLS------GM-----DYLLY 84
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-----LFDGKPIDYSRKGLMklresvGMvfqdpDNQLF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  85 IKNVWNS---------------SQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYY 149
Cdd:PRK13636  97 SASVYQDvsfgavnlklpedevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493753820 150 RTKFFNRITEIHSQQ--LIIISSHYKEELMNVCDKIV 184
Cdd:PRK13636 177 VSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVF 213
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
2-58 3.02e-05

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 43.60  E-value: 3.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493753820   2 ITLNQVRlKT--REMILKDIDFTFEKGniyGMVAI---NGSGKTTLFRAISQLISVNSGKII 58
Cdd:COG1118    3 IEVRNIS-KRfgSFTLLDDVSLEIASG---ELVALlgpSGSGKTTLLRIIAGLETPDSGRIV 60
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
17-188 3.39e-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: 42.59  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  17 KDIDFTFEKGnIYGMVAINGSGKTTLFRAIS-----QLISVNSG-----KIIAPSSLFYYETIEWFDGNlsGMDYLLY-- 84
Cdd:cd03240   14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEALKyaltgELPPNSKGgahdpKLIREGEVRAQVKLAFENAN--GKKYTITrs 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  85 ---IKNVWNSSQNleheieywEMADYIHLPIRKYSLGMKQ------RLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFN 155
Cdd:cd03240   91 laiLENVIFCHQG--------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLA 162
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493753820 156 RITEIHSQ----QLIIISSHykEELMNVCDKIVKIEN 188
Cdd:cd03240  163 EIIEERKSqknfQLIVITHD--EELVDAADHIYRVEK 197
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
16-184 3.64e-05

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 43.47  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG--------------------- 74
Cdd:COG1129   20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-------------LLDGepvrfrsprdaqaagiaiihq 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  75 ------NLSGMDyllyikNVWnssqnLEHEIEYWEMADY---------------IHL----PIRKYSLGMKQRLLIAMYF 129
Cdd:COG1129   87 elnlvpNLSVAE------NIF-----LGREPRRGGLIDWramrrrarellarlgLDIdpdtPVGDLSVAQQQLVEIARAL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820 130 MSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQL-IIISSHYKEELMNVCDKIV 184
Cdd:COG1129  156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADRVT 211
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
22-159 3.81e-05

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: 42.78  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  22 TFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYY--ETIEW-FDGNLsgmDYLLY--IKNVWNSSQNLE 96
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkpQYIKAdYEGTV---RDLLSsiTKDFYTHPYFKT 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820  97 HEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR---TKFFNRITE 159
Cdd:cd03237   98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSKVIRRFAE 163
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1-187 3.88e-05

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 43.26  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTR--EMILKDIDFTFEKGniyGMVAI---NGSGKTTLFRAISQLISVNSGKIIAPS---SLF-----YYe 67
Cdd:COG4178  362 ALALEDLTLRTPdgRPLLEDLSLSLKPG---ERLLItgpSGSGKSTLLRAIAGLWPYGSGRIARPAgarVLFlpqrpYL- 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  68 tiewFDGNLsgMDYLLY--IKNVWNSSQ--------NLEH------EIEYWEmadyihlpiRKYSLGMKQRLLIAMYFMS 131
Cdd:COG4178  438 ----PLGTL--REALLYpaTAEAFSDAElrealeavGLGHlaerldEEADWD---------QVLSLGEQQRLAFARLLLH 502
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493753820 132 QAECWLMDEITNGLDEYYRTKFFNRITEiHSQQLIIIS-SHyKEELMNVCDKIVKIE 187
Cdd:COG4178  503 KPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISvGH-RSTLAAFHDRVLELT 557
cbiO PRK13640
energy-coupling factor transporter ATPase;
11-191 5.35e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 42.48  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  11 TREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLI---SVNSGKIIAPSSLFYYETIeW---------------- 71
Cdd:PRK13640  18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTV-Wdirekvgivfqnpdnq 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  72 FDGNLSGMDYLLYIKNVWNSSQNL----EHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDE 147
Cdd:PRK13640  97 FVGATVGDDVAFGLENRAVPRPEMikivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493753820 148 YYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:PRK13640 177 AGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKL 221
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
25-177 5.57e-05

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: 41.59  E-value: 5.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    25 KGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfYYETIEWFDGNLSGMDYLLYIKNVWNSSQnleheieywem 104
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------YIDGEDILEEVLDQLLLIIVGGKKASGSG----------- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   105 adyihlpirkyslGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR-------TKFFNRITEIHSQQLIIISSHYKEELM 177
Cdd:smart00382  64 -------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEallllleELRLLLLLKSEKNLTVILTTNDEKDLG 130
PLN03232 PLN03232
ABC transporter C family member; Provisional
9-193 6.28e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 43.04  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    9 LKTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRA-ISQLISVNSGKIIAPSSLFYYETIEWF------DGNLSGMDY 81
Cdd:PLN03232  626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVPQVSWIfnatvrENILFGSDF 705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   82 llYIKNVWNS--SQNLEHEIEYWEMADYIHLPIR--KYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRI 157
Cdd:PLN03232  706 --ESERYWRAidVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 493753820  158 T--EIHSQQLIIISSHYkeELMNVCDKIVKIENCRIEE 193
Cdd:PLN03232  784 MkdELKGKTRVLVTNQL--HFLPLMDRIILVSEGMIKE 819
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
17-194 6.71e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 42.85  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  17 KDIDFTFEKGNIYGMVAINGSGKTTLFRAI-------SQLISVNsGKIIAPSSlfYYETIE-------------WFDGNL 76
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLfgvdkraGGEIRLN-GKDISPRS--PLDAVKkgmayitesrrdnGFFPNF 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  77 S---GMDYLLYIKNV-WNSSQNLEHEIEYWEMAD-----------YIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEI 141
Cdd:PRK09700 357 SiaqNMAISRSLKDGgYKGAMGLFHEVDEQRTAEnqrellalkchSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493753820 142 TNGLDEYYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIVKIENCRIEEV 194
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-57 6.99e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 42.29  E-value: 6.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTREM---ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK13632   7 MIKVENVSFSYPNSennALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI 66
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
10-193 1.07e-04

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: 41.45  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  10 KTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyyetiewFDG-NLSGMDYLLYIKNV 88
Cdd:cd03251   12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIL-------------IDGhDVRDYTLASLRRQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  89 WNSSQNL-------------------EHEIEYWEMADYIHLPIR---------------KYSLGMKQRLLIAMYFMSQAE 134
Cdd:cd03251   79 GLVSQDVflfndtvaeniaygrpgatREEVEEAARAANAHEFIMelpegydtvigergvKLSGGQRQRIAIARALLKDPP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493753820 135 CWLMDEITNGLD---EYYRTKFFNRITEiHSQQLIIisSHYKEELMNVcDKIVKIENCRIEE 193
Cdd:cd03251  159 ILILDEATSALDtesERLVQAALERLMK-NRTTFVI--AHRLSTIENA-DRIVVLEDGKIVE 216
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
15-188 1.17e-04

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: 41.77  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWF------DGNLSGMDYLLY-IKN 87
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWImpgtikENIIFGVSYDEYrYKS 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  88 VWNSSQnLEHEIEYWEMADYIHLPIRKYSL--GMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRIT--EIHSQ 163
Cdd:cd03291  132 VVKACQ-LEEDITKFPEKDNTVLGEGGITLsgGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVckLMANK 210
                        170       180
                 ....*....|....*....|....*
gi 493753820 164 QLIIISShyKEELMNVCDKIVKIEN 188
Cdd:cd03291  211 TRILVTS--KMEHLKKADKILILHE 233
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
16-193 1.23e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 41.54  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetiewfdgNLSGMdyLLYIKNVWNSS--- 92
Cdd:PRK13635  23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----------------TVGGM--VLSEETVWDVRrqv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  93 ----QN-----------------LE-HEIEYWEMADYIHLPIR-------------KYSLGMKQRLLIAMYFMSQAECWL 137
Cdd:PRK13635  84 gmvfQNpdnqfvgatvqddvafgLEnIGVPREEMVERVDQALRqvgmedflnrephRLSGGQKQRVAIAGVLALQPDIII 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493753820 138 MDEITNGLDEYYRTKFFNRITEIHSQQLI-IIS-SHYKEELMNVcDKIVKIENCRIEE 193
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGItVLSiTHDLDEAAQA-DRVIVMNKGEILE 220
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
15-58 1.25e-04

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 41.23  E-value: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:PRK09493  16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI 59
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
15-184 1.44e-04

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: 41.09  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVN---SGKIIAPSsLFYYETIEWFDGNLsgmdyllyiknVWNS 91
Cdd:cd03233   22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG-IPYKEFAEKYPGEI-----------IYVS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  92 sqnleheieywemADYIHLP-------------------IRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTK 152
Cdd:cd03233   90 -------------EEDVHFPtltvretldfalrckgnefVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493753820 153 FFNRITEI-HSQQLIIISSHYK--EELMNVCDKIV 184
Cdd:cd03233  157 ILKCIRTMaDVLKTTTFVSLYQasDEIYDLFDKVL 191
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
14-57 1.55e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 41.64  E-value: 1.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 493753820  14 MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
15-182 1.85e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 41.03  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA---------------------PSSLFYYETIEWFD 73
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhararrgigylPQEASIFRRLSVYD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  74 gNLSGmdyLLYIKNVWNSSQNLEHEIEYWEMADYIHLPI---RKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR 150
Cdd:PRK10895  98 -NLMA---VLQIRDDLSAEQREDRANELMEEFHIEHLRDsmgQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
                        170       180       190
                 ....*....|....*....|....*....|...
gi 493753820 151 TKFFNRITEIHSQQL-IIISSHYKEELMNVCDK 182
Cdd:PRK10895 174 IDIKRIIEHLRDSGLgVLITDHNVRETLAVCER 206
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
15-188 1.85e-04

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: 41.43  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEWF------DGNLSGMDYLLY-IKN 87
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWImpgtikDNIIFGLSYDEYrYTS 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820    88 VWNSSQnLEHEIEYWEMADYIHLPIRKYSL--GMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNR--ITEIHSQ 163
Cdd:TIGR01271  521 VIKACQ-LEEDIALFPEKDKTVLGEGGITLsgGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESclCKLMSNK 599
                          170       180
                   ....*....|....*....|....*
gi 493753820   164 QLIIISShyKEELMNVCDKIVKIEN 188
Cdd:TIGR01271  600 TRILVTS--KLEHLKKADKILLLHE 622
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
15-46 2.18e-04

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: 40.20  E-value: 2.18e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAI 46
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI 46
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
14-57 2.26e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.19  E-value: 2.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 493753820  14 MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK15439  25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL 68
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
16-80 2.61e-04

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: 40.82  E-value: 2.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISvNSGKIiapsslfyyetieWFDG-NLSGMD 80
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEI-------------RFDGqDLDGLS 353
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
15-184 3.00e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 40.60  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI------IAPSSLFYYETIEWFDGNLSGM--------- 79
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyIGDKKNNHELITNPYSKKIKNFkelrrrvsm 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  80 -----DYLLYI----KNVWNSSQNL-EHEIEYWEMA---------DYIHLPIRKYSL--GMKQRLLIAMYFMSQAECWLM 138
Cdd:PRK13631 121 vfqfpEYQLFKdtieKDIMFGPVALgVKKSEAKKLAkfylnkmglDDSYLERSPFGLsgGQKRRVAIAGILAIQPEILIF 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493753820 139 DEITNGLDEYYRTKFFNRITEIHSQ-QLIIISSHYKEELMNVCDKIV 184
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVI 247
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
16-171 3.02e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 40.45  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIA-------------------------PSSLFYYETIE 70
Cdd:PRK13639  18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikydkksllevrktvgivfqnPDDQLFAPTVE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  71 WfDGNLSGMDYLLYIKNVwnsSQNLEHEIEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYR 150
Cdd:PRK13639  98 E-DVAFGPLNLGLSKEEV---EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
                        170       180
                 ....*....|....*....|..
gi 493753820 151 TKFFNRITEIHSQQL-IIISSH 171
Cdd:PRK13639 174 SQIMKLLYDLNKEGItIIISTH 195
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1-170 3.29e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 40.12  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRLKTRE---MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIE------- 70
Cdd:PRK13648   7 IIVFKNVSFQYQSdasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhig 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  71 --------WFDGNLSGMDYLLYIKNVWNSSQNLEHE----IEYWEMADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLM 138
Cdd:PRK13648  87 ivfqnpdnQFVGSIVKYDVAFGLENHAVPYDEMHRRvseaLKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 493753820 139 DEITNGLDEYYRTKFFNRITEIHSQQLIIISS 170
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIIS 198
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
18-146 6.41e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 39.52  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  18 DIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIapsslfyYETIEWFDGNLSGMD-----YLL-----YIK- 86
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-------YRMRDGQLRDLYALSeaerrRLLrtewgFVHq 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  87 --------------NV--------WNSSQNLEHEIEYW----EM-ADYIHLPIRKYSLGMKQRLLIAMYFMSQAECWLMD 139
Cdd:PRK11701  97 hprdglrmqvsaggNIgerlmavgARHYGDIRATAGDWlervEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176

                 ....*..
gi 493753820 140 EITNGLD 146
Cdd:PRK11701 177 EPTGGLD 183
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
15-74 7.13e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 39.36  E-value: 7.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIiapsslfyyetieWFDG 74
Cdd:PRK11831  22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-------------LFDG 68
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
15-57 9.03e-04

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: 38.75  E-value: 9.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI 60
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
114-191 9.93e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 38.95  E-value: 9.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493753820 114 KYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRI-TEIHSQQLIIISSHYKEELMNVCDKIVKIENCRI 191
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
15-57 1.04e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 38.58  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 493753820  15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK11264  18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI 60
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
109-191 1.31e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 38.94  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820 109 HLPIRKYSLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQ--LIIISSHYKeELMNVCDKIVKI 186
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkgIIIISSEMP-ELLGITDRILVM 464

                 ....*
gi 493753820 187 ENCRI 191
Cdd:PRK10982 465 SNGLV 469
cbiO PRK13646
energy-coupling factor transporter ATPase;
16-57 1.69e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 38.22  E-value: 1.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV 64
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
15-62 1.94e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 38.47  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 493753820   15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSS 62
Cdd:PTZ00265  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS 447
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
16-58 3.01e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 37.70  E-value: 3.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIL 63
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
10-57 3.61e-03

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 37.38  E-value: 3.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 493753820  10 KTREMILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
2-58 3.62e-03

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: 37.09  E-value: 3.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   2 ITLNQVRLKTRE---MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKII 58
Cdd:cd03244    3 IEFKNVSLRYRPnlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL 62
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
116-182 4.85e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 36.68  E-value: 4.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493753820 116 SLGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKFFNRITEIHSQQLIIISSHYKEELMNVCDK 182
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDM 219
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
16-166 5.18e-03

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 36.69  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  16 LKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKIIAPSSLFYYETIEW--------FDGNLSGMDYLLYIKN 87
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYrsqrirmiFQDPSTSLNPRQRISQ 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820  88 VWNSSQNLEHEIEYWEMADYIHLPIRKYSL--------------GMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKF 153
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLlpdhasyyphmlapGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
                        170
                 ....*....|...
gi 493753820 154 FNRITEIHSQQLI 166
Cdd:PRK15112 189 INLMLELQEKQGI 201
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
15-44 6.18e-03

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: 36.84  E-value: 6.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 493753820   15 ILKDIDFTFEKGNIYGMVAINGSGKTTLFR 44
Cdd:TIGR03719  20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLR 49
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-57 7.38e-03

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 36.36  E-value: 7.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493753820   1 MITLNQVRlKTRE---MILKDIDFTFEKGNIYGMVAINGSGKTTLFRAISQLISVNSGKI 57
Cdd:PRK11650   3 GLKLQAVR-KSYDgktQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
ycf16 CHL00131
sulfate ABC transporter protein; Validated
6-69 8.19e-03

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 36.16  E-value: 8.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820   6 QVRLKTREmILKDIDFTFEKGNIYGMVAINGSGKTTLFRAIS--QLISVNSGKIiapssLFYYETI 69
Cdd:CHL00131  14 HASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDI-----LFKGESI 73
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-187 8.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 36.58  E-value: 8.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493753820 117 LGMKQRLLIAMYFMSQAECWLMDEITNGLDEYYRTKffnrITEIHSQQL-----IIISSHyKEELMNVCDKIVKIE 187
Cdd:PRK03918 797 LGLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRK----LVDIMERYLrkipqVIIVSH-DEELKDAADYVIRVS 867
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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